Objective: To discuss the efficacy and safety of two-incision extracapsular cataract extraction (ECCE) in the treatment of hard-core cataract with corneal endothelial cell density is low. Methods: This study is a retrospective series of case studies. Forty-six patients (47 eyes) with hard-core cataract and corneal endothelial cell density are enrolled in Shandong Eye Hospital from June 2009 to December 2018, including 22 men and 24 women, aged 50 to 74 (63.8 ± 6, 3 years. Preoperative corneal endothelial cell density of less than 1000 cells / mm (2), and cataract nuclear force is equal to or greater than the fourth grade.
According to the method of surgery, patients were divided into single-incision ECCE group (24 eyes) and group ECCE two incisions (23 eyes). Surgical procedures for double-incision group is as follows. First, the pre-tops scleral incision is made. Then the conventional capsulorhexis is done through a transparent 2.6 mm corneal tunnel incision in the temporal or nasal side, after the hydro-dissection is done.
Next, the surgeon cuts a pre-incision in the sclera, lens nucleus delivered, sutured scleral incision and removed the residual cortical material from corneal incision. Finally, foldable intraocular lens implantation, and viscoelastic substance has been removed. The intraoperative conditions and postoperative anterior chamber corneal edema condition monitored. During 6 months of follow-up after surgery, endothelial cell density, visual acuity and astigmatism in the two groups were compared. The χ (2) test was used to compare the data calculation, and t test was used to compare measurement data.
Results: No difference was significant (t = P = group ECCE, which is (827 ± 164) cells / mm (2) and (802 ± 121) cells / mm (2), respectively At 6 months after surgery ,. in two incisions and single-incision group, the density of endothelial cells is (793 ± 147) cells / mm (2) and (706 ± 101) cells / mm (2), respectively, and the difference was statistically significant (t = P
Conclusion: The double-incision ECCE, in which the core is delivered through an incision scleral lenses and other procedures done through a corneal tunnel incision, safe and effective for patients of cataract with hard core and low corneal endothelial cell density
[Efficacy of double-incision extracapsular cataract extraction in the treatment of hard-nucleus cataract with low corneal endothelial cell density].
Endogenous structure ESX-3 secretion system.
ESX secretion system (or Type VII) is a protein export system in mycobacteria and many Gram-positive bacteria that mediate a variety of functions including virulence, conjugation, and regulation of metabolism.
This system translocate folded dimer WXG100-superfamily protein substrates across the cytoplasmic membrane. We report cryo-electron microscopy structure of the system of ESX-3, purified using epitope tag recombineering inserted in the chromosomes of a model organism Mycobacterium smegmatis.
Description: This gene encodes a member of the intermediate filament family. Intermediate filamentents, along with microtubules and actin microfilaments, make up the cytoskeleton. The protein encoded by this gene is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. It is also involved in the immune response, and controls the transport of low-density lipoprotein (LDL)-derived cholesterol from a lysosome to the site of esterification. It functions as an organizer of a number of critical proteins involved in attachment, migration, and cell signaling. Mutations in this gene causes a dominant, pulverulent cataract.
Description: This gene encodes a member of the intermediate filament family. Intermediate filamentents, along with microtubules and actin microfilaments, make up the cytoskeleton. The protein encoded by this gene is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. It is also involved in the immune response, and controls the transport of low-density lipoprotein (LDL)-derived cholesterol from a lysosome to the site of esterification. It functions as an organizer of a number of critical proteins involved in attachment, migration, and cell signaling. Mutations in this gene causes a dominant, pulverulent cataract.
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.
Description: Along with the microfilaments (actins) and microtubules (tubulins), the intermediate filaments represent a third class of well-characterized cytoskeletal elements. The subunits display a tissue-specific pattern of expression. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
Description: Along with the microfilaments (actins) and microtubules (tubulins), the intermediate filaments represent a third class of well-characterized cytoskeletal elements. The subunits display a tissue-specific pattern of expression. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
Description: Along with the microfilaments (actins) and microtubules (tubulins), the intermediate filaments represent a third class of well-characterized cytoskeletal elements. The subunits display a tissue-specific pattern of expression. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
Description: Along with the microfilaments (actins) and microtubules (tubulins), the intermediate filaments represent a third class of well-characterized cytoskeletal elements. The subunits display a tissue-specific pattern of expression. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. It is involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. [UniProt]
Description: The VIM gene was one of many that Gieser and Swaroop (1992) recovered from a subtracted cDNA library for retinal pigment epithelium. The Vimentin gene expresses in human lymphocytes and in Burkitts lymphoma cells and it is secreted by activated macrophages. The gene encoding human protein is located on the short arm of chromosome 10.
Description: Vimentin is also known as HEL113 or CTRCT30 and the gene encodes a member of the intermediate filament family. Intermediate filamentents, along with microtubules and actin microfilaments, make up the cytoskeleton. The protein encoded by this gene is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. It is also involved in the immune response, and controls the transport of low-density lipoprotein (LDL)-derived cholesterol from a lysosome to the site of esterification. It functions as an organizer of a number of critical proteins involved in attachment, migration, and cell signaling. Mutations in this gene causes a dominant, pulverulent cataract.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-Vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-Vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-Vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This antibody specifically reacts with an ~ 58kDa protein identified as Vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin antibody alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for tumor sub-classification. Expression of vimentin, when used in conjunction with keratin antibody, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with vimentin antibody. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity with vimentin antibody is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Vimentin antibody is also useful as a tissue process control reagent.
Description: This antibody specifically reacts with an ~ 58kDa protein identified as Vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin antibody alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for tumor sub-classification. Expression of vimentin, when used in conjunction with keratin antibody, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with vimentin antibody. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity with vimentin antibody is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Vimentin antibody is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This antibody specifically reacts with an ~ 58kDa protein identified as Vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin antibody alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for tumor sub-classification. Expression of vimentin, when used in conjunction with keratin antibody, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with vimentin antibody. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity with vimentin antibody is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Vimentin antibody is also useful as a tissue process control reagent.
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. It is involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. [UniProt]
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. It is involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. [UniProt]
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. It is involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. [UniProt]
Description: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. It is involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. [UniProt]
Description: This mAb reacts with a 58kDa protein identified as vimentin. It reacts with a non-hematopoietic epitope of vimentin and shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin is ubiquitously expressed in mesenchymal cells such as fibroblasts, smooth muscle cells, and endothelium. Antibody against vimentin is useful as part of an antibody panel for differential diagnosis of tumors of unknown origin. Ab-2 does not react with leukocyte common antigen-positive tissues such as lymphomas and leukemias.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It reacts with a non-hematopoietic epitope of vimentin and shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin is ubiquitously expressed in mesenchymal cells such as fibroblasts, smooth muscle cells, and endothelium. Antibody against vimentin is useful as part of an antibody panel for differential diagnosis of tumors of unknown origin. Ab-2 does not react with leukocyte common antigen-positive tissues such as lymphomas and leukemias.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It reacts with a non-hematopoietic epitope of vimentin and shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin is ubiquitously expressed in mesenchymal cells such as fibroblasts, smooth muscle cells, and endothelium. Antibody against vimentin is useful as part of an antibody panel for differential diagnosis of tumors of unknown origin. Ab-2 does not react with leukocyte common antigen-positive tissues such as lymphomas and leukemias.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It reacts with a non-hematopoietic epitope of vimentin and shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Vimentin is ubiquitously expressed in mesenchymal cells such as fibroblasts, smooth muscle cells, and endothelium. Antibody against vimentin is useful as part of an antibody panel for differential diagnosis of tumors of unknown origin. Ab-2 does not react with leukocyte common antigen-positive tissues such as lymphomas and leukemias.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This mAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFPs) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: The VIM gene encodes a type III intermediate filament protein. Intermediate filaments, along with microtubules and actin microfilaments, make up the cytoskeleton. The encoded protein is responsible for maintaining cell shape and integrity of the cytoplasm, and stabilizing cytoskeletal interactions. This protein is involved in neuritogenesis and cholesterol transport and functions as an organizer of a number of other critical proteins involved in cell attachment, migration, and signaling. [RefSeq]
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP's) such as desmin, keratin, neurofilament, and glial fibrillary acid protein.Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: This MAb reacts with a 58kDa protein identified as vimentin. It shows no cross-reaction with other closely related intermediate filament proteins (IFP s) such as desmin, keratin, neurofilament, and glial fibrillary acid protein. Anti-vimentin alone is of limited value as a diagnostic tool; however, when used in panels with other antibodies, it is useful for the sub-classification of a given tumor. Expression of vimentin, when used in conjunction with anti-keratin, is helpful when distinguishing melanomas from undifferentiated carcinomas and large cell lymphomas. All melanomas and Schwannomas react strongly with anti-vimentin. It labels a variety of mesenchymal cells, including melanocytes, lymphocytes, endothelial cells, and fibroblasts. Non-reactivity of anti-vimentin is often considered more useful than its positive reactivity, since there are a few tumors that do not contain vimentin, e.g. hepatoma and seminoma. Anti-vimentin is also useful as a tissue process control reagent.
Description: Available in various conjugation types.
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The structure reveals stacked architecture that extends above and below the membrane in bacteria. ESX-3 protomer complex assembled from a single copy of EccB3, EccC3, and EccE3 and two copies of the proteins EccD3. In the structure, protomers form a stable dimer that is consistent with the assembling into larger oligomers. ESX-3 structure provides a framework for further study of this important bacterial transporter.
![[Efficacy of double-incision extracapsular cataract extraction in the treatment of hard-nucleus cataract with low corneal endothelial cell density].](https://ecceterra.fr/wp-content/uploads/2020/08/photo_2020-08-08_20-02-14-800x600.jpg)
![[Efficacy of double-incision extracapsular cataract extraction in the treatment of hard-nucleus cataract with low corneal endothelial cell density].](https://ecceterra.fr/wp-content/uploads/2020/08/photo_2020-08-08_20-02-14-1024x498.jpg)
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