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anti-Human Vimentin Antibodies:
anti-Mouse (Murine) Vimentin Antibodies:
anti-Rat (Rattus) Vimentin Antibodies:
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Human Polyclonal Vimentin Primary Antibody for IHC (p), WB - ABIN3042344
Quan, Du, Hou, Wang, Zhang: Utilization of E-cadherin by monocytes from tumour cells plays key roles in the progression of bone invasion by oral squamous cell carcinoma. in Oncology reports 2017
Show all 86 Pubmed References
Human Monoclonal Vimentin Primary Antibody for IHC (p), WB - ABIN3043673
Zhu, Liu, Li, Liu, Wang, Sun, Xiong, Jiang, Zheng, Hu: Protein tyrosine phosphatase receptor U (PTPRU) is required for glioma growth and motility. in Carcinogenesis 2014
Show all 77 Pubmed References
Human Polyclonal Vimentin Primary Antibody for FACS, IF (cc) - ABIN672786
Liu, Han, Wang, Feng: Down-regulation of Wnt10a affects odontogenesis and proliferation in mesenchymal cells. in Biochemical and biophysical research communications 2013
Show all 51 Pubmed References
Dog (Canine) Polyclonal Vimentin Primary Antibody for ICC, IF - ABIN152563
Johnstone, Mongroo, Rich, Schupp, Bowser, Delemos, Tobias, Liu, Hannigan, Rustgi: Parvin-beta inhibits breast cancer tumorigenicity and promotes CDK9-mediated peroxisome proliferator-activated receptor gamma 1 phosphorylation. in Molecular and cellular biology 2008
Show all 28 Pubmed References
Human Polyclonal Vimentin Primary Antibody for ELISA, ICC - ABIN6269441
Li, Zhang, Sun, Sun, Shi, Liu, Liu: MicroRNA-181a regulates epithelial-mesenchymal transition by targeting PTEN in drug-resistant lung adenocarcinoma cells. in International journal of oncology 2016
Show all 14 Pubmed References
Human Polyclonal Vimentin Primary Antibody for IF, IHC - ABIN6712041
Fang, Wang, Zhang, Qu, Liu, Qian, Zhu, Zhou, Wang: Transcatheter arterial embolization promotes liver tumor metastasis by increasing the population of circulating tumor cells. in OncoTargets and therapy 2013
Show all 10 Pubmed References
Human Monoclonal Vimentin Primary Antibody for ICC, FACS - ABIN335382
Brussee, Smit, Koopman, Wijga, Kerkhof, Corver, Vos, Gerritsen, Grobbee, Brunekreef, Merkus, de Jongste: Interrupter resistance and wheezing phenotypes at 4 years of age. in American journal of respiratory and critical care medicine 2004
Show all 7 Pubmed References
Human Monoclonal Vimentin Primary Antibody for FACS, ICC - ABIN6729369
Cajigas-Du Ross, Martinez, Woods-Burnham, Durán, Roy, Basu, Ramirez, Ortiz-Hernández, Ríos-Colón, Chirshev, Sanchez-Hernandez, Soto, Greco, Boucheix, Chen, Unternaehrer, Wang, Casiano: RNA sequencing reveals upregulation of a transcriptomic program associated with stemness in metastatic prostate cancer cells selected for taxane resistance. in Oncotarget 2018
Show all 6 Pubmed References
Human Monoclonal Vimentin Primary Antibody for ICC, FACS - ABIN335380
Pieper, Schaart, Krimpenfort, Henderik, Moshage, van de Kemp, Ramaekers, Berns, Bloemendal: Transgenic expression of the muscle-specific intermediate filament protein desmin in nonmuscle cells. in The Journal of cell biology 1989
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Chicken Monoclonal Vimentin Primary Antibody for ICC, IHC (fro) - ABIN1042493
Ramaekers, Huysmans, Schaart, Moesker, Vooijs: Tissue distribution of keratin 7 as monitored by a monoclonal antibody. in Experimental cell research 1987
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When beta4 integrin is knocked down there is a loss of vimentin filaments from lamellipodia.
Both at the primary site and metastatic lymph nodes of invasive breast cancer samples, vimentin-positive tumors have worse disease-free and overall survival. E-cadherin and vimentin proteins are colocalized within the same tumor cells in a human breast cancer specimen.
Intestinal type of gastric cancer associated with connective tissue dysplasia is characterized by a high level of expression of galectin-1 and vimentin in the perifocal zone and TGF-beta in the tumor zone.
The high expression of vimentin plays a pivotal role in the development and poor progression of nasopharyngeal carcinoma
VIM gene expression increased within Caco2 cells after cocultivation with Proteus vulgaris. On the other hand, VIM gene expression decreased by half after cocultivation with Pseudomonas aeruginosa and Proteus mirabilis
These data show that vimentin is required for lung adenocarcinoma metastasis by maintaining heterotypic tumor cell-CAF interactions during collective invasion.
this study shows that methylation status of VIM gene changes in breast cancer
vimentin may play an important role in the progression of glioblastoma multiforme
overexpression of the epithelial to mesenchymal transition marker vimentin is associated with poor clinical outcome in older patients with cytogenetically normal acute myeloid leukemia.
Assembly Kinetics of Vimentin Tetramers
The crystal structure of coil 1B of human vimentin reveals how coiled coil dimers may assemble into a high-order filamentous structure.
Therefore, the present study demonstrated that ZEB1 is a potential biomarker of the tumorigenesis and progression of HCC, and it may regulate transcription of the VIM gene.
vimentin and nestin intermediate filaments interact with caveolae central component caveolin-1 (CAV-1) and importantly, restrain the intracellular trafficking of CAV-1 positive vesicles by serving as a physical barrier.
Cell analyses revealed that all major cytoskeleton components were disrupted during pyroptosis and that sensitivity to rupture was calpain-dependent and linked with cleavage of vimentin and loss of intermediate filaments.
extracellular vimentin may play an important role in cancer or trauma-complications by inducing suppression of the adaptive immune response. In a positive sense, the presence of extracellular vimentin may prevent tissue-damage from contributing to the development of autoimmunity.
VIM is downregulated and E-cad is upregulated in T1 stage non-small-cell lung cancer, suggesting that a mesenchymal-epithelial transition may take place in the early-stage of tumor development
aberrant methylation of SOX1 and VIM promoters may be potential biomarkers for noninvasive detection of hepatocellular carcinoma and metastasis
cell surface vimentin was identified as a candidate surface receptor mediating stiffness-dependent adhesion of Listeria monocytogenes to human microvascular endothelial cells.
shape and inner structure of these mutant filaments is significantly altered
Vimentin and Sam68, are identified as bona fide SRMS substrates through in vitro and in vivo assays.
The Group B Streptococcal surface antigen I/II protein, BspC, interacts with host vimentin to promote adherence to brain endothelium and inflammation during the pathogenesis of meningitis.
vimentin resists the stress fiber contractility, as hypothesized, thus indicating the importance of vimentin in regulating cellular stress generation by adherent cells
This study detected a seemingly proliferative first response from ischemia-activated vimentin-induced cardiac endogenous mesenchymal stem cells with spatial enrichment in the early infarction border zone after acute myocardial infarction.
the results show the implication of FAs both in ECs and vascular SMCs in the role of vimentin in arterial stiffening.
mutation of the serine sites phosphorylated in vimentin during mitosis alters intermediate filament protein expression but has no effect on astrocyte morphology or proliferation, and leads to increased neuronal differentiation of neural progenitor cells.
The Listeria monocytogenes virulence factor InlF was found to bind vimentin and was necessary for optimal bacterial colonization of the brain.
MAGE-G1 interacted with fascin 1 or vimentin in P19 cells after a 6-day retinoic acid-induced neuronal differentiation.
Results found that the absence of vimentin impairs spontaneous endothelial differentiation in vitro and have furthering the understanding of the regulators of differentiation.
Results indicate that vimentin orchestrates the healing by controlling fibroblast proliferation, TGF-beta1-Slug signaling, and epithelial-mesenchymal transition (EMT) processing, and all of which in turn govern the required keratinocyte activation.
Protein phosphatase 1 is a key protein serine/threonine phosphatase that controls vimentin Ser-56 dephosphorylation in smooth muscle.
These findings identify vimentin as a positive regulator of stemness in the developing mouse mammary gland and in breast cancer cells.
This study is the first to show that vimentin has an important role in tumor metastasis in vivo in the setting of pre-diabetes and endogenous hyperinsulinemia.
These findings identify two specific sites on vimentin that are phosphorylated by Cadmium.
The expression level of vimentinin liver cirrhotic tissues were significantly higher than that in chronic hepatitis tissues.
both arthritis-susceptible and -resistant mice can generate cellular and humoral immunity to Vim.
vimentin knockout neurons were insensitive to the axonotrophic effects of Clostridium botulinum C3 exoenzyme
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser-56.
findings thus show that the inability to produce GFAP and Vim affects normal retinal physiology and that the effect of IF deficiency on retinal cell survival differs, depending on the underlying pathologic condition
these findings identify a hereto-unappreciated role for serine-38 phosphorylated vimentin as an important determinant of myofibroblast sensitivity to Withaferin A.
Vimentin expression increased after traumatic brain injury and was positively correlated with edema and neurological impairments.
Taken together these findings suggest that reactive oxygen species and vimentin integrate early wound signals to orchestrate the formation of collagen-based projections that guide regenerative growth during efficient wound repair.
Knockdown of filamin A or vimentin in normal cells profoundly suppresses apical extrusion of the neighbouring transformed cells.
Immunocytochemistry for Vimentin detection in nuclei of IVF and NT bovine embryos
These results indicate that the inner mass differentiates dynamically in blastocysts, as reflected by the expression of vimentin; higher vimentin expression may reflect the higher developmental competence of embryos.
an intact vimentin intermediate filament network contributes to the maintenance of the chondrocyte phenotype
Vimentin- like transcript was expressed in both chordocytes and chordoblasts, whereas the elastin- like transcript was uniquely expressed in the chordoblasts lining the notochordal sheath.
This study evaluated the expression pattern of vimentin in testes of mature Arabian stallions and correlated its distribution with grade of seminiferous tubule impairment as indicated by a Johnsen score.
ANXA2 can interact with vimentin and enhance porcine reproductive and respiratory syndrome virus (PRRSV) growth. This contributes to the regulation of PRRSV replication in infected cells and may have implications for the future antiviral strategies.
As the inner cell mass forms the epiblast, SSEA1 is lost and VIMENTIN is lost and re-expressed.
These observations indicate that vimentin serves as a putative receptor for Japanese encephalitis virus in porcine kidney cells.
Interaction of nucleocapsid protein of transmissible gastroenteritis virus with host vimentin is required for virus infection.
protein(s) that associated with RPTPbeta in response to IGF-I and IGFBP-2 in vascular smooth muscle cells
This study demonstrates that maternal VIM, as a genomic protector, is crucial for nuclear reprogramming in porcine cloned embryos.
Vim expression in corneal epithelium is found in a cell population composed of highly motile cells.
These differentially expressed proteins associated with key mechanisms involved in atherosclerosis and signaling mechanisms related with vitamin E.
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.
, vimentin 1
, class-III intermediate microfilament