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V6389

Sigma-Aldrich

Anti-Vimentin antibody, Mouse monoclonal

clone V9, purified from hybridoma cell culture

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Synonym(s):
Anti-Vimentin antibody, Mouse monoclonal
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

V9, monoclonal

form

buffered aqueous solution

mol wt

antigen ~58 kDa

species reactivity

hamster, monkey, dog, horse, bovine, rat, gerbil, chicken, pig, feline, human

packaging

antibody small pack of 25 μL

concentration

~1 mg/mL

technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 25-50 μg/mL using human tissue
microarray: suitable
western blot: 0.2-0.5 μg/mL using human fibroblasts HS-68

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... VIM(7431)
rat ... Vim(81818)

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This Item
SAB4200761V6630SAB4200716
biological source

mouse

biological source

mouse

biological source

mouse

biological source

mouse

antibody form

purified from hybridoma cell culture

antibody form

purified from hybridoma cell culture

antibody form

ascites fluid

antibody form

purified from hybridoma cell culture

species reactivity

hamster, monkey, dog, horse, bovine, rat, gerbil, chicken, pig, feline, human

species reactivity

rat, human, porcine, monkey, bovine, canine, mouse, rabbit, hamster

species reactivity

pig, canine, feline, hamster, rabbit, gerbil, monkey, bovine, chicken, human, horse, rat

species reactivity

mouse, bovine, canine, rat, monkey, human, chicken

Gene Information

human ... VIM(7431)
rat ... Vim(81818)

Gene Information

bovine ... Vim(280955)
dog ... Vim(477991)
hamster ... Vim(100689099)
human ... VIM(7431)
mouse ... Vim(22352)
pig ... Vim(100522394)
rabbit ... Vim(100008924)
rat ... Vim(81818)
rhesus monkey ... Vim(705289)

Gene Information

human ... VIM(7431)
rat ... Vim(81818)

Gene Information

bovine ... Vim(280955)
chicken ... Vim(420519)
dog ... Vim(477991)
human ... VIM(7431)
mouse ... Vim(22352)
rat ... Vim(81818)
rhesus monkey ... Vim(705289)

clone

V9, monoclonal

clone

LN-6, monoclonal

clone

V9, monoclonal

clone

VIM-13.2, monoclonal

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General description

Monoclonal Anti-Vimentin (mouse IgG1 isotype) is derived from the V9 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a mouse immunized with vimentin purified from pig eye lens.
Vimentin is encoded by a single-copy gene mapped to human chromosome 10p13. 53kDa vimentin protein belongs to type III intermediate filament (IF) family and is specifically expressed in normal mesenchymal cells. Vimentin protein with 466 amino acids is characterized with a highly conserved α-helical “rod” domain that is flanked by non-α--helical amino- terminal “head” and carboxy-terminal “tail” domain.

Specificity

The antibody localizes vimentin in fibroblasts, endothelial cells, lymphoid tissue and melanocytes in immunohistochemical staining. It also stains vimentin in sarcomas, lymphomas, and melanomas.

Immunogen

pig eye lens vimentin.

application

Monoclonal Anti-Vimentin antibody produced in mouse has been used in immunohistochemical analysis and western blot assay.
Monoclonal Anti-Vimentin antibody produced in mouse has been used in:
  • immunofluorescence
  • immunohistochemistry
  • immunocytochemistry
  • immunoblotting
  • flow cytometry.

Biochem/physiol Actions

Vimentin plays a vital role in maintaining the structural integrity of the cells. Overexpression of vimentin is observed in prostate cancer, breast cancer, endometrial cancer, central nervous system (CNS) tumors, malignant melanoma and gastrointestinal tumors including pancreatic, colorectal and hepatic cancers. Thus, vimentin can act as a target for developing therapeutics for the treatment of cancer. Vimentin plays a crucial role in the vascular endothelial growth factor receptor-1 (VEGFR-1)-induced activation of the protein kinase G (PKG) 1 signaling pathway, stimulating regression of cardiomyocyte hypertrophy. Vimentin filaments are implicated in various physiological process including migration, maintenance of cell shape and tolerance of mechanical stress of mesenchymal cells. Vimentin interacts with LARP6 (La ribonucleoprotein domain family member 6) and stabilizes type I collagen mRNAs and might play a vital role in the development of tissue fibrosis. Vimentin plays an essential role in the maintenance of lens integrity, therefore, mutation of the vimentin gene causes dominant and pulverulent cataract.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Decellularized Rhesus Monkey Kidney as a Three-Dimensional Scaffold for Renal Tissue Engineering
Nakayama KH, et al.
Tissue Engineering: Part A, 16(7), 2207-2207 (2010)
Multimodal tumor suppression by miR-302 cluster in melanoma and colon cancer
Maadi H, et al.
The International Journal of Biochemistry, 81(1), 121-132 (2016)
Epithelial to mesenchymal transition is increased in patients with COPD and induced by cigarette smoke
Milara J, et al.
Thorax, 68(5), 410420-410420 (2013)
Probing the biophysical properties of primary breast tumor-derived fibroblasts
Alcoser TA, et al.
Cellular and Molecular Bioengineering, 8(1), 76-76 (2015)
Shuping Hou et al.
Journal of bacteriology, 195(5), 951-957 (2012-12-12)
We previously reported that the Chlamydia trachomatis outer membrane complex protein B (OmcB) was partially processed in Chlamydia-infected cells. We have now confirmed that the OmcB processing occurred inside live cells during chlamydial infection and was not due to proteolysis

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