AFfirm™ Vimentin Mouse Monoclonal Antibody - #BF8175
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
CTRCT30; Epididymis luminal protein 113; FLJ36605; HEL113; VIM; VIME_HUMAN; Vimentin;
Immunogens
Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines.
- P08670 VIME_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
PTMs - P08670 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S2 | Phosphorylation | Uniprot | |
T3 | Phosphorylation | Uniprot | |
R4 | Methylation | Uniprot | |
S5 | Phosphorylation | P17252 (PRKCA) | Uniprot |
S7 | O-Glycosylation | Uniprot | |
S7 | Phosphorylation | P17252 (PRKCA) , Q96GD4 (AURKB) , Q02156 (PRKCE) , P17612 (PRKACA) | Uniprot |
S8 | Phosphorylation | P17252 (PRKCA) | Uniprot |
S9 | Phosphorylation | P17252 (PRKCA) | Uniprot |
S10 | Phosphorylation | P17252 (PRKCA) | Uniprot |
Y11 | Phosphorylation | Uniprot | |
R12 | Methylation | Uniprot | |
R13 | Methylation | Uniprot | |
T20 | Phosphorylation | Uniprot | |
S22 | Phosphorylation | Uniprot | |
R23 | Methylation | Uniprot | |
S25 | Phosphorylation | P17252 (PRKCA) , Q96GD4 (AURKB) , P17612 (PRKACA) | Uniprot |
S26 | Phosphorylation | Q13153 (PAK1) , P17252 (PRKCA) , Q13177 (PAK2) | Uniprot |
S27 | Phosphorylation | Uniprot | |
R28 | Methylation | Uniprot | |
S29 | Phosphorylation | Uniprot | |
Y30 | Phosphorylation | Uniprot | |
T32 | Phosphorylation | Uniprot | |
T33 | O-Glycosylation | Uniprot | |
T33 | Phosphorylation | Uniprot | |
S34 | O-Glycosylation | Uniprot | |
S34 | Phosphorylation | P17252 (PRKCA) | Uniprot |
T35 | Phosphorylation | Uniprot | |
R36 | Methylation | Uniprot | |
T37 | Phosphorylation | Uniprot | |
Y38 | Phosphorylation | Uniprot | |
S39 | Phosphorylation | P49137 (MAPKAPK2) , Q13177 (PAK2) , P17612 (PRKACA) , O75116 (ROCK2) , P31749 (AKT1) , Q13153 (PAK1) , Q96GD4 (AURKB) , P17252 (PRKCA) | Uniprot |
S42 | Phosphorylation | P17252 (PRKCA) | Uniprot |
R45 | Methylation | Uniprot | |
S47 | Phosphorylation | P17612 (PRKACA) , Q96GD4 (AURKB) | Uniprot |
T48 | Phosphorylation | Uniprot | |
S49 | Phosphorylation | Uniprot | |
R50 | Methylation | Uniprot | |
S51 | Phosphorylation | Q13177 (PAK2) , Q13153 (PAK1) , P49137 (MAPKAPK2) | Uniprot |
Y53 | Phosphorylation | Uniprot | |
S55 | O-Glycosylation | Uniprot | |
S55 | Phosphorylation | P24941 (CDK2) , P06493 (CDK1) | Uniprot |
S56 | Phosphorylation | P78527 (PRKDC) , P06493 (CDK1) , P49137 (MAPKAPK2) , Q13153 (PAK1) , P24941 (CDK2) , Q00535 (CDK5) | Uniprot |
Y61 | Phosphorylation | Uniprot | |
T63 | Phosphorylation | Uniprot | |
R64 | Methylation | Uniprot | |
S65 | Phosphorylation | Q96GD4 (AURKB) | Uniprot |
S66 | Phosphorylation | Q96GD4 (AURKB) , Q13177 (PAK2) , Q13153 (PAK1) | Uniprot |
R69 | Methylation | Uniprot | |
R71 | Methylation | Uniprot | |
S72 | Phosphorylation | P17612 (PRKACA) , Q96GD4 (AURKB) , Q13464 (ROCK1) , O75116 (ROCK2) | Uniprot |
S73 | Phosphorylation | Q13177 (PAK2) , Q96GD4 (AURKB) , P17612 (PRKACA) , Q13153 (PAK1) | Uniprot |
S83 | Phosphorylation | Q13557 (CAMK2D) , Q9UQM7 (CAMK2A) , P49137 (MAPKAPK2) , P53350 (PLK1) | Uniprot |
S87 | Phosphorylation | Q96GD4 (AURKB) | Uniprot |
K97 | Ubiquitination | Uniprot | |
T99 | Phosphorylation | Uniprot | |
T101 | Phosphorylation | Uniprot | |
K104 | Acetylation | Uniprot | |
K104 | Ubiquitination | Uniprot | |
R113 | Methylation | Uniprot | |
Y117 | Phosphorylation | Uniprot | |
K120 | Acetylation | Uniprot | |
K120 | Methylation | Uniprot | |
K120 | Ubiquitination | Uniprot | |
K129 | Acetylation | Uniprot | |
K129 | Ubiquitination | Uniprot | |
K139 | Acetylation | Uniprot | |
K139 | Ubiquitination | Uniprot | |
K143 | Ubiquitination | Uniprot | |
S144 | Phosphorylation | Uniprot | |
Y150 | Phosphorylation | Uniprot | |
R158 | Methylation | Uniprot | |
K168 | Acetylation | Uniprot | |
K168 | Ubiquitination | Uniprot | |
R184 | Methylation | Uniprot | |
K188 | Ubiquitination | Uniprot | |
T202 | Phosphorylation | Uniprot | |
S205 | Phosphorylation | Uniprot | |
S214 | Phosphorylation | Uniprot | |
K223 | Ubiquitination | Uniprot | |
S226 | Phosphorylation | Uniprot | |
K235 | Acetylation | Uniprot | |
K235 | Ubiquitination | Uniprot | |
K236 | Acetylation | Uniprot | |
K236 | Ubiquitination | Uniprot | |
S261 | Phosphorylation | Uniprot | |
K262 | Ubiquitination | Uniprot | |
T266 | Phosphorylation | Uniprot | |
Y276 | Phosphorylation | Uniprot | |
S278 | Phosphorylation | Uniprot | |
K282 | Acetylation | Uniprot | |
K282 | Ubiquitination | Uniprot | |
Y291 | Phosphorylation | Uniprot | |
K292 | Acetylation | Uniprot | |
K292 | Ubiquitination | Uniprot | |
K294 | Acetylation | Uniprot | |
K294 | Ubiquitination | Uniprot | |
S299 | Phosphorylation | Uniprot | |
R310 | Methylation | Uniprot | |
K313 | Acetylation | Uniprot | |
K313 | Sumoylation | Uniprot | |
K313 | Ubiquitination | Uniprot | |
S316 | Phosphorylation | Uniprot | |
T317 | Phosphorylation | Uniprot | |
S325 | Phosphorylation | Uniprot | |
T327 | Phosphorylation | Uniprot | |
C328 | S-Nitrosylation | Uniprot | |
K334 | Acetylation | Uniprot | |
K334 | Ubiquitination | Uniprot | |
T336 | Phosphorylation | Uniprot | |
S339 | Phosphorylation | Uniprot | |
Y358 | Phosphorylation | Uniprot | |
T361 | Phosphorylation | Uniprot | |
K373 | Acetylation | Uniprot | |
K373 | Ubiquitination | Uniprot | |
R381 | Methylation | Uniprot | |
Y383 | Phosphorylation | Uniprot | |
Y400 | Phosphorylation | Uniprot | |
R401 | Methylation | Uniprot | |
K402 | Acetylation | Uniprot | |
K402 | Sumoylation | Uniprot | |
K402 | Ubiquitination | Uniprot | |
S409 | Phosphorylation | Uniprot | |
R410 | Methylation | Uniprot | |
S412 | Phosphorylation | Uniprot | |
S419 | Phosphorylation | Uniprot | |
S420 | Phosphorylation | Uniprot | |
T426 | Phosphorylation | Uniprot | |
S430 | Phosphorylation | P78527 (PRKDC) | Uniprot |
T436 | Phosphorylation | Uniprot | |
S438 | Phosphorylation | Uniprot | |
K439 | Acetylation | Uniprot | |
K439 | Ubiquitination | Uniprot | |
T441 | Phosphorylation | Uniprot | |
K445 | Acetylation | Uniprot | |
K445 | Methylation | Uniprot | |
K445 | Sumoylation | Uniprot | |
K445 | Ubiquitination | Uniprot | |
T446 | Phosphorylation | Uniprot | |
T449 | Phosphorylation | Uniprot | |
T458 | Phosphorylation | P00540 (MOS) | Uniprot |
S459 | Phosphorylation | P78527 (PRKDC) , P53350 (PLK1) , P00540 (MOS) | Uniprot |
Research Backgrounds
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.
Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2.
Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity). One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS.
O-glycosylated during cytokinesis at sites identical or close to phosphorylation sites, this interferes with the phosphorylation status.
S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.
Cytoplasm. Cytoplasm>Cytoskeleton. Nucleus matrix.
Highly expressed in fibroblasts, some expression in T- and B-lymphocytes, and little or no expression in Burkitt's lymphoma cell lines. Expressed in many hormone-independent mammary carcinoma cell lines.
Homopolymer assembled from elementary dimers. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1. Interacts with BCAS3. Interacts with DIAPH1. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Interacts with EPPK1; interaction is dependent of higher-order structure of intermediate filament. Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM. Interacts with NOD2. Interacts (via head region) with CORO1C (By similarity). Interacts with HDGF (isoform 2).
(Microbial infection) Interacts with HCV core protein.
The central alpha-helical coiled-coil IF rod domain mediates elementary homodimerization.
The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.
Belongs to the intermediate filament family.
Research Fields
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
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