Phospho-Vimentin (Ser39) Antibody - #AF8233
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# AF8233, RRID:AB_2840295.
展开/折叠
CTRCT30; Epididymis luminal protein 113; FLJ36605; HEL113; VIM; VIME_HUMAN; Vimentin;
抗原和靶标
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
种属预测
score>80的预测可信度较高,可尝试用于WB检测。*预测模型主要基于免疫原序列比对,结果仅作参考,不作为质保凭据。
High(score>80) Medium(80>score>50) Low(score<50) No confidence
翻译修饰 - P08670 作为底物
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 |
研究背景
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.
研究领域
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Human Diseases > Cancers: Overview > MicroRNAs in cancer.
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