CTRCT30; Epididymis luminal protein 113; FLJ36605; HEL113; VIM; VIME_HUMAN; Vimentin;
WB 1:500-1:2000, IHC 1:50-1:200, IF 1:200, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat
Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Vimentin Antibody detects endogenous levels of total Vimentin.
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide.
A synthesized peptide derived from human Vimentin
Observed Mol.Wt.: 53kDa.
Predicted Mol.Wt.: 54kDa.
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.
VIM is an intermediate filament protein. Intermediate filament proteins are expressed in a tissue-specific manner. Desmin is the subunit specific for muscle and vimentin the subunit specific for mesenchymal tissue.
10 20 30 40 50
MSTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR
60 70 80 90 100
SLYASSPGGV YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR
110 120 130 140 150
TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY
160 170 180 190 200
EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE
210 220 230 240 250
NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE EIQELQAQIQ
260 270 280 290 300
EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
310 320 330 340 350
AANRNNDALR QAKQESTEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN
360 370 380 390 400
FAVEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY
410 420 430 440 450
RKLLEGEESR ISLPLPNFSS LNLRETNLDS LPLVDTHSKR TLLIKTVETR
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.
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 (PubMed:21465480). Phosphorylated by STK33 (PubMed:18811945). Phosphorylated on tyrosine residues by SRMS (PubMed:29496907).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.
Homopolymer assembled from elementary dimers. Interacts with HCV core protein (PubMed:15846844). Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain) (By similarity). Interacts with SLC6A4 (PubMed:19270731). Interacts with STK33 (PubMed:18811945). Interacts with LARP6 (PubMed:21746880). Interacts with RAB8B (By similarity). Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton (PubMed:16361107, PubMed:18827015). Interacts with TOR1AIP1 (PubMed:16361107). Interacts with BCAS3 (PubMed:17505058). Interacts with DIAPH1 (PubMed:23325789). 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 (PubMed:16923132). Interacts with the non-receptor tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM (PubMed:29496907).
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.
Application: IF/ICC Species:mouse; Sample:Not available
Lenalidomide (1μM) inhibited JAM-A-transfected cell invasion (B) and EMT (C).
Application: WB Species:human; Sample:A549 cells
Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)
Application: WB Species:human; Sample:ARPE-19
Figure 4. Crocetin inhibits TGF-β2-induced EMT. After 1 h of pretreatment with crocetin, ARPE-19 cells used for EMT assay were stimulated with or without recombinant human TGF-β2 for up to 24 or 48 h. (A) Phase contrast photomicrographs of confluent cultures of cells were captured after treatment for 48 h. Scale bar: 200 μm. (B) Western blot analysis levels of of ZO-1, E-cadherin, Vimentin, α-SMA and the housekeeping protein GAPDH in the lysates of ARPE-19 cells after treatment for 48 h. *P< 0.05, **P< 0.01, ***P< 0.001. The data are presented as the mean ± S.D. (n = 3/group).
Application: WB Species:human; Sample:Not available
Fig. 2 YAF influences HIF-1α and EMT expression analysis in HCT-116 cell lines. a. Cells were incubated for 48 h in YAF. The level of HIF-1α, Clau-4, E-cd and VIM mRNA were found. b HCT-116 cells were incubated with YAF for 48 h. The level of HIF-1α, Clau-4, E-cd and VIM protiens were found. *P < 0.05. Results are folden change ± SE of at least three independent experiments
Application: IHC Species:human,mouse; Sample:Not available
Figure 6: Effect of PTL on p-ERK 2, NF-κB, Snail, and EMT protein levels. Brown or yellow staining was observed in the cytoplasmor nucleus. (A and C) Representative photographs of treated and untreated cells. PTL treatment reduced p-ERK 2, NF-κB, and Snail staining compared with sections obtained from control mice. (B and D) Representative photographs of treated and untreated cells. PTL treatment increased E-cadherin and Occludin staining and reduced Vimentin and N-cadherin staining compared with sections obtained from control mice. Each experiment was performed in triplicate. Results show the means of the three experiments, and the error bars represent standard deviation (*P < 0.05 and **P < 0.01).
Application: WB Species:rat; Sample:Not available
Effects of null-MVs and miR-200b-MVs administration on protein expression in TGFb-Indeced EMT.
Application: WB Species:mouse; Sample:B16F10
Fig. 5 The expression of p-PKCζ, p-cofilin and COX-2 after combined treatment of J-4 and Celecoxib. (a) Western blotting images of p-cofilin and COX-2 in B16-F10 cells with various treatments for 24 h. (b) Western blotting images of p-cofilin and COX-2 in A375 cells with various treatments for 24 h. (c) Relative mRNA level of PKCζ and COX-2 determined via RT-PCR. (d) The expression of EMT markers, E-Cadherin and Vimentin, and MMP-2/MMP-9 was affected in B16-F10 and A375 cells after various treatments for 24 h. J-4: 25 μM; Celecoxib: 25 μM. * P < 0.05; ** P < 0.01
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
|S7||Phosphorylation||P17252 (PRKCA) , Q96GD4 (AURKB) , Q02156 (PRKCE) , P17612 (PRKACA)||Uniprot|
|S25||Phosphorylation||P17252 (PRKCA) , Q96GD4 (AURKB) , P17612 (PRKACA)||Uniprot|
|S26||Phosphorylation||Q13153 (PAK1) , P17252 (PRKCA) , Q13177 (PAK2)||Uniprot|
|S39||Phosphorylation||P49137 (MAPKAPK2) , Q13177 (PAK2) , P17612 (PRKACA) , O75116 (ROCK2) , P31749 (AKT1) , Q13153 (PAK1) , Q96GD4 (AURKB) , P17252 (PRKCA)||Uniprot|
|S47||Phosphorylation||P17612 (PRKACA) , Q96GD4 (AURKB)||Uniprot|
|S51||Phosphorylation||Q13177 (PAK2) , Q13153 (PAK1) , P49137 (MAPKAPK2)||Uniprot|
|S55||Phosphorylation||P24941 (CDK2) , P06493 (CDK1)||Uniprot|
|S56||Phosphorylation||P78527 (PRKDC) , P06493 (CDK1) , P49137 (MAPKAPK2) , Q13153 (PAK1) , P24941 (CDK2) , Q00535 (CDK5)||Uniprot|
|S66||Phosphorylation||Q96GD4 (AURKB) , Q13177 (PAK2) , Q13153 (PAK1)||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|
|S459||Phosphorylation||P78527 (PRKDC) , P53350 (PLK1) , P00540 (MOS)||Uniprot|