Recombinant Mouse Vimentin (Vim)

Code CSB-YP025857MO
MSDS
Size Pls inquire
Source Yeast
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Code CSB-EP025857MO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP025857MO
MSDS
Size Pls inquire
Source Baculovirus
Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
>85% (SDS-PAGE)
Target Names
Vim
Uniprot No.
Alternative Names
VimVimentin
Species
Mus musculus (Mouse)
Expression Region
2-466
Target Protein Sequence
STRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPTFSS LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
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.
Gene References into Functions
  1. The Listeria monocytogenes virulence factor InlF was found to bind vimentin and was necessary for optimal bacterial colonization of the brain. PMID: 29487235
  2. MAGE-G1 interacted with fascin 1 or vimentin in P19 cells after a 6-day retinoic acid-induced neuronal differentiation. PMID: 28374796
  3. Results found that the absence of vimentin impairs spontaneous endothelial differentiation in vitro and have furthering the understanding of the regulators of differentiation. PMID: 27480130
  4. Protein phosphatase 1 is a key protein serine/threonine phosphatase that controls vimentin Ser-56 dephosphorylation in smooth muscle. PMID: 27457922
  5. These findings identify vimentin as a positive regulator of stemness in the developing mouse mammary gland and in breast cancer cells. PMID: 28947532
  6. 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. PMID: 27568979
  7. These findings identify two specific sites on vimentin that are phosphorylated by Cadmium. PMID: 28450285
  8. The expression level of vimentinin liver cirrhotic tissues were significantly higher than that in chronic hepatitis tissues. PMID: 27538444
  9. both arthritis-susceptible and -resistant mice can generate cellular and humoral immunity to Vim. PMID: 27602574
  10. vimentin knockout neurons were insensitive to the axonotrophic effects of Clostridium botulinum C3 exoenzyme PMID: 27419376
  11. These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser-56. PMID: 27662907
  12. 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 PMID: 26251181
  13. these findings identify a hereto-unappreciated role for serine-38 phosphorylated vimentin as an important determinant of myofibroblast sensitivity to Withaferin A. PMID: 26186445
  14. Vimentin expression increased after traumatic brain injury and was positively correlated with edema and neurological impairments. PMID: 26039099
  15. Annexin, lamin, and vimentin were identified as universal dystrophic markers PMID: 26102067
  16. Astrocytes deficient of GFAP and vimentin showed decreased Notch signal sending competence and altered expression of Notch signaling pathway-related genes PMID: 26118771
  17. Absence of GFAP, or both GFAP and vimentin, alters Alzheimer's disease-induced changes in gene expression profile of astrocytes, showing a compensation of the decrease of neuronal support genes and a trend for a higher inflammatory expression profile PMID: 25731615
  18. Vimentin is not only a major organizing element of the intermediate filament network but is also involved in both binding and uptake of C3 exoenzyme. PMID: 24967582
  19. Cytokinetic Failure-induced Tetraploidy Develops into Aneuploidy, Triggering Skin Aging in Phosphovimentin-deficient Mice. PMID: 25847236
  20. Vimentin has a role in regulating activation of the NLRP3 inflammasome PMID: 25762200
  21. protein(s) that associated with RPTPbeta in response to IGF-I and IGFBP-2 in vascular smooth muscle cells PMID: 25787077
  22. Data suggest MAP kinase-interacting kinases (Mnk1, Mnk2) regulate cell migration/wound healing, expression of Vim, stability of Vim, and binding of eIF4E (eukaryotic translation initiation factor 4E)/Cyfip1 (cytoplasmic FMR1 interacting protein 1). PMID: 25588502
  23. This review discusses various novel functions which are now known to be mediated by vimentin, summarizing structure, regulation and roles of vimentin in cell adhesion, migration, angiogenesis, neurite extension, and cancer. PMID: 24387004
  24. Double-immunostaining experiments with antibodies against Stk33 and vimentin showed a striking colocalization of Stk33 and vimentin in the hypothalamus. PMID: 24057876
  25. Keratocyte activation and differentiation play a key role in fibrosis, and vimentin, a major structural type III intermediate filament, is a required component of this process. PMID: 24854859
  26. absence of GFAP and vimentin in glial cells does not seem to affect the outcome after peripheral motoneuron injury but may have an important effect on the response dynamics PMID: 24223940
  27. We demonstrate, using long-term 4D imaging, that the vimentin intermediate filament establishes mitotic polarity in mammalian cell lines and mediates the asymmetric partitioning of damaged proteins. PMID: 24843142
  28. defect of mitotic vimentin phosphorylation causes microophthalmia and cataract PMID: 24142690
  29. Vimentin synthesis initiates during a differentiation process of trophoblast giant cells and continues throughout the stage of vascular TGC. PMID: 23664004
  30. These data suggest that vimentin is required for the minute virus of mice life cycle, presenting possibly a dual role: (1) following virus escape from endosomes and (2) during endosomal trafficking PMID: 23838001
  31. Data indicate interaction of PPARgamma with vimentin in the cytosolic compartment, in which vimentin regulating the turnover rate of PPARgamma, which further regulate genomic or non-genomic activities through the regulation of PPARgamma protein degradation. PMID: 23297177
  32. involvement of vimentin in migration processes at different stages of development and try to resolve current contradictions concerning the role of vimentin in various events of cell migration PMID: 23885566
  33. we propose a novel regulatory mechanism of IP3R1 activity by type III intermediate filament vimentin PMID: 22929228
  34. Data indicate that vimentin intermediate filaments must coalesce at mature focal adhesions for efficient endoplasmic spreading. PMID: 23115305
  35. These data show for the first time that decorin has an impact on the biology of alpha2beta1 integrin and the vimentin intermediate filament system. PMID: 23226541
  36. overexpression of mesangial integrin alpha1 and podocyte vimentin and integrin alpha3 may be important features of glomerular Alport disease PMID: 23236390
  37. expression detected in the mylohyoid muscle and surrounding tissues at embryonic day 12 PMID: 22476899
  38. TGFbeta stimulates vimentin production via PI3K-Akt-mTOR signaling, which leads to suppression of ATF4-dependent Ocn transcription and osteoblast differentiation. PMID: 22952236
  39. vimentin ablation results in defective steroidogenesis PMID: 22535769
  40. vimentin is a regulator of NRG1 type III function and peripheral nerve myelination PMID: 22357929
  41. Endothelial cell surface vimentin binding peptide induces angiogenesis under hypoxic/ischemic conditions. PMID: 21803052
  42. absence of Zmpste24 profoundly alters the processing of the cytoskeletal protein vimentin PMID: 21828285
  43. Corneal antifibrotic switch identified in genetic and pharmacological deficiency of vimentin. PMID: 22117063
  44. Data demonstrated that Abeta toxic species cross the plasma membrane, accumulate in cells and bind to a variety of internal proteins, vimentin (cytoskeleton), cathepsin D (lysosomes), GRP-78 (endoplasmic reticulum and associated membranes). PMID: 21966382
  45. study reports that vimentin filaments associate with collagen mRNAs in a 5'stem-loop sequence and LARP6-dependent manner and stabilize collagen mRNAs PMID: 21746880
  46. When vimentin organization is disrupted by a dominant-negative mutant or by silencing, there is a loss of polarity. These findings demonstrate an antagonistic relationship between vimentin intermediate filaments (VIF) and the formation of lamellipodia. PMID: 21346197
  47. Mature focal adhesions and their derivative fibronectin fibril-aligned fibrillar adhesions (FbAs) serve as docking sites for vimentin intermediate filaments (IFs) in a plectin isoform 1f (P1f)-dependent manner. PMID: 20702585
  48. Increases in post-traumatic vimentin mRNA levels in the cortex and in the hippocampus appear together with vimentin immunoreactivity in astrocytes starting one day after severe trauma. PMID: 20479526
  49. The interaction of hormone-sensitive lipase with vimentin, and its hormonal dependence, was confirmed by coimmunoprecipitation. PMID: 20143880
  50. Sol-gel polymerization of tetraethoxysilane proceeded preferentially on the surface of intermediate filaments assembled from vimentin protein in vitro, resulting in silica-coated fibres. PMID: 19656809

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Subcellular Location
Cytoplasm. Cytoplasm, cytoskeleton. Nucleus matrix. Cell membrane.
Protein Families
Intermediate filament family
Tissue Specificity
Detected in eye lens fiber cells (at protein level). Expressed in retinal lens epithelial cells (at protein level).
Database Links
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