Recombinant Mouse Vimentin (VIM) Protein (His&Myc)

Name: Recombinant Mouse Vimentin (VIM) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05157P
Price: 680.8 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Vimentin (VIM) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P20152
Target Symbol	VIM
Synonyms	VimVimentin
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	STRSVSSSSYRRMFGGSGTSSRPSSNRSYVTTSTRTYSLGSALRPSTSRSLYSSSPGGAYVTRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPTFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
Expression Range	2-466aa
Protein Length	Full Length of Mature Protein
Mol. Weight	61.0 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm. Cytoplasm, cytoskeleton. Nucleus matrix. Cell membrane.
Protein Families	Intermediate filament family
Database References	KEGG: mmu:22352 STRING: 10090.ENSMUSP00000028062 UniGene: Mm.268000
Tissue Specificity	Detected in eye lens fiber cells (at protein level). Expressed in retinal lens epithelial cells (at protein level).

Gene Functions References

The Listeria monocytogenes virulence factor InlF was found to bind vimentin and was necessary for optimal bacterial colonization of the brain. PMID: 29487235
MAGE-G1 interacted with fascin 1 or vimentin in P19 cells after a 6-day retinoic acid-induced neuronal differentiation. PMID: 28374796
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
Protein phosphatase 1 is a key protein serine/threonine phosphatase that controls vimentin Ser-56 dephosphorylation in smooth muscle. PMID: 27457922
These findings identify vimentin as a positive regulator of stemness in the developing mouse mammary gland and in breast cancer cells. PMID: 28947532
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
These findings identify two specific sites on vimentin that are phosphorylated by Cadmium. PMID: 28450285
The expression level of vimentinin liver cirrhotic tissues were significantly higher than that in chronic hepatitis tissues. PMID: 27538444
both arthritis-susceptible and -resistant mice can generate cellular and humoral immunity to Vim. PMID: 27602574
vimentin knockout neurons were insensitive to the axonotrophic effects of Clostridium botulinum C3 exoenzyme PMID: 27419376
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser-56. PMID: 27662907
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
these findings identify a hereto-unappreciated role for serine-38 phosphorylated vimentin as an important determinant of myofibroblast sensitivity to Withaferin A. PMID: 26186445
Vimentin expression increased after traumatic brain injury and was positively correlated with edema and neurological impairments. PMID: 26039099
Annexin, lamin, and vimentin were identified as universal dystrophic markers PMID: 26102067
Astrocytes deficient of GFAP and vimentin showed decreased Notch signal sending competence and altered expression of Notch signaling pathway-related genes PMID: 26118771
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
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
Cytokinetic Failure-induced Tetraploidy Develops into Aneuploidy, Triggering Skin Aging in Phosphovimentin-deficient Mice. PMID: 25847236
Vimentin has a role in regulating activation of the NLRP3 inflammasome PMID: 25762200
protein(s) that associated with RPTPbeta in response to IGF-I and IGFBP-2 in vascular smooth muscle cells PMID: 25787077
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
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
Double-immunostaining experiments with antibodies against Stk33 and vimentin showed a striking colocalization of Stk33 and vimentin in the hypothalamus. PMID: 24057876
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
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
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
defect of mitotic vimentin phosphorylation causes microophthalmia and cataract PMID: 24142690
Vimentin synthesis initiates during a differentiation process of trophoblast giant cells and continues throughout the stage of vascular TGC. PMID: 23664004
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
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
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
we propose a novel regulatory mechanism of IP3R1 activity by type III intermediate filament vimentin PMID: 22929228
Data indicate that vimentin intermediate filaments must coalesce at mature focal adhesions for efficient endoplasmic spreading. PMID: 23115305
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
overexpression of mesangial integrin alpha1 and podocyte vimentin and integrin alpha3 may be important features of glomerular Alport disease PMID: 23236390
expression detected in the mylohyoid muscle and surrounding tissues at embryonic day 12 PMID: 22476899
TGFbeta stimulates vimentin production via PI3K-Akt-mTOR signaling, which leads to suppression of ATF4-dependent Ocn transcription and osteoblast differentiation. PMID: 22952236
vimentin ablation results in defective steroidogenesis PMID: 22535769
vimentin is a regulator of NRG1 type III function and peripheral nerve myelination PMID: 22357929
Endothelial cell surface vimentin binding peptide induces angiogenesis under hypoxic/ischemic conditions. PMID: 21803052
absence of Zmpste24 profoundly alters the processing of the cytoskeletal protein vimentin PMID: 21828285
Corneal antifibrotic switch identified in genetic and pharmacological deficiency of vimentin. PMID: 22117063
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
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
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
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
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
The interaction of hormone-sensitive lipase with vimentin, and its hormonal dependence, was confirmed by coimmunoprecipitation. PMID: 20143880
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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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