Recombinant Human Vimentin Protein (His Tag)

Name: Recombinant Human Vimentin Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-4812
Availability: InStock

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Human
Accession	P08670
Synonym	CTRCT30, HEL113
Background	Vimentin is a type III intermediate filament (IF) protein found in various non-epithelial cells, especially mesenchymal cells. A vimentin monomer, has a central alpha-helical domain and carboxyl (tail) domains. Two monomers compose the basic subunit of vimentin assembly. Vimentin is crucial for supporting and anchoring the position of the organelles in the cytosol. Vimentin provided cells with a resilience absent from the microtubule or actin filament networks, when under mechanical stress in vivo. Therefore, in general, it is accepted that vimentin is the cytoskeletal component responsible for maintaining cell integrity. Vimentin is also responsible for stabilizing cytoskeletal interactions. It is found that vimentin control the transport of low-density lipoprotein. It has been used as a sarcoma tumor marker to identify mesenchyme.
Description	A DNA sequence encoding the human VIM (Met 1-Glu466) (P08670) was expressed, with a C-terminal His tag.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met 1-Glu466
Molecular Weight	The secreted recombinant human VIM consists of 476 a.a. and predicts a molecular mass of 55 KDa. The apparent molecular mass of the protein is approximately 56 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 40% acetonitrile, 0.1% TFA.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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	HGNC: 12692 OMIM: 116300 KEGG: hsa:7431 STRING: 9606.ENSP00000224237 UniGene: Hs.455493
Associated Diseases	Cataract 30, multiple types (CTRCT30)
Tissue Specificity	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.

Gene Functions References

This study measured the effects of vimentin expression on the mechano-elastic and migratory properties of the highly invasive breast carcinoma cell line MDA231. It demonstrated that vimentin stiffens cells and enhances cell migration in dense cultures, but exerts little or no effect on the migration of sparsely plated cells. PMID: 29022351
Positive vimentin expression could serve as a poor prognostic marker in gastric cancer[review, meta-analysis] PMID: 30078472
High vimentin expression is associated with pancreatic cancer. PMID: 29956814
the HDAC inhibitors augmented both Ecadherin and vimentin expression and their effects varied in different cholangiocarcinoma cell lines. Therefore, the clinical use of HDAC inhibitors in biliary cancer should be considered cautiously PMID: 29767267
miR-373 suppresses gastric cancer metastasis by downregulating vimentin. PMID: 29257346
Vimentin role in the M2BP inhibition of the HIV-1 virion production.M2BP mediates the interaction between HIV-1 Gag and Vimentin. PMID: 27604950
Desmin, Glial Fibrillary Acidic Protein, Vimentin, and Peripherin are type III intermediate filaments that have roles in health and disease [review] PMID: 29196434
Silencing of Vimentin in CNE2 cells leads to a decrease of microvessel density and VEGF, CD31, MMP2, and MMP9 expressions in pulmonary metastatic tumors. PMID: 28744809
Carcinoid-like/labyrinthine pattern of cell arrangement in vimentin/cytokeratin 20 expressing sebaceous neoplasms may represent a morphological phenotype of sebaceous mantles. PMID: 28027080
Cell surface vimentin mediates DENV-2 infection of vascular endothelial cells. PMID: 27910934
HIF-1alpha expression was upregulated in the vasculogenic mimicry-positive CRC cell line HCT-116 and thereby affected the expression of the EMT-related markers Claudin-4, E-cadherin (E-cd) and Vimentin(VIM). PMID: 27869227
our results demonstrated that vimentin in human GC tissues and cell lines was upregulated due to its de-ubiquitination after interactions with USP14 and miR-320a, which could promote the aggressiveness of GC cells. PMID: 27448976
Knocking down long pentraxin-3 (PTX3) or vimentin repressed oleate-induced head and neck squamous cell carcinomas (HNSCCs) invasion. PMID: 28489600
stromal vimentin expression is a promising indicator for survival prediction and adjuvant chemotherapy response in patients with stage II colorectal cancer with high-risk factors for recurrence. PMID: 28611349
Vimentin and its interaction with Shigella flexneri IpaC are dispensable for effector translocation pore formation, but are required for stable docking of Shigella flexneri to cells; moreover, stable docking triggers effector secretion. PMID: 27572444
the elongation reaction of vimentin in solution and in situ by time-resolved static and dynamic light scattering, is reported. PMID: 27655889
Vimentin induced by exosomes is necessary for lung cancer to induce mesenchymal transition (EMT) in recipient bronchial epithelial cells (HBECs). PMID: 27363026
our results demonstrate that vimentin silencing in ovarian cancer cells upregulates proteins of the exocytotic process to decrease cellular cisplatin accumulation PMID: 27322682
The combined biomarkers E-cadherin, membranous epidermal growth factor receptor (EGFR) and vimentin show a stronger prognostic value for and disease-free survival than any of the single biomarkers. PMID: 27172790
AHR protein-vimentin protein complex is formed in the cytoplasm resulting in proteasome degradation of vimentin. PMID: 27752740
TRIM56 is the ubiquitin ligase that is degrading vimentin in ovarian cancer cells, regulation cell migration and neoplasm invasiveness. PMID: 28771721
TIS21 attenuated Doxorubicin-induced cancer cell senescence by inhibiting linear actin nucleation via Nox4-ROS-ABI2-DRF signal cascade PMID: 27932314
this study indicates that OPN can induce epithelial-mesenchymal transition of hepatocellular carcinoma cells through increasing vimentin stability PMID: 26824421
The findings support a mechanism in which miR-375 suppresses RUNX1 levels, resulting in reduced vimentin and L-plastin expression. Knockdown of RUNX1, L-plastin, and vimentin resulted in significant reductions in cell invasion in vitro, indicating the functional significance of miR-375 regulation of specific proteins involved in head and neck squamous cell carcinoma (HNSCC) invasion. PMID: 28499703
Vimentin expression was an adverse prognostic factor for DSS in TSCC patients, even after the adjustment for cell differentiation, pathological stage, and expression levels of Snail, Twist, E-cadherin, and N-cadherin. Snail, E-cadherin, N-cadherin, and Vimentin were associated with tumorigenesis and pathological outcomes PMID: 28570699
circulating anti-vimentin IgG autoantibody levels are much greater in idiopathic pulmonary fibrosis subjects than in normal controls PMID: 28754682
RhoA/ROCK and Raf-1/CK2 pathway are responsible for TNF-alpha-mediated endothelial cytotoxicity via regulation of the vimentin cytoskeleton. PMID: 28743511
It was concluded that islet cell expression of vimentin indicates a degree of plasticity and dedifferentiation with potential loss of cellular identity in diabetes. PMID: 28348116
findings have identified a role for members of these signaling pathways in the regulation of EGF-induced vimentin expression in the MDA-MB-468 breast cancer cell line PMID: 27163529
changes in methylation levels in cfDNA associated with hepatocellular carcinoma and could represent useful plasma-based biomarker PMID: 28333958
vimentin regulates the differentiation switch via modulation of K5/K14 expression. Moreover, because there was a significant correlation between high vimentin-K14 expression and recurrence/poor survival in oral cancer patients, vimentin-K14 together may prove to be the novel markers for the prognostication of human oral cancer. PMID: 28225793
Data indicate that ellagic aicd (EA) down-regulates the expression of COX-2, NF-kappa B, vimentin and up-regulates the expression of E-cadherin in in pancreatic carcinom PANC-1 cells. PMID: 28135203
Bevacizumab treatment was also associated with structural protein abnormalities, with decreased GFAP and vimentin content and upregulated GFAP and vimentin mRNA expression. PMID: 28419863
Decreasing cell surface vimentin by small interfering RNA (siRNA) knockdown in HeLa and NIKS cells significantly increased human papillomavirus 16 infectious internalization, while overexpression of vimentin had the opposite effect identifying vimentin as a viral restriction factor. PMID: 28566373
From these data, we suggest that filamentous vimentin underneath the plasma membrane is involved in increasing integrin adhesiveness, and thus regulation of the vimentin-integrin interaction might control cell adhesion PMID: 27044755
depletion induces phosphorylation of the microtubule-associated GEF-H1 on Ser886, and thereby promotes RhoA activity and actin stress fiber assembly. PMID: 28096473
Data show that the filament elongation of both desmin and keratin K8/K18 proceeds very similar to that of vimentin. PMID: 27304995
Coexistence of vimentin-positive and Axl-high expression is a poor prognostic factor for primary breast cancer. Vimentin and Axl expression might contribute to the aggressive phenotype in breast cancer. PMID: 27506606
our findings suggest that the HIF-1alpha-HDAC1 complex transcriptionally inhibits miR-548an expression during hypoxia, resulting in the upregulation of vimentin that facilitates the pancreatic tumorigenesis. PMID: 27353169
Rab7a depletion decreases the amount of active Rac1 but not its abundance and reduces the number of cells with vimentin filaments facing the wound, indicating that Rab7a has a role in the orientation of vimentin filaments during migration PMID: 27888097
Over-expression of TNC, SMA, and vimentin were significantly correlated with the lower overall survival in prostate cancer patients. PMID: 28341124
Results show that VIM mRNA is regulated in melanoma by UNR protein. PMID: 27908735
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin phosphorylation at Ser-56. PMID: 27662907
Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange.( PMID: 27694444
These findings are the first to demonstrate that vimentin is critical for influenza viral infection as it facilitates endosomal trafficking and acidification, and mediates viral genome penetration into the cytoplasm to propagate the infection. PMID: 27423069
RAP1 promotes colorectal cell migration through the regulation of Vimentin and RAP1 may act as a potential target for the diagnosis and therapy of CRC. PMID: 28381157
High vimentin expression is associated with Non Small-cell Lung Cancer. PMID: 28373440
data demonstrates that keratinocyte migration requires the interaction between vimentin and keratins at the -YRKLLEGEE- sequence at the helical 2B domain of vimentin PMID: 27072292
High vimentin expression is associated with malignant pleural mesothelioma. PMID: 27646775
Increased TET1 induced re-expression of vimentin through active DNA demethylation, and cause partial epithelial-to-mesenchymal (EMT) in A2780 cells. PMID: 28150354

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.