Recombinant Human Vinculin (VCL) Protein (GST)

Name: Recombinant Human Vinculin (VCL) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02332P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Vinculin (VCL) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P18206
Target Symbol	VCL
Synonyms	CMD1W; CMH15; Epididymis luminal protein 114; HEL114; Metavinculin; MV; MVCL; OTTHUMP00000019861; OTTHUMP00000019862; VCL; VINC; VINC_HUMAN; Vinculin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	PVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVE
Expression Range	2-235aa
Protein Length	Partial
Mol. Weight	53.0kDa
Research Area	Cell Adhesion
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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	Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular Location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction, adherens junction. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side.
Protein Families	Vinculin/alpha-catenin family
Database References	HGNC: 12665 OMIM: 193065 KEGG: hsa:7414 STRING: 9606.ENSP00000211998 UniGene: PMID: 29241625 ERalpha upregulates vinculin expression in breast cancer cells; Loss of vinculin promotes amoeboid features of cancer cells PMID: 28266545 We report that polyoma small T antigen leads to upregulation of tubulin and vinculin in a time dependent manner with tubulin expression being most significantly affected. PMID: 29104053 Differential phosphatidylinositol 4,5-diphosphate binding of vinculin isoforms promotes quasi-equivalent dimerization. PMID: 27503891 Study used an all-heavy-atom structure-based model to study vinculin activation by talin in a high-tension context mechanically driven by F-actin, showed that vinculin activation may proceed from an intermediate state stabilized by partial talin-vinculin association. There is a low-force regime and a high-force regime where vinculin activation is dominated by two different pathways with distinct responses to force. PMID: 29045864 Vinculin head-tail interaction is required on soft substrates to destabilize vinculin and talin in FAs, and to allow hMSCs branching. Another module involves paxillin and FAK, which soft substrates also destabilize, but independently of vinculin head-tail interaction. This multi-modularity may be key to allow a versatile response to complex biomechanical cues. PMID: 27169142 The central role of talin and vinculin in cell adhesions suggests that the disintegration of the tissue in atherosclerosis could be partially driven by downregulation of these genes, leading to loosening of cell-ECM interactions and remodeling of the tissue. PMID: 27816808 East Asian common VCL variant p.Asp841His (D841H) was associated with sudden unexplained nocturnal death syndrome (SUNDS) in the Chinese Han population. PMID: 28373245 We identified mutations in VCL associated with Short segment Hirschsprung disease. Correction of this mutation in induced pluripotent stem cells using CRISPR/Cas9 editing, as well as the RET G731del mutation that causes Hirschsprung disease with total colonic aganglionosis, restored enteric neural crest cell function. PMID: 28342760 This review discusses the current understanding of the roles of vinculin in cell-cell and cell-matrix adhesions. Emphasis is placed on the how vinculin is recruited, activated and regulated. [review] PMID: 28401269 Study predicted the structure of the MAPK1-vinculin binding interface using a combination of flexible docking and molecular dynamics simulations, and confirmed that the MAPK1-vinculin interaction is mechanically regulated, and implicated a change in the vinculin D3-D4 cleft size upon vinculin activation as the basis for the conformational selectivity of MAPK1 binding toward open vinculin. PMID: 28494959 These results suggest that vinculin promotes the nuclear localization of transcription factor TAZ to inhibit the adipocyte differentiation on rigid extracellular matrix. PMID: 28115535 The VCL-encoding protein was involved in cardiomyopathy that associated with hypertension, therefore our results suggest the rs4746172 of VCL may be a novel target for clinical interventions to reduce CVD risk by regulating blood pressure in male Chinese PMID: 26487440 Three novel genes were identified as recurrently mutated; MYCN, MYO5B and VCL, and mutations in these genes were exclusively found in malignant sympathetic paraganglioma tumors. PMID: 26650627 roles and mechanisms of phospholipids in regulating the structure and function of vinculin and of its muscle-specific metavinculin splice variant. PMID: 26728462 Upon actin engagement, the N-terminal "strap" and helix 1 are displaced from the vinculin tail helical bundle to mediate actin bundling. PMID: 26493222 This study defined a plastic relationship between vinculin-mediated tension and adhesion complex area that controls fundamental cell-matrix adhesion properties. PMID: 26109125 Analysis showed that ITGB4 and VCL were upregulated in exosomes derived from taxane-resistant prostate cancer cells suggesting them as useful markers for progression of prostate cancer associated with taxane-resistance. PMID: 25997717 vinculin, present in the joints of anti-citrullinated protein antibody (ACPA)(+) rheumatoid arthritis patients, was identified as an autoantigen targeted by ACPA and CD4(+) T cells. PMID: 25942574 The activation of vinculin by stretched talin induces a positive feedback that reinforces the actin-talin-vinculin association. PMID: 24452080 Data indicate that specific protein interactions are spatially segregated within focal adhesions (FAs) at the nanoscale to regulate vinculin activation and function. PMID: 26053221 Vinculin expression was found to be significantly downregulated. PMID: 25496021 Our NMR and ITC data indicate that the SH3a and SH3b domains of CAP simultaneously bind to a long proline-rich region of vinculin with different binding specificities PMID: 24878663 PIP2 binding is required for the control of vinculin dynamics and turnover in focal adhesions. PMID: 25488920 Vinculin was identified as a potential plasma biomarker for age-related macular degeneration. PMID: 25298412 vinculin negatively regulates malignant phenotype of tumor cells including MT1-MMP transcription through MEK/ERK pathway PMID: 25449281 Vinculin is a new marker for atherosclerosis. PMID: 24369271 Data indicate the role of vinculin in inducing the talin mediated integrin activation. PMID: 24446374 vinculin binds to Rab5 and is required for Staphylococcus aureus uptake in cells. PMID: 24466349 Case Report: VCL-ALK gene fusion in renal cell carcinoma in patient with sickle cell trait. PMID: 24698962 These data reveal an unexpected regulatory mechanism in which vinculin Y822 phosphorylation determines whether cadherins transmit force and provides a paradigm for how a shared component of adhesions can produce biologically distinct functions. PMID: 24751539 p38 mitogen-activated protein kinase interacts with vinculin at focal adhesions during fatty acid-stimulated cell adhesion. PMID: 24219282 These results indicate that mechanical forces loaded to focal adhesions (FAs) facilitate vinculin binding to talin at FAs. PMID: 24452377 this study elucidated how tensile forces generated by single stress fibers are temporally and spatially distributed to vinculin mechanosensors located within cell-matrix adhesions PMID: 23687380 Data indicate that lasp-2 interacts with the focal adhesion proteins vinculin and paxillin. PMID: 23389630 VAX1 rs10787760, rs6585429 and rs1871345 polymorphisms may be involved in nonsyndromic cleft lip with or without cleft palate in Brazilian patients, but there is no association with polymorphisms in FGF12, VCL, or CX43 PMID: 23679094 Vinculin protein level in SW620 was much higher than that in SW480 cells. PMID: 23627409 Studies indicate that that vinculin not only bundles actin filaments but can also cap these filaments and promote actin polymerization. PMID: 23466368 these data suggest that metavinculin enrichment in attachment sites of muscle cells leads to higher mechanical stability of adhesion complexes allowing for greater shear force resistance. PMID: 23159629 Western blotting demonstrated that vinculin was predominantly expressed in the pancreatic cancer tissues compared with non-cancerous tissues; findings indicate that vinculin may be a clinically useful biomarker of pancreatic cancer PMID: 22940724 These binding assays show that raver1 forms a ternary complex with metavinculin and vinculin mRNA. PMID: 22709580 The metavinculin promoted severing of actin filaments, most efficiently at substoichiometric concentrations. PMID: 22613835 binding studies suggest that vinculin must be in an activated state to bind to alpha-catenin and that this interaction is stabilized by the formation of a ternary alpha-catenin-vinculin-F-actin complex, which can be formed via the F-actin binding domain PMID: 22493458 Results implicate Vinculin-dependent VE-cadherin mechanosensing in endothelial processes such as leukocyte extravasation and angiogenesis. PMID: 22391038 Data show that SGK1 regulates cell migration via vinculin dephosphorylation, a mechanism that is controlled by membrane androgen receptor function. PMID: 22309306 alpha-catenin employs a novel mechanism to activate vinculin and may explain how vinculin is differentially recruited and/or activated in cell-cell and cell-matrix adhesions. PMID: 22235119 sca4 activates vinculin and interacts with the actin cytoskeleton; vinculin has roles in Rickettsia pathogenesis PMID: 21841197 VCL is expressed differently in benign prostatic hyperplasia and prostate cancer, which may serve as an indicator for the differential diagnosis of benign and malignant prostate diseases. PMID: 21171262 When myosin II contractility was inhibited, the k(off) values for all three proteins changed rapidly, in a highly protein-specific manner: dissociation of vinculin from FAs was facilitated, whereas dissociation of paxillin and zyxin was attenuated. PMID: 21486952 Talin-1 and vinculin negatively affect tyrosine phosphorylation of paxillin, a novel positive regulator of HIV-1 infection, and impose an early block to infection by distinct retroviruses. PMID: 21763488

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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.

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