Analytical Data
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Gene name
Vinculin
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简介
Vinculin (Vinculin Protein) is an important actin filament (F-actin) binding protein, actively participates in cell-matrix and cell-cell adhesion, regulates E-cadherin expression, and regulates E-cadherin expression through E-cadherin.Complex enhances mechanosensing of cell morphology and movement (by similarity).Vinculin self-associates with and is part of the complex (by similarity) with THSD1, PTK2/FAK1, TLN1 and VCL.Vinculin Protein, Mouse (HEK293, His) is the recombinant mouse-derived Vinculin protein, expressed by HEK293 , with C-His labeled tag.
- Application
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Alternative Names
Vinculin; Metavinculin; VCL
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Species
Mouse
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Source
HEK293
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Tag
C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q64727
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Expression Region
M1-Q1066
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Protein Length
Full Length
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Molecular Weight
118 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Vinculin is a crucial cytoskeletal protein that plays a significant role in cell adhesion, migration, and signaling by connecting integrins to the actin filament system. It is vital for maintaining the structural integrity of focal adhesions, cellular structures that mediate the attachment of cells to the extracellular matrix. Research on vinculin has gained momentum as its dysregulation is implicated in various diseases, including cancer and cardiovascular disorders. Understanding its structure and function is essential for developing therapeutic strategies targeting these conditions. Recombinant vinculin proteins are produced to study its molecular properties and interactions in detail, providing insights into its activation mechanisms and role in cellular processes. Techniques such as X-ray crystallography and cryo-electron microscopy are employed to elucidate the structural dynamics of vinculin in different conformational states. Furthermore, recombinant vinculin can be used in in vitro assays to examine its role in mechanotransduction, where cells convert mechanical stimuli into biochemical signals. This research is vital for uncovering the complexities of vinculin’s function and its impact on cellular behavior, helping to identify potential targets for clinical intervention in vinculin-related pathologies.
