Analytical Data
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Gene name
Integrin alpha V beta 3
- Application
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Alternative Names
αVβ3; Integrin alpha V beta 3; beta3; alphaV; ITGAV&ITGB3; Integrin alpha V β 3; β3
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Species
Mouse
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Source
HEK293
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Tag
C-hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P43406 (F31-V988)&O54890
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Expression Region
P43406 (F31-V988)&O54890 (E26-D717)
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Molecular Weight
110-135 kDa & 50-60 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
Integrin alpha V beta 3 is a critical transmembrane protein that plays a fundamental role in cellular adhesion and signaling processes. It is primarily expressed on the surface of various cell types, including endothelial cells and osteoclasts, and is involved in numerous physiological functions such as wound healing, angiogenesis, and bone remodeling. Aberrant expression of alpha V beta 3 integrin has been implicated in several pathological conditions, particularly in tumor progression and metastasis, making it a significant target for cancer therapies. Research has focused on the molecular structure and functional mechanisms of this integrin to understand its role in tumor microenvironments. The development of recombinant alpha V beta 3 proteins has enabled scientists to study its interactions with extracellular matrix components and signaling pathways in more detail. Furthermore, these recombinant proteins have been utilized to design integrin inhibitors that can potentially block tumor cell adhesion and migration, thus providing a novel approach for cancer treatment. The exploration of integrin alpha V beta 3 continues to be a promising area of biomedical research, contributing to advances in targeted therapy and improved clinical outcomes for patients facing integrin-related diseases.
