Recombinant Mouse Integrin alpha V beta 3 Protein, CF Summary
|Mouse Integrin alpha V
Accession # P43406
|His-Pro||GGGSGGGS||Acidic Tail||6-His tag|
|Mouse Integrin beta 3
Accession # O54890
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 400 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Integrin alpha V beta 3
Integrin alpha V beta 3 together with alpha IIb beta 3, constitutes the only known beta 3 Integrins (1‑3). The non‑covalent heterodimer of 170 kDa alpha V/CD51 and 93 kDa beta 3/CD61 subunits shows wide expression, notably by endothelial cells and osteoclasts (2‑4). Each subunit has a transmembrane sequence and a short cytoplasmic tail connected to the cytoskeleton. Active cell surface alpha V beta 3 adheres to matrix proteins including vitronectin, fibronectin, fibrinogen and thrombospondin (2, 3). The ligand binding site of alpha V beta 3 is in the N‑terminal head region, formed by interaction of the beta 3 vWFA domain with the alpha V beta-propeller structure (4). The alpha V subunit contributes a thigh and a calf region, while the beta 3 subunit contains a PSI domain and four cysteine‑rich I‑EGF folds. The alpha V subunit domains termed thigh, calf‑1 and calf‑2 generate a “knee” region that is bent when the alpha V beta 3 is in its constitutively inactive state. Activation, either by “inside out” signaling or by Mg2+ or Mn2+ binding, extends the Integrin to expose its ligand binding site (1, 4). The 958 aa mouse alpha V ECD shares 92‑95% aa sequence identity with human, rat and bovine alpha V while the 692 aa mouse beta 3 ECD shares 95% aa identity with rat and 89‑91% with human, canine, equine, bovine and porcine beta 3. alpha V beta 3 is essential for the maturation of osteoclasts and their binding and resorption of bone; it also, however, promotes their apoptosis (5, 6). M‑CSF R and alpha V beta 3 share signaling pathways during osteoclastogenesis, and deletion of either molecule causes osteopetrosis (5, 6). alpha V beta 3 is involved in several other signaling pathways by direct interaction with receptor tyrosine kinases and ligands. For example, it cooperates with endothelial cell VEGF R2 in angiogenesis, and with IGF‑1 to promote cancer cell proliferation and invasiveness (7, 8). Also, cell entry of several viruses is mediated by alpha V beta 3 (4, 9).
- Hynes, R. O. (2002) Cell 110:673.
- Serini, G. et al. (2006) Exp. Cell Res. 312:651.
- Ross, F. P. and S. L. Teitelbaum (2005) Immunol. Rev. 208:88.
- Xiong, J. et al. (2001) Science 294:339.
- McHugh, K. P. et al. (2000) J. Clin. Invest. 105:433.
- Faccio, R. et al. (2003) J. Clin. Invest. 111:749.
- Somanath, P.R. et al. (2009) Angiogenesis 12:177.
- Saegusa, J. et al. (2009) J. Biol. Chem. 284:24106.
- Chu, J. J. and M. Ng (2004) J. Biol. Chem. 279:54533.
Citations for Recombinant Mouse Integrin alpha V beta 3 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 3
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The RGD-binding integrins alphavbeta6 and alphavbeta8 are receptors for mouse adenovirus-1 and -3 infection
Authors: M Bieri, R Hendrickx, M Bauer, B Yu, T Jetzer, B Dreier, PRE Mittl, J Sobek, A Plückthun, UF Greber, S Hemmi
PloS Pathogens, 2021;17(12):e1010083.
Sample Types: Whole Cells
Nonimmune cell-derived ICOS ligand functions as a renoprotective alphavbeta3 integrin-selective antagonist
Authors: KH Koh, Y Cao, S Mangos, NJ Tardi, RR Dande, HW Lee, B Samelko, MM Altintas, VP Schmitz, H Lee, K Mukherjee, V Peev, DJ Cimbaluk, J Reiser, E Hahm
J. Clin. Invest., 2019;129(4):1713-1726.
Sample Types: Recombinant Protein
Applications: Surface Plasmon Resonance (SPR
Development of a Screening System for Targeting Carriers Using Peptide-Modified Liposomes and Tissue Sections
Authors: Y Negishi, N Hamano, H Sato, F Katagiri, K Takatori, Y Endo-Takah, Y Kikkawa, M Nomizu
Biol. Pharm. Bull., 2018;41(7):1107-1111.
Sample Types: Whole Tissue
What is the amino acid sequence of the acidic and basic tails?
Acidic and basic tails are added to the protein to help facilitate optimal activity. While we generally include sequence information on the product datasheet, the sequences of these tails are considered confidential information.
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