Recombinant Mouse Integrin alpha V beta 5 Protein, CF
Recombinant Mouse Integrin alpha V beta 5 Protein, CF Summary
Product Specifications
| Mouse Integrin alpha V (Phe31-Val988) Accession # P43406 |
HP | GS Linker | Acidic Tail | HHHHHH | |
| Mouse Integrin beta 5 (Gly24-Asn719) Accession # NP_001139356 |
HP | GS Linker | Basic Tail | ||
| N-terminus | C-terminus | ||||
Analysis
Product Datasheets
Carrier Free
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.
7706-AV
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 300 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.
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Reconstitution Calculator
Background: Integrin alpha V beta 5
Integrin alpha V beta 5 is one of five alpha V integrins and the only known beta 5 integrin (1‑3). The non‑covalent heterodimer of 170 kDa alpha V and 100‑110 kDa beta 5 integrin type I transmembrane glycoprotein subunits is expressed on a wide variety of cell types including keratinocytes, fibroblasts, adhesive monocytes, embryonic stem cells, and select endothelium and epithelium (4‑8). alpha V beta 5 binds ligands containing an RGD motif, notably vitronectin (1‑10). The 958 aa mouse alpha V extracellular domain (ECD) shares 92‑95% aa sequence identity with human and bovine alpha V, while the 696 aa mouse beta 5 ECD shares 97%, 91% and 91% aa sequence identity with rat, human and bovine beta 5, respectively. The alpha V ECD contains an N‑terminal beta ‑propeller structure, followed by domains termed thigh, calf‑1 and calf‑2 (1). The 799 aa beta 5 contains a vWFA domain within the ECD, which interacts with the alpha V beta ‑propeller to form a binding domain. Each subunit has a transmembrane sequence and a short cytoplasmic tail. Potential beta 5 isoforms include a 691 aa form with an alternate start site at aa 109, a 958 aa form with an alternate N‑terminus, and a 795 aa form with an alternate C‑terminus. Post‑translational modifications, such as proteolytic cleavage of the alpha V subunit or phosphorylation of the beta 5 cytoplasmic tail, can increase endocytic turnover of the alpha V beta 5 protein and/or promote cell migration (7‑10). Growth factors that increase PKC activity, such as VEGF or TGF‑ alpha, promote alpha V beta 5-mediated angiogenesis while alpha V beta 3, which may be expressed in the same cell, responds to FGF‑basic and TNF‑ alpha (11). An inhibitor of both down‑regulates tumor angiogenesis (12). During lung inflammation, up‑regulation of alpha V beta 5 on myofibroblasts or infiltrating lymphocytes may contribute to fibrosis by freeing TGF‑ beta from latency (13, 14). On retinal pigment epithelia, alpha V beta 5 is important for normal diurnal phagocytosis of outer rod segments, and contributes to adhesion of retinal cells (15).
- Hynes, R.O. (2002) Cell 110:673.
- Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.
- Suzuki, S. et al. (1990) Proc. Natl. Acad. Sci. USA 87:5354.
- Smith, J.W. et al. (1990) J. Biol. Chem. 265:11008.
- Pasqualini, R. et al. (1993) J. Cell Sci. 105:101.
- Braam, S.R. et al. (2008) Stem Cells 26:2257.
- Memmo, L.M. and P. McKeown-Longo (1998) J. Cell Sci. 111:425.
- Kim, J.P. et al. (1994) J. Biol. Chem. 269:26926.
- Berthet, V. et al. (2004) FEBS Lett. 557:159.
- Li, Z. et al. (2010) Mol. Biol. Cell 21:3317.
- Friedlander, M. et al. (1995) Science 270:1500.
- Desgrosellier, J.S. and D.A. Cheresh (2010) Nat. Rev. Cancer 10:9.
- Wipff, P.J. et al. (2007) J. Cell Biol. 179:1311.
- Luzina, I.G. et al. (2009) Arthritis Rheum. 60:1530.
- Nandrot, E.F. et al. (2004) J. Exp. Med. 200:1539.
Citation for Recombinant Mouse Integrin alpha V beta 5 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.
1 Citation: Showing 1 - 1
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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, 2021-12-15;17(12):e1010083.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
FAQs
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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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