Recombinant Mouse Integrin alpha X beta 2 Protein, CF Summary
|Mouse Integrin alpha X
Accession # Q9QXH4
|His-Pro||GGGSGGGS||Acidic Tail||6-His tag|
|Mouse Integrin beta 2
Accession # P11835
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 100 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. 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 X beta 2
Integrin alpha X beta 2, also called CD11c/CD18, p150/95 or complement receptor type 4 (CR4), is one of four beta 2 integrins. The non-covalent heterodimer of 150 kDa alpha X/CD11c and 95 kDa beta 2/CD18 integrin subunits is commonly used as a marker for dendritic cells (DC) and classically activated macrophages (M1), but is also expressed on hairy cell leukemias, with lower amounts on other myeloid cells and activated B, NK and some cytotoxic T cells (1‑7). Inflammation enhances surface expression of alpha X beta 2 in states such as obesity (adipose DC), asthma (lung DC) and hypertriglyceridemia (circulating monocytes), increasing the adhesive capacity of the cells and contributing to pathology (8‑10). The alpha X vWFA or I‑domain, which contains the adhesion sites, forms the N‑terminal head region with the alpha X beta-propeller and the beta 2 vWFA domain (1, 11). Like other integrins, alpha X beta 2 has multiple activation states (3). In the presence of divalent cations and "inside-out" signaling, alpha X beta 2 is fully active and extended. In the inactive state, the heterodimer flexes in the center at the alpha X thigh and calf domains and beta 2 I‑EGF domains, impeding access to adhesion sites (1). The 1097 aa mouse alpha X/CD11c ECD shares 87% aa sequence identity with rat, and 71‑73% with human, canine and equine alpha X, while the 679 aa mouse beta 2/CD18 ECD shares 91% aa sequence identity with rat, and 80-82% with human, bovine, canine, and porcine beta 2 ECD. Active alpha X beta 2 shares some adhesion partners with alpha M beta 2/CD11b/CD18, including complement opsonin fragment iC3b, ICAMs, vWF and fibrinogen, and is expressed on many of the same cells (4-14). However, alpha M beta 2 activity is often constitutive, while alpha X beta 2 activity requires cell activation (4-7). alpha X beta 2 also binds osteopontin, Thy-1, plasminogen, heparin, and proteins with abnormally exposed acidic residues (14-18). The adhesion events are important for proliferation, degranulation, chemotactic migration, and phagocytosis of complement-opsonized particles (5, 6, 12, 14, 15). Mutations of beta 2, especially in the vWFA domain, cause leukocyte adhesion deficiency (LAD-1) and susceptibility to bacterial infections (19).
- Corbi, A.L. et al. (1987) EMBO J. 6:4023.
- Kishimoto, T.K. et al. (1987) Cell 48:681.
- Hynes, R.O. (2002) Cell 110:673.
- Arnaout, M.A. (1990) Blood 75:1037.
- Postigo, A.A. et al. (1991) J. Exp. Med. 174:1313.
- Beyer, M. et al. (2005) Respir. Res. 6:70.
- Nicolaou, F. et al. (2003) Blood 101:4033.
- Stefanovic-Racic, M. et al. (2012) Diabetes 61:2330.
- Gower, R.M. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:160.
- van Rijt, L.S. et al. (2005) J. Exp. Med. 201:981.
- Vorup-Jensen, T. et al. (2003) Proc. Natl. Acad. Sci. USA 100:1873.
- Bilsland, C.A.G. et al. (1994) J. Immunol. 152:4582.
- Pendu, R. et al. (2006) Blood 108:3746.
- Sadhu, C. et al. (2007) J. Leukoc. Biol. 81:1395.
- Schack, L. et al. (2009) J. Immunol. 182:6943.
- Choi, J. et al. (2005) Biochem. Biophys. Res. Commun. 331:557.
- Gang, J. et al. (2007) Mol. Cells 24:240.
- Vorup-Jensen, T. et al. (2007) J. Biol. Chem. 282:30869.
- Kishimoto, T.K. et al. (1987) Cell 50:193.
Citation for Recombinant Mouse Integrin alpha X beta 2 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
CD147 is a Novel Interaction Partner of Integrin &alphaM&beta2 Mediating Leukocyte and Platelet Adhesion
Authors: D Heinzmann, M Noethel, SV Ungern-Ste, I Mitroulis, M Gawaz, T Chavakis, AE May, P Seizer
Sample Types: Cell Culture Supernates
Applications: ELISA Capture
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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