Recombinant Mouse Integrin alpha V beta 1 Protein, CF Summary
|Mouse Integrin alpha V
Accession # P43406
|HP||GS Linker||Acidic Tail||HHHHHH|
|Mouse Integrin beta 1
Accession # P09055
|His||GS Linker||Basic Tail|
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 1
Integrin alpha V beta 1 is one of five alpha V and twelve beta 1 containing Integrin family adhesion receptor heterodimers (1‑3). The non‑covalent heterodimer of 170 kDa alpha V and 130 kDa beta 1/CD29 is present on cells that express both subunits, and dimer formation is dependent on the availability of the individual subunits (4). Since the alpha V and beta 1 subunits are widely expressed, the alpha V beta 1 heterodimer potentially forms in many cell types. The 958 aa mouse alpha V extracellular domain (ECD) shares 92‑95% aa sequence identity with human and bovine alpha V, while the 708 aa mouse beta 1 ECD shares 98% aa identity with rat and 93‑94% aa identity with human, bovine, porcine, ovine, canine and feline beta 1. The alpha V ECD contains an N‑terminal beta ‑propeller structure, followed by domains termed thigh, calf‑1 and calf‑2 (1). The beta 1 ECD contains a vWFA domain, which participates in binding. Each subunit then has a transmembrane sequence and a short cytoplasmic tail. The dimer is folded when it is least active. Divalent cations and intracellular (inside‑out) signaling convert it to its most active, extended and open conformation (1). alpha V integrins bind ligands that contain an RGD motif, including vitronectin, fibronectin and osteopontin (4‑9). The relatively weak binding affinity of alpha V beta 1 to vitronectin and fibronectin is thought to facilitate its activity in cyclic binding and release during cell migration (4, 5). In oligodendrocytes, astrocytes and pancreatic beta cells, alpha V beta 1 is expressed early in differentiation when cells are migrating and is down‑regulated when differentiation is complete (5‑7). alpha V beta 1 has also been found to be a receptor for angiopoietin‑2 in Tie2‑deficient glioma cells, and to mediate cell entry of viruses such as foot‑and‑mouth disease virus and human metaneumovirus (10‑12).
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- Hu, B. et al. (2006) Cancer Res. 66:775.
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- Cseke, G. et al. (2009) Proc. Natl. Acad. Sci. USA 106:1566.
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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