Recombinant Human Integrin alpha V beta 5 Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Vitronectin (Catalog # 2308-VN) is coated at 1 μg/mL, Recombinant Human Integrin alpha V beta 5 binds with an apparent KD <0.5 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha V beta 5 protein
Human Integrin alpha V (Phe31-Val992) Accession # P06756
His-Pro
GGGSGGGS
Acidic Tail
6-His tag
Human Integrin beta 5 (Gly24-Asn719) Accession # P18084
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
115.4 kDa ( alpha V subunit) & 84.8 kDa ( beta 5 subunit). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
100-155 kDa, reducing conditions
Publications
Read Publications using 2528-AV in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Integrin alpha V beta 5 Protein, CF
CD51
Integrin alpha V beta 5
integrin subunit alpha V
ITGAV
MSK8
VNRA
VTNR
Background
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 962 aa human alpha V extracellular domain (ECD) shares 92-95% aa sequence identity with mouse, rat and cow alpha V, while the 696 aa human beta 5 ECD shares 89%-93% aa identity with mouse, rat, bovine, equine, and canine beta 5. 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).
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