Recombinant Human Integrin alpha V beta 3 Fc Protein, CF

In a functional ELISA, Recombinant Human Integrin alpha V beta 3 Fc Chimera Protein (Catalog # 11648-AV) binds to Recombinant Human Vitronectin (2308-VN) with an ED50 of 60.0‑600 ng/mL.

2 μg/lane of Recombinant Human Integrin alpha V beta 3 Fc Chimera Protein (Catalog # 11648-AV) was resolved with SDS-PAGE under non-reducing (NR) condition and visualized by Coomassie® Blue staining, showing bands at >190 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Integrin alpha V beta 3 Fc Protein, CF Summary

• Additional Information: Fc Chimera
• Details of Functionality: Measured by its binding ability in a functional ELISA. Recombinant Human Integrin alpha V beta 3 Fc Chimera (Catalog # 11648-AV) binds to Recombinant Human Vitronectin (Catalog # 2308-VN) with an ED₅₀ of 60.0-600 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived human Integrin alpha V beta 3 protein
  

  Human ITGAV (Phe31-Val992) Accession # AAA36808.1	IEGR	Human IgG1 (Glu99-Lys330) (with modifications)
  Human ITGB3 (Gly27-Asp718) Accession # P05106.2	HPIEGR	Human IgG1 (Glu99-Lys330) (with modifications)
  N-terminus		C-terminus

• N-terminal Sequence: Phe 31 (Integrin alpha V) & Gly 27 (Integrin Beta 3)
• Structure / Form: Disulfide linked heterodimer
• Protein/Peptide Type: Recombinant Proteins
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 133 kDa (Integrin alpha V) & 103 kDa (Integrin beta 3).
  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: >190 kDa, under non-reducing conditions.

Packaging, Storage & Formulations

• Storage: 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 with Trehalose.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

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 3 Fc Protein, CF

• antigen identified by monoclonal L230
• CD51 antigen
• CD51
• Integrin alpha V beta 3
• integrin alpha-V
• integrin, alpha V (vitronectin receptor, alpha polypeptide, antigen CD51)
• MSK8
• Vitronectin receptor subunit alpha
• VNRADKFZp686A08142

Background

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 962 aa human alpha V ECD(11) shares 92‑95% aa sequence identity with mouse, rat and bovine  alpha V while the 685 aa human beta ₃ ECD(12) shares 95% aa identity with equine and canine, and 89‑92% aa identity with mouse, rat and porcine beta ₃. Two splice variants of beta 3 (b and c) diverge over the last 21 amino acids (aa) and lack cytoplasmic phosphorylation sites (5, 6). Another beta 3 splice variant diverges after the vWFA domain, producing a soluble 60 kDa form in platelets and endothelial cells (7). alpha V beta 3 is essential for the maturation of osteoclasts and their binding and resorption of bone; it also, however, promotes their apoptosis (8, 9). M‑CSF R and alpha V beta 3 share signaling pathways during osteoclastogenesis, and deletion of either molecule causes osteopetrosis (8, 9). 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 (13, 14). Also, cell entry of several viruses is mediated by alpha V beta 3 (4, 10).

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13. Somanath, P.R. et al. (2009) Angiogenesis 12:177.
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