Recombinant Human Integrin alpha V beta 8 Protein, CF

Catalog # Availability Size / Price Qty
4135-AV-050
Graph showing bioactivity of Human Integrin alpha V beta 8 protein
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Citations (5)
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Recombinant Human Integrin alpha V beta 8 Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human Integrin  alpha V beta 8 at 2 µg/mL can bind recombinant human Lap with an apparent Kd <0.5 nM.
Source
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha V beta 8 protein
Human Integrin alpha V
(Phe31-Val992)
Accession # NP_002201.1
His-Pro GGGSGGGS Acidic Tail
Human Integrin beta 8
(Glu43-Arg684)
Accession # P26012.1
His-Pro GGGSGGGS Basic Tail
N-terminus C-terminus
N-terminal Sequence
Analysis
Phe31 ( alpha V subunit) & Glu43 ( beta 8 subunit)
Predicted Molecular Mass
110.5 kDa ( alpha V subunit), 75.3 kDa ( beta 8 subunit)
SDS-PAGE
130-155 kDa and 85-100 kDa, reducing conditions

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4135-AV

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

4135-AV

Formulation Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and MgCl2.
Reconstitution Reconstitute at 100 μg/mL in sterile 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.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 2 weeks, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Data Image

Bioactivity Bioactivity of Human Integrin  alpha V beta 8 View Larger

Recombinant human Integrin alpha V beta 8 (4135-AV) binds recombinant human LAP (246-LP) in a functional ELISA. The estimated Kd for this interaction is < 0.5 nM.

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Background: Integrin alpha V beta 8

Integrin alpha V beta 8 is one of five alpha V integrins and the only known beta 8 integrin (1-3). The non-covalent heterodimer of 170 kDa alpha V and ~90 kDa beta 8 integrin type I transmembrane glycoprotein subunits is expressed in yolk sac, placenta, brain perivascular astrocytes, Schwann cells, renal glomerular mesangial cells and pulmonary epithelial cells (3-7). Unlike other alpha V integrins, alpha V beta 8 does not appear to assume different activation states, and the cytoplasmic tail does not connect to the cytoskeleton (3, 8). It binds ligands containing an RGD motif, including vitronectin, fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex (7-12). High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP, which releases active TGF-beta. This mechanism differs from that of alpha V beta 6, the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms (13). Downstream effects of TGF-beta activation include control of cell growth and associated vascularization (10-13). Deletion of either alpha V or  beta 8 reveals that alpha V beta 8 is required for vascular morphogenesis in the embryonic brain and yolk sac (4, 14, 15). The 962 aa human alpha V extracellular domain (ECD) shares 92-95% aa sequence identity with mouse, rat and cow alpha V, while the 642 aa human beta 8 ECD shares 92%, 92%, 89%, 87% and 87% aa identity with cow, dog, rabbit, mouse and rat beta 8, respectively. The beta 8 ECD of beta 8 shows low (~35%) aa identity with other integrin beta subunits, and the cytoplasmic tail is unlike any other integrin. The alpha V ECD contains an N-terminal beta - propeller structure, followed by domains termed thigh, calf-1 and calf-2 (1). The beta 8 ECD contains a vWFA domain, which interacts with the alpha V beta -propeller to form a binding domain. Each subunit has a transmembrane sequence and a short cytoplasmic tail.

References
  1. Hynes, R. O. (2002) Cell 110:673.
  2. Suzuki, S. et al. (1987) J. Biol. Chem. 262:14080.
  3. Moyle, M. et al. (1991) J. Biol. Chem. 266:19650.
  4. Zhu, J. et al. (2002) Development 129:2891.
  5. Cambier, S. et al. (2000) Cancer Res. 60:7084.
  6. Lakhe-Reddy, S. et al. (2006) J. Biol. Chem. 281:19688.
  7. Chernousov, M. A. and D. J. Carey (2003) Exp. Cell Res. 291:514.
  8. Nishimura, S. L. et al. (1994) J. Biol. Chem. 269:28708.
  9. Milner, R. et al. (1999) J. Cell Sci. 112:4271.
  10. Cambier, S. et al. (2005) Am. J. Pathol. 166:1883.
  11. Fjellbirkeland, L. et al. (2003) Am. J. Pathol. 163:533.
  12. Araya, J. et al. (2006) Am. J. Pathol. 169:405.
  13. Mu, D. et al. (2002) J. Cell Biol. 157:493.
  14. Proctor, J. M. et al. (2005) J. Neurosci. 25:9940.
  15. McCarty, J. H. et al. (2005) Development 132:165.
Entrez Gene IDs
3685 (Human)
Alternate Names
Integrin alpha V beta 8

Citations for Recombinant Human Integrin alpha V beta 8 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.

5 Citations: Showing 1 - 5
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  1. Integrin &alphav&beta8 on T�cells suppresses anti-tumor immunity in multiple models and is a promising target for tumor immunotherapy
    Authors: E Dodagatta-, HY Ma, B Liang, J Li, DS Meyer, SY Chen, KH Sun, X Ren, B Zivak, MD Rosenblum, MB Headley, L Pinzas, NI Reed, JS Del Cid, BC Hann, S Yang, A Giddabasap, K Noorbehesh, B Yang, J Dal Porto, T Tsukui, K Niessen, A Atakilit, RJ Akhurst, D Sheppard
    Cell Reports, 2021;36(1):109309.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  2. 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;17(12):e1010083.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. The TGF-? inhibitory activity of antibody 37E1B5 depends on its H-CDR2 glycan
    Authors: Lynne A Murray
    MAbs, 2016;0(0):0.
    Species: Mouse
    Sample Types: Protein
    Applications: Bioassay
  4. Oxidation-induced structural changes of ceruloplasmin foster NGR motif deamidation that promotes integrin binding and signaling.
    Authors: Barbariga, Marco, Curnis, Flavio, Spitaleri, Andrea, Andolfo, Annapaol, Zucchelli, Chiara, Lazzaro, Massimo, Magnani, Giuseppe, Musco, Giovanna, Corti, Angelo, Alessio, Massimo
    J Biol Chem, 2014;289(6):3736-48.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. Critical role of flanking residues in NGR-to-isoDGR transition and CD13/integrin receptor switching.
    Authors: Curnis F, Cattaneo A, Longhi R, Sacchi A, Gasparri AM, Pastorino F, Di Matteo P, Traversari C, Bachi A, Ponzoni M, Rizzardi GP, Corti A
    J. Biol. Chem., 2010;285(12):9114-23.
    Species: Human
    Sample Types: Peptide
    Applications: Binding Assay

FAQs

  1. 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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