Recombinant Human Integrin alpha X beta 2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Integrin alpha X beta 2 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support adhesion of J45.01 human acute lymphoblastic leukemia T lymphocytes. >50% of cells will adhere at 10 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Integrin alpha X beta 2 protein
Human Integrin alpha X
(Phe20-Pro1107)
Accession # P20702
Acidic Tail 6-His tag
Human Integrin beta 2
(Gln23-Asn700)
Accession # AAA59490
Basic Tail
N-terminus C-terminus
Accession #
N-terminal Sequence
Phe20 ( alpha X) & Gln23: predicted, no results obtained ( beta 2)
Protein/Peptide Type
Recombinant Proteins
Gene
ITGAX
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
128.9 kDa ( alpha X) & 83.1 kDa ( beta 2).
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
149 kDa & 103 kDa, 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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
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 X beta 2 Protein, CF

  • Integrin alpha X beta 2

Background

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 expressed on macrophages, dendritic cells and hairy cell leukemias, with lower amounts on other myeloid cells and activated B, NK and some cytotoxic T cells (1‑7). 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. 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, 8). 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 1088 aa human alpha X/CD11c ECD shares 70‑76% aa sequence identity with mouse, rat and canine alpha X while the 678 aa human beta 2/CD18 ECD shares 81‑83% aa sequence identity with mouse, rat, cow, dog, goat, sheep, and pig beta 2. Potential alpha X isoforms containing 719 and 725 aa (as compared to full-length 1163 aa alpha X) lack the vWFA domain and the N-terminus. 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 (4‑11). 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 (11‑16). The adhesion events are important for proliferation, degranulation, chemotactic migration, and phagocytosis of complement-opsonized particles (5, 6, 9, 11, 12, 16). Mutations of beta 2, especially in the vWFA domain, cause leukocyte adhesion deficiency (LAD-1) and susceptibility to bacterial infections (17).

  1. Corbi, A.L. et al. (1987) EMBO J. 6:4023.
  2. Kishimoto, T.K. et al. (1987) Cell 48:681.
  3. Hynes, R.O. (2002) Cell 110:673.
  4. Arnaout, M.A. (1990) Blood 75:1037.
  5. Postigo, A.A. et al. (1991) J. Exp. Med. 174:1313.
  6. Beyer, M. et al. (2005) Respir. Res. 6:70.
  7. Nicolaou, F. et al. (2003) Blood 101:4033.
  8. Vorup-Jensen, T. et al. (2003) Proc. Natl. Acad. Sci. USA 100:1873.
  9. Bilsland, C.A.G. et al. (1994) J. Immunol. 152:4582.
  10. Pendu, R. et al. (2006) Blood 108:3746.
  11. Sadhu, C. et al. (2007) J. Leukoc. Biol. 81:1395.
  12. Schack, L. et al. (2009) J. Immunol. 182:6943.
  13. Choi, J. et al. (2005) Biochem. Biophys. Res. Commun. 331:557.
  14. Gang, J. et al. (2007) Mol. Cells 24:240.
  15. Vorup-Jensen, T. et al. (2007) J. Biol. Chem. 282:30869.
  16. Vorup-Jensen, T. et al. (2004) Proc. Natl. Acad. Sci. USA 102:1614.
  17. Kishimoto, T.K. et al. (1987) Cell 50:193.

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