Recombinant Human CD9-LEL Fc Chimera Protein, CF

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When Recombinant Human CD9 Fc Chimera (Catalog # 10015-CD) isimmobilized at 1 µg/mL, Biotinylated Recombinant CD81 Fc Chimera binds with anED50 of 2-10 μg/mL.
2 μg/lane of Recombinant Human CD9 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 38-42 kDa and 75-85 kDa, respectively.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human CD9-LEL Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human CD9 Fc Chimera is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human CD81 Fc Chimera binds with an ED50 of 2-10 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human CD9 protein
Human IgG1
MD + (Pro100-Lys330)
IEGR Human CD9-LEL
(Ser112-Ile195)
Accession # P21926
N-terminusC-terminus
Accession #
N-terminal Sequence
MD + Pro100
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Purity Statement
Antigen Affinity-purified
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
36.3 kDa.
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
38-42 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 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °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 500 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 CD9-LEL Fc Chimera Protein, CF

  • BA2
  • BA-2/p24 antigen
  • BTCC-1
  • CD9 antigen
  • CD9 molecule
  • CD9
  • Cell growth-inhibiting gene 2 protein
  • DRAP-27
  • Leukocyte antigen MIC3
  • MIC3
  • motility related protein-1,5H9 antigen
  • Motility-related protein
  • MRP-1FLJ99568
  • p24
  • tetraspanin-29
  • TSPAN29
  • TSPAN-29
  • TSPAN29MIC3CD9 antigen (p24)

Background

CD9, also known as Tspan29, is a 24-27 kDa cell surface protein belonging to the tetraspanin family (1). Common to other tetraspanins, CD9 is composed of four transmembrane domains, short N- and C-terminal cytoplasmic domains, and two extracellular loops. The larger extracellular loop, referred to as the LEL or EC2, contains highly conserved CCG and PXSC motifs (2, 3). The LEL mediates noncovalent protein-protein interactions, allowing tetraspanins to associate with each other as well as signaling molecules, structural proteins, and G-protein coupled receptors (4-6). Human CD9 is expressed in multiple cell and tissue types and has been identified in diverse biological roles due to its involvement in the formation of tetraspanin-enriched microdomains (TEMs). TEMs are associated with numerous processes ranging from cell adhesion and fusion, membrane trafficking, and endocytosis to leukocyte adherence and motility (4-7). These tetraspanin-enriched microdomains (TEMs) are associated with a wide range of functions from cell adhesion and fusion, membrane trafficking and endocytosis, and eukocyte adherence and motility. The LEL of human CD9 shares 77% and 84% amino acid sequence identity with mouse and rat CD9, respectively.  CD9 can form homodimers or interact with other proteins including CD117, CD29, CD46, CD49c, CD81, CD315, Tspan4, TGF-alpha , and HBEGF (1, 4, 8-13). Increased expression of CD9 has been shown to enhance transmembrane TGF-alpha -induced EGFR stimulation (1), and injection of human CD9 mRNA into CD9 knock-out mouse oocytes restored sperm-egg fusion (14). CD9-LEL may also be involved in the inhibition of multinucleated giant cell formation (3) as well as possess anti-adhesive effects against bacteria trying to invade mammalian cells (6, 15). CD9 interacts with integrins to regulate cell adhesion and motility (16-18). CD9 has been implicated in platelet activation and aggregation (17, 19). It may act as the terminal signal of myelination in the peripheral nervous system and can regulate the formation of paranodal junctions (20). Also, it has been suggested CD9 plays an important role both in the self-antigen and recall antigen-induced T cell activation (21).
  1. Shi, W. et al. (2000) J. Cell Biol. 148:591.
  2. Hemler, M. (2003) Annu Rev Cell Biol. 19:397.
  3. Hulme, R. et al. (2014) PLoS One 9:e116289.
  4. Stipp, C. et al. (2003) Trends Biochem Sci. 28:106.
  5. Barreiro, O. et al. (2005) Blood 105:2852.
  6. Ventress, J. et al. (2016) PLoS One 11:e0160387.
  7. Rubinstein, E. (2011) Biochem Soc Trans. 39:501.
  8. Anzai, N. et al. (2002) Blood 99:4413.
  9. Radford, K. et al. (1996) Biochem. Biophys. Res. Commun. 222:13.
  10. Lozahic, S. et al. (2000) Eur. J. Immunol. 30:900.
  11. Park, K. et al. (2000) Mol. Hum. Reprod. 6:252.
  12. Charrin, S. et al. (2001) J. Biol. Chem. 276:14329.
  13. Tachibana, I. et al. (1997) J. Biol. Chem. 272:29181.
  14. Zhu, G. et al. (2002) Development 129:1995.
  15. Green, L. et al. (2011) Infect Immun. 79:2241.
  16. Powner, D. et al. (2011) Biochem. Soc. Trans. 39:563.
  17. Detchokul, S. et al. (2014) British Journal of Pharmacology 171:5462.
  18. Reyes, R. et al. (2018) Front. Immunol. 9:863.
  19. Slupsky, J. et al. (1989) J Biol chem. 264:12289.
  20. Ishibashi, T. et al. (2004) J. Neuroscience 24:96.
  21. Kobayashi, H. et al. (2004) Clin Exp Immunol. 137:101.

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