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-terminus | | C-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 |
|
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
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).
- Shi, W. et al. (2000) J. Cell Biol. 148:591.
- Hemler, M. (2003) Annu Rev Cell Biol. 19:397.
- Hulme, R. et al. (2014) PLoS One 9:e116289.
- Stipp, C. et al. (2003) Trends Biochem Sci. 28:106.
- Barreiro, O. et al. (2005) Blood 105:2852.
- Ventress, J. et al. (2016) PLoS One 11:e0160387.
- Rubinstein, E. (2011) Biochem Soc Trans. 39:501.
- Anzai, N. et al. (2002) Blood 99:4413.
- Radford, K. et al. (1996) Biochem. Biophys. Res. Commun. 222:13.
- Lozahic, S. et al. (2000) Eur. J. Immunol. 30:900.
- Park, K. et al. (2000) Mol. Hum. Reprod. 6:252.
- Charrin, S. et al. (2001) J. Biol. Chem. 276:14329.
- Tachibana, I. et al. (1997) J. Biol. Chem. 272:29181.
- Zhu, G. et al. (2002) Development 129:1995.
- Green, L. et al. (2011) Infect Immun. 79:2241.
- Powner, D. et al. (2011) Biochem. Soc. Trans. 39:563.
- Detchokul, S. et al. (2014) British Journal of Pharmacology 171:5462.
- Reyes, R. et al. (2018) Front. Immunol. 9:863.
- Slupsky, J. et al. (1989) J Biol chem. 264:12289.
- Ishibashi, T. et al. (2004) J. Neuroscience 24:96.
- Kobayashi, H. et al. (2004) Clin Exp Immunol. 137:101.
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