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Mouse Anti-CD9 Recombinant Antibody (1) (CBMAB-C0034-LY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
1
Antibody Isotype
IgG1
Application
ELISA, ICC/IF, FC

Basic Information

Immunogen
Recombinant Human CD9 protein.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
ELISA1:1,000-1:2,000
IF(ICC)1:50-1:1,000
FC1:25-1:100

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Preservative
None
Concentration
Batch dependent
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
CD9 Molecule
Introduction
CD9 (CD9 Molecule) is a Protein Coding gene. Diseases associated with CD9 include Cytomegalovirus Retinitis and Diphtheria. Among its related pathways are Response to elevated platelet cytosolic Ca2+ and Uptake and actions of bacterial toxins. Gene Ontology (GO) annotations related to this gene include integrin binding. An important paralog of this gene is TSPAN2.
Entrez Gene ID
928
UniProt ID
P21926
Alternative Names
CD9 Molecule; Cell Growth-Inhibiting Gene 2 Protein; Motility Related Protein-1; Leukocyte Antigen MIC3; CD9 Antigen (P24); Tetraspanin-29; 5H9 Antigen; CD9 Antigen; TSPAN-29; TSPAN29;
Function
Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:8478605, PubMed:14575715, PubMed:18541721).
Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity).
In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity).
In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480).
Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity).
Acts as a receptor for PSG17 (By similarity).
Involved in platelet activation and aggregation (PubMed:18541721).
Regulates paranodal junction formation (By similarity).
Involved in cell adhesion, cell motility and tumor metastasis (PubMed:8478605, PubMed:7511626).
Biological Process
Cell adhesion Source: UniProtKB
Cellular response to low-density lipoprotein particle stimulus Source: UniProtKB
Fusion of sperm to egg plasma membrane involved in single fertilization Source: UniProtKB
Glial cell migration Source: FlyBase
Myoblast fusion involved in skeletal muscle regeneration Source: UniProtKB
Negative regulation of cellular component movement Source: UniProtKB
Negative regulation of platelet aggregation Source: UniProtKB
Paranodal junction assembly Source: UniProtKB
Platelet activation Source: UniProtKB
Platelet degranulation Source: Reactome
Receptor internalization Source: UniProtKB
Sperm-egg recognition Source: UniProtKB
Cellular Location
Extracellular exosome; Cell membrane; Membrane. Present at the cell surface of oocytes. Accumulates in the adhesion area between the sperm and egg following interaction between IZUMO1 and its receptor IZUMO1R/JUNO.
Topology
Cytoplasmic: 2-12
Helical: 13-33
Extracellular: 34-55
Helical: 56-76
Cytoplasmic: 77-87
Helical: 88-111
Extracellular: 112-195
Helical: 196-221
Cytoplasmic: 222-228
PTM
Palmitoylated at a low, basal level in unstimulated platelets. The level of palmitoylation increases when platelets are activated by thrombin (in vitro). The protein exists in three forms with molecular masses between 22 and 27 kDa, and is known to carry covalently linked fatty acids (PubMed:11959120). Palmitoylation by ZDHHC2 regulates CD9 expression, association with other tetraspanin family proteins and function in cell adhesion (PubMed:18508921).
More Infomation

Milburn, J. V., Hoog, A. M., Winkler, S., van Dongen, K. A., Leitner, J., Patzl, M., ... & Gerner, W. (2021). Expression of CD9 on porcine lymphocytes and its relation to T cell differentiation and cytokine production. Developmental & Comparative Immunology, 121, 104080.

Mathieu, M., Névo, N., Jouve, M., Valenzuela, J. I., Maurin, M., Verweij, F. J., ... & Théry, C. (2021). Specificities of exosome versus small ectosome secretion revealed by live intracellular tracking of CD63 and CD9. Nature Communications, 12(1), 1-18.

Umeda, R., Satouh, Y., Takemoto, M., Nakada-Nakura, Y., Liu, K., Yokoyama, T., ... & Nureki, O. (2020). Structural insights into tetraspanin CD9 function. Nature communications, 11(1), 1-11.

Oosterheert, W., Xenaki, K. T., Neviani, V., Pos, W., Doulkeridou, S., Manshande, J., ... & Gros, P. (2020). Implications for tetraspanin-enriched microdomain assembly based on structures of CD9 with EWI-F. Life science alliance, 3(11).

Inoue, N., Saito, T., & Wada, I. (2020). Unveiling a novel function of CD9 in surface compartmentalization of oocytes. Development, 147(15), dev189985.

Xing, C., Xu, W., Shi, Y., Zhou, B., Wu, D., Liang, B., ... & Feng, J. (2020). CD9 knockdown suppresses cell proliferation, adhesion, migration and invasion, while promoting apoptosis and the efficacy of chemotherapeutic drugs and imatinib in Ph+ ALL SUP‑B15 cells. Molecular Medicine Reports, 22(4), 2791-2800.

Jankovicova, J., Secova, P., Manaskova-Postlerova, P., Simonik, O., Frolikova, M., Chmelikova, E., ... & Antalikova, J. (2019). Detection of CD9 and CD81 tetraspanins in bovine and porcine oocytes and embryos. International journal of biological macromolecules, 123, 931-938.

Brosseau, C., Colas, L., Magnan, A., & Brouard, S. (2018). CD9 tetraspanin: a new pathway for the regulation of inflammation?. Frontiers in immunology, 9, 2316.

Reyes, R., Cardeñes, B., Machado-Pineda, Y., & Cabañas, C. (2018). Tetraspanin CD9: a key regulator of cell adhesion in the immune system. Frontiers in immunology, 9, 863.

Machado-Pineda, Y., Cardeñes, B., Reyes, R., López-Martín, S., Toribio, V., Sánchez-Organero, P., ... & Cabañas, C. (2018). CD9 controls integrin α5β1-mediated cell adhesion by modulating its association with the metalloproteinase ADAM17. Frontiers in immunology, 9, 2474.

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For research use only. Not intended for any clinical use.

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