Mouse Anti-CD9 Recombinant Antibody (CBFYC-0053) (CBMAB-C0060-FY)

Name: Mouse Anti-CD9 Recombinant Antibody (CBFYC-0053)
SKU: CBMAB-C0060-FY
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-CD9 Recombinant Antibody (CBFYC-0053) (CBMAB-C0060-FY) in WB

Presence of CD9, calnexin, and heat shock protein 70 (Hsc/Hsp70) on exosomes were measured by Western blotting. ...View More

Aas, V., Øvstebø, R., Brusletto, B. S., Aspelin, T., Trøseid, A. M. S., Qureshi, S., ... & Haug, K. B. F. (2023). Distinct microRNA and protein profiles of extracellular vesicles secreted from myotubes from morbidly obese donors with type 2 diabetes in response to electrical pulse stimulation. Frontiers in Physiology, 14, 1143966.

Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CD9 Recombinant Antibody (CBFYC-0053) (CBMAB-C0060-FY) in WB

CD63, CD81 and CD9 expression in plasma-isolated exosomes from healthy volunteers (Lines 1-4) and polytrauma patients (Lines 5-7), Representative Western-blot analysis. ...View More

Weber, B., Henrich, D., Schindler, C. R., Marzi, I., & Leppik, L. (2023). Release of exosomes in polytraumatized patients: The injury pattern is reflected by the surface epitopes. Frontiers in immunology, 14, 1107150.

Distributed under Open Access license CC BY 4.0, without modification.

Mouse Anti-CD9 Recombinant Antibody (CBFYC-0053) (CBMAB-C0060-FY) in IF

Confocal microscopy to evaluate the relative expression of CD9, CD63, CD81, CD24, CD44, CD54, CD326 and CD340 membrane protein markers in the exosomes derived from MCF7, MDA-MB-231 and SKBr3 breast cancer cell lines. ...View More

Lima Moura, S., Martì, M., & Pividori, M. I. (2020). Matrix effect in the isolation of breast cancer-derived nanovesicles by immunomagnetic separation and electrochemical immunosensing-a comparative study. Sensors, 20(4), 965.

Distributed under Open Access license CC BY 4.0, without modification.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYC-0053

Application

FC, WB, IF

Immunogen

CD9 purified from HeLa cells.

Host Species

Mouse

Specificity

Human, Mouse

Antibody Isotype

IgG1

Clonality

Monoclonal Antibody

Application Notes

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Application	Note
WB	1 µg/ml

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

Format

Liquid

Buffer

PBS

Preservative

0.09% sodium azide

Concentration

0.5 mg/ml

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

More Infomation

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

Research Area

Cardiovascular

Function

Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:14575715, PubMed:18541721, PubMed:8478605).
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:7511626, PubMed:8478605).

Biological Process

Cell adhesion
Cell population proliferation
Cellular response to low-density lipoprotein particle stimulus
Fusion of sperm to egg plasma membrane involved in single fertilization
Glial cell migration
Myoblast fusion involved in skeletal muscle regeneration
Negative regulation of cell population proliferation
Negative regulation of platelet aggregation
Paranodal junction assembly
Platelet activation
Receptor internalization
Regulation of macrophage migration
Sperm-egg recognition

Cellular Location

Cell membrane
Membrane
Secreted, extracellular exosome
Note: 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).

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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

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