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Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY)


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Published Data
CBMAB-AP1330LY-1
Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY) in WB
Western blotting of the exosomal markers CD9, CD81, CD63 and syntenin in lysates from purified HUVEC EVs and cells from mono- and coculture conditions. ...View More
Njock, M. S., O'Grady, T., Nivelles, O., Lion, M., Jacques, S., Cambier, M., ... & Struman, I. (2022). Endothelial extracellular vesicles promote tumour growth by tumour-associated macrophage reprogramming. Journal of extracellular vesicles, 11(6), e12228.
Distributed under Open Access license CC BY 4.0, without modification.
CBMAB-AP1330LY-2
Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY) in WB
The expression of tetraspanins is shown in separate panels: CD9. ...View More
Grzanka, M., Stachurska-Skrodzka, A., Adamiok-Ostrowska, A., Gajda, E., & Czarnocka, B. (2022). Extracellular vesicles as signal carriers in malignant thyroid tumors?. International Journal of Molecular Sciences, 23(6), 3262.
Distributed under Open Access license CC BY 4.0, without modification.
CBMAB-AP1330LY-3
Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY) in WB
Western blotting of CD63, CD81 and CD9 in EC EVs, SMC EVs and cells. ...View More
Fontaine, M., Herkenne, S., Ek, O., Paquot, A., Boeckx, A., Paques, C., ... & Struman, I. (2021). Extracellular vesicles mediate communication between endothelial and vascular smooth muscle cells. International journal of molecular sciences, 23(1), 331.
Distributed under Open Access license CC BY 4.0, without modification.
CBMAB-AP1330LY-4
Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY) in WB
Characterisation of exosome-like vesicles released from serum by western blotting. Presence of exosomal markers, CD63, CD9, CD81 and mitochondrial protein cytochrome c in lysates from sera-derived exosomes and cell lysate. ...View More
Xu, J., Yin, Z., Yang, L., Wu, F., Fan, J., Huang, Q., ... & Yang, G. (2020). Evidence that dysplasia related microRNAs in Barrett's esophagus target PD-L1 expression and contribute to the development of esophageal adenocarcinoma. Aging (Albany NY), 12(17), 17062.
Distributed under Open Access license CC BY 4.0, without modification.
CBMAB-AP1330LY-5
Mouse Anti-CD9 Recombinant Antibody (P1/33/2) (CBMAB-AP1330LY) in Immunoblot
EVs were enriched by polyethylene glycol incubation and ultracentrifugation before subsequent purification and fractionation on an iodixanol density gradient. Equal volume was loaded for immunoblot analysis. One μg of cell lysate was run to demonstrate depletion of Calnexin in isolated EV fractions. Blots are representative images from at least three repeated independent experiments. ...View More
Cone, A. S., Hurwitz, S. N., Lee, G. S., Yuan, X., Zhou, Y., Li, Y., & Meckes, D. G. (2020). Alix and Syntenin-1 direct amyloid precursor protein trafficking into extracellular vesicles. BMC Molecular and Cell Biology, 21, 1-20.
Distributed under Open Access license CC BY 4.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
P1/33/2
Antibody Isotype
IgG1, κ
Application
WB, IP, IF

Basic Information

Immunogen
Common acute lymphoblastic leukemia.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500

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

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
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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