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Key Documents

SAB4700094

Sigma-Aldrich

Monoclonal Anti-CD9-Biotin antibody produced in mouse

clone MEM-61, purified immunoglobulin, buffered aqueous solution

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

biotin conjugate

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

MEM-61, monoclonal

Forme

buffered aqueous solution

Espèces réactives

human

Concentration

1 mg/mL

Technique(s)

flow cytometry: suitable

Isotype

IgG1

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

2-8°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... CD9(928)

Description générale

Cluster of differentiation 9 (CD 9) molecule, a member of transmembrane 4 super family (TM4SF) or tetraspanin superfamily, possesses four transmembrane domain. In human chromosome, the gene CD9 is localized on 12p13.31. The antibody MEM-61 recognizes an epitope on second extracellular domain (EC2) of CD9 antigen, a 24 kDa transmembrane protein expressed on platelets, monocytes, pre-B lymphocytes, granulocytes and activated T lymphocytes.

Immunogène

Pre-B cell line NALM-6

Application

The reagent is designed for Flow Cytometry analysis. Suggested working dilution is 1:400. Indicated dilution is recommended starting point for use of this product. Working concentrations should be determined by the investigator.

Actions biochimiques/physiologiques

Functions of cluster of differentiation 9 (CD9) molecule (CD9) include cell proliferation, activation, motility, and metastasis of tumor cells. CD9 along with CD81 is implicated to play a key role in muscle cell fusion and myotube maintenance. CD9 is associated with Interleukin 16 (IL-16) and induces migration and activation of mast cells. CD9 is involved in megakaryopoiesis. CD9 is expressed in Cord Blood CD34+ cells and might play a key role in hematopoietic stem cell (HSC) homing. CD9 associates with β1 integrin, membrane type 1−matrix metalloproteinase (MT1-MMP) and CD26 for HSC motility and homing. CD9 is crucial for sperm-egg fusion during fertilization. CD9 is a key molecule for glycoprotein 130 (gp130) mediated tumorigenic signal transduction in glioblastoma and a potential target for therapy.

Caractéristiques et avantages

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Forme physique

Solution in phosphate buffered saline, pH 7.4, with 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

Human and mouse mast cells use the tetraspanin CD9 as an alternate interleukin-16 receptor
Qi JC, et al.
Blood, 107(1), 135-142 (2006)
The tetraspanin CD9 regulates migration, adhesion, and homing of human cord blood CD34+ hematopoietic stem and progenitor cells
Leung KT, et al.
Blood, 117(6), 1840-1850 (2011)
The gamete fusion process is defective in eggs of Cd9-deficient mice
Kaji K, et al.
Nature Genetics, 24(3), 279-282 (2000)
Genomic deletion of chromosome 12p is an independent prognostic marker in prostate cancer
Kluth M, et al.
Oncotarget, 6(29), 27966-27979 (2015)
Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
Tachibana I and Hemler ME
The Journal of Cell Biology, 146(4), 893-904 (1999)

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