anti-human CD9, Biotin-conjugated, Clone HI9a
Description
CD9 belongs to proteins of tetraspanin family that orchestrate cholesterol-associated tetraspanin- enriched signaling microdomains within the plasma membrane, forming complexes with each other as well as with integrins, membrane-anchored growth factors and other proteins. CD9 is involved in cell motility, osteoclastogenesis, neurite outgrowth, myotube formation, and sperm-egg fusion, plays roles in cell attachment and proliferation and is necessary for association of heterologous MHC II molecules on the dendritic cell plasma membrane which is important for effective T cell stimulation. CD9 is also considered as metastasis suppressor in solid tumors.
Properties
The monoclonal antibody ADG5007/L (clone HI9a) is a murine monoclonal antibody, subclass IgG1 recognizing human CD9. The antibody has been purified from cell culture supernatant using Protein G affinity chromatography.
The purified antibody is conjugated with Biotin-LC-NHS under optimum conditions. The reagent is free of unconjugated biotin.
Specificity
The antibody HI9a 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 tivated T lymphocytes.
Presentation
Vial containing 50 µg /100 µl (ADG5007) or 150 µg/300 ml (ADG5007L) of purified antibody in PBS containing 0.09 % sodium azide (pH 7.2). The IgG concentration is 0.5 mg/ml. Spin the vial briefly before opening.
Storage and Stability
Store at 4 °C. For long-term storage aliquot and store at -20°C. It is recommended to avoid freeze-thaw cycles. The reagent is stable until the expiry date stated on the vial label.
Applications
Flow Cytometry
Immunohistochemistry (acetone-fixed frozen sections)
Category: Research use only
Type: Antibody
Product Availability: Worldwide
Manufacturer: ImmBioMed GmbH & Co KG, Germany
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anti-human CD9, Biotin-conjugated, Clone HI9a
Cat.No. ADG5007L
Article no.: 938258
Unit: 150 µg
Code: ADG5007L
Manufacturer: ImmBioMed GmbH & Co. KG
References
- Haematologica. 2015 Jun;100(6):757-67. doi: 10.3324/haematol.2014.118497. Epub 2015 Apr 3.
Tetraspanin CD9 participates in dysmegakaryopoiesis and stromal interactions in primary myelofibrosis.
Desterke C, Martinaud C, Guerton B, Pieri L, Bogani C, Clay D, Torossian F, Lataillade JJ, Hasselbach HC, Gisslinger H, Demory JL, Dupriez B, Boucheix C, Rubinstein E, Amsellem S, Vannucchi AM, Le Bousse-Kerdilès MC.
The authors analyzed whether CD9 participates in the dysmegakaryopoiesis observed in patients with primary myelofibrosis. They asked, whether CD 9 is involved in the altered interplay between megakaryocytes and stromal cells. Their results indicate that CD9 plays a role in the dysmegakaryopoiesis that occurs in primary myelofibrosis and affects interactions between megakaryocytes and bone marrow stromal cells.
- Thromb Res. 1999 Sep 1;95(5):215-27.
Studies on the dual effects on platelets of a monoclonal antibody to CD9, and on the properties of platelet CD9.
Inngjerdingen M, Waterhouse K, Solum NO.
The authors found that binding of anti CD9 antibody to platelets exerts a dual action on human platelets in plasma depending on whether the complement system can be activated or not, resulting either in membrane permeabilization or a true platelet aggregation. Moreover, CD9 was found to be present on the surface of microvesicles derived from calcium ionophore-treated platelets.
- Br J Haematol. 1997 Feb;96(2):275-86.
Analysis of CD9, CD32 and p67 signalling: use of degranulated platelets indicates direct involvement of CD9 and p67 in integrin activation.
Slupsky JR, Cawley JC, Kaplan C, Zuzel M.
The authors found that, like intact cells, degranulated platelets can be activated and induced to aggregate by monoclonal antibodies against a 67 kD membrane protein (also known as PTA1) and CD9, and by crosslinked CD32 (Fcgamma-RII). They take their findings to suggest that the function of both CD9 and PTA1 antigen is closely associated with gpIIb/IIIa activation.
- Leukocyte Typing VI. Kishimoto T. et al. (Eds.), Garland Publishing Inc. (1997).
- Schlossman S., L. Bloumsell, W. Gilks, et al., eds. 1995. Leucocyte Typing Ⅴ: White Cell Differentiation