Carbonic Anhydrase IX (Renal Cell Marker) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone CA9/781 ]
|Application ||WB, IHC, IF, FC|
|Other Accession||768, 63287|
|Isotype||Mouse / IgG2b, kappa|
|Other Names||Carbonic anhydrase 9, 184.108.40.206, Carbonate dehydratase IX, Carbonic anhydrase IX, CA-IX, CAIX, Membrane antigen MN, P54/58N, Renal cell carcinoma-associated antigen G250, RCC-associated antigen G250, pMW1, CA9, G250, MN|
|Storage||Store at 2 to 8°C.Antibody is stable for 24 months.|
|Precautions||Carbonic Anhydrase IX (Renal Cell Marker) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.|
|Cellular Location||Nucleus. Nucleus, nucleolus. Cell membrane; Single-pass type I membrane protein. Cell projection, microvillus membrane; Single-pass type I membrane protein. Note=Found on the surface microvilli and in the nucleus, particularly in nucleolus|
|Tissue Location||Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa|
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Provided below are standard protocols that you may find useful for product applications.
Recognizes a glycoprotein of ~200kDa, identified as carbonic anhydrase IX (CAIX/gp200). Carbonic Anhydrases (CAs) are members of a large family of zinc metallo-enzymes that catalyze the reversible hydration of carbon dioxide. CAs are involved in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption and the formation of aqueous humor, cerebrospinal fluid, saliva and gastric juice. They show extensive diversity in distribution and in their subcellular localization. CA IX is specifically expressed in clear-cell renal carcinomas.
Sly, W.S., et al. 1995. Human Carbonic Anhydrases and Carbonic Anhydrase deficiencies. Annu. Rev. Biochem. 64: 375-401
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