|Application ||WB, E|
|Calculated MW||29246 Da|
|Antigen Region||209-238 aa|
|Other Names||Carbonic anhydrase 2, Carbonate dehydratase II, Carbonic anhydrase C, CAC, Carbonic anhydrase II, CA-II, CA2|
|Target/Specificity||This CA2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 209-238 amino acids from the C-terminal region of human CA2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CA2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6.|
|Cellular Location||Cytoplasm. Cell membrane. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells|
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Provided below are standard protocols that you may find useful for product applications.
CA2 is one of several (at least 7) isozymes of carbonic anhydrase. The protein catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis.
Fisher,S.Z. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 (PT 5), 495-498 (2009)
Adamus,G. and Karren,L. J. Autoimmun. 32 (2), 133-139 (2009)
Hu,P.Y., Roth,D.E. Hum. Mutat. 1 (4), 288-292 (1992)
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