Human Carbonic Anhydrase II / CA2 Protein, His Tag

Source : 

Human CA2, His Tag (CA2-H5228) is expressed from human 293 cells (HEK293). It contains AA Met 1 - Lys 260 (Accession # NP_000058.1).

 

Molecule : Carbonic Anhydrase II

 

Synonyms : CA2,CA-II,CAII,Car2

 

Format : Powder

 

Category : Bio-Markers & CD Antigens

 

Accession : NP_000058.1

 

Storage : -20℃

 

Shipping condition : Powder,RT

 

Molecular Weight : 30.1 kDa

 

Characteristics :

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 30.1 kDa. The protein migrates as 31-33 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.

 

Buffer : 20 mM Tris, 150 mM NaCl, pH8.0

 

Description :

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes. CAs form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs rather slowly in the absence of a catalyst. One of the functions of the enzyme in animals is to interconvert carbon dioxide and bicarbonate to maintain acid-base balance in blood and other tissues, and to help transport carbon dioxide out of tissues. The active site of most carbonic anhydrases contains a zinc ion. They are, therefore, classified as metalloenzymes. There are at least five distinct CA families (α, β, γ, δ and ε). These families have no significant amino acid sequence similarity and in most cases are thought to be an example of convergent evolution. The α-CAs are found in humans.
Carbonic anhydrase II (CA2) is also known as Carbonate dehydratase II, Carbonic anhydrase C, is one of fourteen forms of human α carbonic anhydrases. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of sodium ions in the proximal tubule. Carbonic anhydrase II has been shown to interact with Band 3 and Sodium-hydrogen antiporter 1.

 

References :

(1) Badger MR, Price GD, 1994, Annu. Rev. Plant Physiol. Plant Mol. Bio. 45: 369–392.
(2) Nair, S. K. et al., 1991, The Journal of biological chemistry 266 (26): 17320–17325.
(3) Sterling, D., et al., 2001, J. Biol. Chem. (United States) 276 (51): 47886–94.
(4) Vince, J W., et al., 2000, Biochemistry (UNITED STATES) 39 (44): 13344–9.
(5) Li, Xiuju, et al., 2002, J. Biol. Chem. (United States) 277 (39): 36085–91.