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  • 产品名称：CarbonicAnhydraseIX(CA9)(AA38-414)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
CarbonicAnhydraseIX(CA9)(AA38-414)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 41.2 kDa. The protein migrates as 53-54 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its esterase activity. The specific activity is measured with 1 mM 4-Nitrophenyl acetate and 2.5 μg enzyme at 400 nm in 100 μL of 12.5 mM Tris, 75 mM NaCl, pH 7.5 The specific activity is > 15 pmoles / min / μg.
Background 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. There are at least five distinct CA families (α, β, γ, δ and ε). Carbonic anhydrase 9 (CA9 / CAIX) is also known as Membrane antigen MN (MN), Renal cell carcinoma-associated antigen G250, which belongs to the alpha-carbonic anhydrase family. CA9 / CAIX with an optimal activity at pH 6.49. Reversible hydration of carbon dioxide. CA IX participates in pH regulation. CA9 may be involved in the control of cell proliferation and transformation. CA-IX appears to be a novel specific biomarker for a cervical neoplasia.
Molecular Weight 41.2 kDa
NCBI Accession NP_001207
UniProt Q16790
Research Area Cancer, Metabolism
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 20 mM MES, 100 mM NaCl, pH 6.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for Carbonic Anhydrase IX (CA9) (AA 38-414) (Active) protein (His tag) (ABIN2180677) Human Carbonic Anhydrase IX (38-414), His Tag on SDS-PAGE under reducing (R) conditio...
Background publications Vitale, Alterio, Innocenti, Winum, Monti, De Simone, Supuran: "Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-sulfamate adducts with isozymes II and IX as a platform for designing tight-binding, more isoform-selective inhibitors." in: Journal of medicinal chemistry, Vol. 52, Issue 19, pp. 5990-8, 2009 (PubMed).

Alterio, Hilvo, Di Fiore, Supuran, Pan, Parkkila, Scaloni, Pastorek, Pastorekova, Pedone, Scozzafava, Monti, De Simone: "Crystal structure of the catalytic domain of the tumor-associated human carbonic anhydrase IX." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, Issue 38, pp. 16233-8, 2009 (PubMed).

Hilvo, Baranauskiene, Salzano, Scaloni, Matulis, Innocenti, Scozzafava, Monti, Di Fiore, De Simone, Lindfors, Jänis, Valjakka, Pastoreková, Pastorek, Kulomaa, Nordlund, Supuran, Parkkila: "Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes." in: The Journal of biological chemistry, Vol. 283, Issue 41, pp. 27799-809, 2008 (PubMed).

Temperini, Innocenti, Guerri, Scozzafava, Rusconi, Supuran: "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I." in: Bioorganic & medicinal chemistry letters, Vol. 17, Issue 8, pp. 2210-5, 2007 (PubMed).

Yu, Price, Badger: "A Mutant Isolated from the Cyanobacterium Synechococcus PCC7942 Is Unable to Adapt to Low Inorganic Carbon Conditions." in: Plant physiology, Vol. 104, Issue 2, pp. 605-611, 2002 (PubMed).