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  • 产品名称：serpinPeptidaseInhibitor,CladeA(Alpha-1Antiproteinase,Antitrypsin),Member3(SERP

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  • 产品厂商：ACROBiosystems
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简单介绍：
serpinPeptidaseInhibitor,CladeA(Alpha-1Antiproteinase,Antitrypsin),Member3(SERPINA3)(AA23-423)(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 46.6 kDa. The protein migrates as 55-70 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 ability to inhibit chymotrypsin cleavage of a fluorogenic peptide substrate MCA-RPKPVE-Nval-WRK(Dnp)-NH2. The IC50 value is <6 nm.="" <="" td="">
Background Serpin A3 is also known as Alpha-1-antichymotrypsin (ACT or AACT), Cell growth-inhibiting gene 24/25 protein, which belongs to the serpin family. Serpin A3 can bind DNA. Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.
Molecular Weight 46.6 kDa
UniProt P01011
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 HEPES, 150 mM NaCl, pH 7.5
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), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 3 (SERPINA3) (AA 23-423) (Active) protein (His tag) (ABIN2181746) Human Serpin A3, His Tag on SDS-PAGE under reducing (R) condition. The gel was staine...
Background publications Liu, Qian, Gritsenko, Camp, Monroe, Moore, Smith: "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." in: Journal of proteome research, Vol. 4, Issue 6, pp. 2070-80, 2005 (PubMed).

Kroczynska, Evangelista, Samant, Elguindi, Blond: "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity." in: The Journal of biological chemistry, Vol. 279, Issue 12, pp. 11432-43, 2004 (PubMed).

Rubin, Wang, Nickbarg, McLarney, Naidoo, Schoenberger, Johnson, Cooperman: "Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins." in: The Journal of biological chemistry, Vol. 265, Issue 2, pp. 1199-207, 1990 (PubMed).