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  • 产品名称：CarboxypeptidaseA4(CPA4)(AA17-421)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
CarboxypeptidaseA4(CPA4)(AA17-421)(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 46.4 kDa. The protein migrates as 48 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 cleave the colorimetric peptide substrate Ac-Phe-Thiaphe-OH in the presence of 5,5'Dithio-bis (2-nitrobenzoic acid) (DTNB). The specific activity is >3000 pmol/min/μg.
Background Carboxypeptidases are zinc-containing exopeptidases that catalyze the release of carboxy-terminal amino acids, and are synthesized as zymogens that are activated by proteolytic cleavage. Carboxypeptidases cleave amino acids from the C-terminus of proteins and peptides and many are metalloproteases. Carboxypeptidase A4 (CPA4) is also known as Carboxypeptidase A3 (CPA3), which belongs to the peptidase M14 family. Fetal express the protein in the adrenal gland, brain, heart, intestine, kidney, liver and lung.
Molecular Weight 46.4 kDa
UniProt Q9UI42
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 50 mM Tris, 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 Carboxypeptidase A4 (CPA4) (AA 17-421) (Active) protein (His tag) (ABIN2180902) Human Carboxypeptidase A4, His Tag on SDS-PAGE under reducing (R) condition. The gel ...
Background publications Sánchez de Groot, Pallarés, Avilés, Vendrell, Ventura: "Prediction of "hot spots" of aggregation in disease-linked polypeptides." in: BMC structural biology, Vol. 5, pp. 18, 2005 (PubMed).

Pallarès, Bonet, García-Castellanos, Ventura, Avilés, Vendrell, Gomis-Rüth: "Structure of human carboxypeptidase A4 with its endogenous protein inhibitor, latexin." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 102, Issue 11, pp. 3978-83, 2005 (PubMed).

Huang, Reed, Zhang, Shridhar, Wang, Smith: "Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells." in: Cancer research, Vol. 59, Issue 12, pp. 2981-8, 1999 (PubMed).