추천 제품
애플리케이션
Endoproteinase Arg-C from mouse submaxillary gland has been used to study the syncytium formation in MERS-CoV (middle East respiratory syndrome coronavirus)-infected Vero cells in the presence of exogenous proteases. It has been used for the digestion of Rpl23ab (ribosomal protein L23ab)-containing fraction for LC-MS (liquid chromatography–mass spectrometry)/MS analysis.
생화학적/생리학적 작용
Endoproteinase Arg-C is a serine endoprotease from mouse submaxillary gland which hydrolyzes peptide bonds at the carboxyl side of arginyl residues. The enzyme has been shown to cleave Lys-Lys and Lys-Arg bonds, and all Arg-X bonds may not be hydrolyzed.
단위 정의
One unit will hydrolyze 1.0 μmole of Nα-p-tosyl-L-arginine methyl ester per min at pH 8.0 at 25 °C.
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
표적 기관
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
이미 열람한 고객
Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.
Shirato K, et al.
Journal of Virology, 87, 12552-12552 (2013)
Tanya R Porras-Yakushi et al.
The Journal of biological chemistry, 282(17), 12368-12376 (2007-03-01)
Ribosomal protein L23ab is specifically dimethylated at two distinct sites by the SET domain-containing enzyme Rkm1 in the yeast Saccharomyces cerevisiae. Using liquid column chromatography with electrospray-ionization mass spectrometry, we determined that Rpl23ab purified from the Deltarkm1 deletion strain demonstrated
Naoto Hoshi et al.
Molecular cell, 37(4), 541-550 (2010-03-02)
A-kinase anchoring proteins (AKAPs) coordinate cell signaling events. AKAP79 brings together different combinations of enzyme binding partners to customize the regulation of effector proteins. In neurons, muscarinic agonists mobilize an AKAP79-anchored pool of PKC that phosphorylates the KCNQ2 subunit of
Tanya R Porras-Yakushi et al.
The Journal of biological chemistry, 281(47), 35835-35845 (2006-09-29)
The ribosomal protein L12ab (Rpl12ab) in Saccharomyces cerevisiae is modified by methylation at both arginine and lysine residues. Although the enzyme responsible for the modification reaction at arginine 66 has been identified (Rmt2), the enzyme(s) responsible for the lysine modification(s)
Proteomics in Functional Genomics: Protein Structure Analysis (2000)
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