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P6056

Sigma-Aldrich

Endoproteinase Arg-C from mouse submaxillary gland

suitable for protein sequencing, lyophilized powder

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.56

form

lyophilized powder

packaging

vial of 5 μg

suitability

suitable for protein sequencing

storage temp.

−20°C

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Application

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.

Biochem/physiol Actions

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.

Unit Definition

One unit will hydrolyze 1.0 μmole of Nα-p-tosyl-L-arginine methyl ester per min at pH 8.0 at 25 °C.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

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J R Casas-Finet et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(3), 1050-1054 (1992-02-01)
To identify the functional residues of the N-terminal B region of bacteriophage T4 gene 32 protein involved in its cooperative binding to single-stranded nucleic acids, a process dependent on homotypic protein-protein interaction, we have studied the interaction of the protein
Proteomics in Functional Genomics: Protein Structure Analysis (2000)
Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.
Shirato K, et al.
Journal of Virology, 87, 12552-12552 (2013)
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)

Protocols

An optimized LC-MS/MS based workflow for low artifact tryptic digestion and peptide mapping of monoclonal antibody, adalimumab (Humira) using filter assisted sample preparation (FASP).

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