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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:
82047-85-6
Enzyme Commission number:
3.4.21.35 (BRENDA, IUBMB)
EC Number:
279-893-6
MDL number:
MFCD01324999
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
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

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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Analysis of endoproteinase Arg C action on adrenocorticotrophic hormone by capillary electrophoresis and reversed-phase high-performance liquid chromatography.
Krueger RJ, et al.
Journal of Chromatography A, 543, 451-461 (1991)
Leesa J Deterding et al.
Journal of proteome research, 7(6), 2368-2379 (2008-04-18)
Global changes in the phosphorylation state of human H1 isoforms isolated from UL3 cells have been investigated using mass spectrometry. Relative changes in H1 phosphorylation between untreated cells and cells treated with dexamethasone or various CDK inhibitors were determined. The
P I Bastiaens et al.
Proceedings of the National Academy of Sciences of the United States of America, 93(16), 8407-8412 (1996-08-06)
We have devised a microspectroscopic strategy for assessing the intracellular (re)distribution and the integrity of the primary structure of proteins involved in signal transduction. The purified proteins are fluorescent-labeled in vitro and reintroduced into the living cell. The localization and
Proteomics in Functional Genomics: Protein Structure Analysis (2000)
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)
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