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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

Quality Level

200

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
J C Neagle et al.
The Biochemical journal, 278 ( Pt 2), 423-427 (1991-09-01)
Selective proteolysis of the protein X subunit of native bovine heart pyruvate dehydrogenase complex may be accomplished without loss of overall complex activity. Partial loss of function occurs if Mg2+ and thiamin pyrophosphate are not present during proteinase arg C
Nikki R Rhodin et al.
Infection and immunity, 72(8), 4680-4688 (2004-07-24)
Monoclonal antibody (MAb) 6-11A directed against Streptococcus mutans surface adhesin P1 was shown previously to influence the mucosal immunogenicity of this organism in BALB/c mice. The specificity of anti-P1 serum immunoglobulin G (IgG) and secretory IgA antibodies and the subclass
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
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