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Arg-C, Enzymogenes

CAT: 0209-100-403-L100Size: 5x 20 µgDry Ice: NoHazardous: No
CAT#:0209-100-403-L100Size:5x 20 µg
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Description
Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants and by Co2+, Cu2+, Cd2+, and heavy metal ions. Recombinant Lysobacter Enzymogenes Arg-C is a 26.8 kDa protease consisting of 252 amino acid residues including a C-terminal His-Tag.
Synonyms
Proteolytic enzymes, peptidases, proteinases
UniProt
O87544
Accession Number
AAD11571.1
Accession Number mRNA
AF083621.1
Reactivity
Lysobacter
Label
His-Tag
Sequence
GVGDIGSSDY CEKDIVCRVK PSAEFLSASK SVARMVFTPK TGYTGYCSGT LLNNSNSPKR QLFWSAAHCI STQKVANTLQ TYWLYDATGC DNDTLSDKAV TLTGGATLLH SHATRDTLLL ELKSAPPSGA YYAGWNSSAI ATKGTAIEGI HHPSGDLKKY SLGSVTALSS TIDGKKPLTK VAWTTGVTEG GSSGSGLFTI SSTSGYQLRG GLYGGTSYCS APSDPDYYSQ LDGVWSSIKT YFSPHHHHHH HH
Endotoxin
< 0.1 ng/µg of protein (< 1EU/µg)
Purity
> 95% by SDS-PAGE & HPLC analyses
Bioactivity
The reaction is measured as an increase in absorbance at 253 nm resulting from the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE) .
Length
252
Form
Lyophilized
Molecular Weight
26.8 kDa
Host or Source
Insect cells

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