human Enterokinase

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Cat-Nr.100-409
Size50 µg
Price170 €
SourceCHO cells
Formulationlyophilized
Purity Confirmation>90% by SDS-PAGE & HPLC analyses
Length [aa]784/235
Molecular Weight108.7 kDa
Endotoxin Levels< 0.1 ng/µg of protein (<1EU/µg)
Biological ActivitySequentially cleaves carboxyl side of D-D-D-D-K.
Species ReactivityHuman
SynonymsEnteropeptidase, Serine protease 7
DescriptionProteases (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. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light consists of 235 amino acid residues.
Protein SequenceHeavy chain: LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN
Uniprot IDP98073
Protein RefSeqNP_002763.2
mRNA RefSeqNM_002772.2

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