Enterokinase

CAT: 0209-100-409SSize: 10 µgDry Ice: NoHazardous: No

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CAT#:0209-100-409SSize:10 µg

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24/48H Stock Items & 2 to 6 Weeks non Stock Items.

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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. 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.

Synonyms

Enteropeptidase, Serine protease 7

NCBI Gene ID

5651

UniProt

P98073

Accession Number

NP_002763.2

Accession Number mRNA

NM_002772.2

Chromosomal Location

21q21.1

Reactivity

Human

Cross Reactivity

Human

Sequence

Heavy chain: LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIPEPCKADHFQC KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FSTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPK Light Chain: IVGGSNAKEG AWPWVVGLYY GGRLLCGASL VSSDWLVSAA HCVYGRNLEP SKWTAILGLH MKSNLTSPQT VPRLIDEIVI NPHYNRRRKD NDIAMMHLEF KVNYTDYIQP ICLPEENQVF PPGRNCSIAG WGTVVYQGTT ANILQEADVP LLSNERCQQQ MPEYNITENM ICAGYEEGGI DSCQGDSGGP LMCQENNRWF LAGVTSFGYK CALPNRPGVY ARVSRFTEWI QSFLH

Endotoxin

< 0.1 ng/µg of protein (< 1EU/µg)

Purity

>90% by SDS-PAGE & HPLC analyses

Bioactivity

Sequentially cleaves carboxyl side of D-D-D-D-K.

Length

784/235

Form

Lyophilized

Molecular Weight

108.7 kDa

Host or Source

CHO cells

Alternative Products

Catalog	Name
BX112011-01	Enterokinase
YP-W22717-01	Mouse enterokinase (enterokinase) ELISA Kit
PT_40494-01	Enteropeptidase/Enterokinase Porcine (Enterokinase Porcine)
YP-W60665-01	Chicken enterokinase (enterokinase) ELISA Kit
TP780003	Enterokinase Recombinant Protein (Enterokinase) Recombinant Protein
HY-E70202	Recombinant enterokinase
32-13688-20	Enterokinase Human
OM298260-01	Enterokinase Bovine
OPPA00831-20IU	Enterokinase Protein
PE0022	EK/Enterokinase

Enterokinase

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