Enterokinase Active Protein | TMPRSS15 active protein

Human Enterokinase

Cat. Num. AAA692126

• Gene Names: TMPRSS15; ENTK; PRSS7
• Reactivity: Human
• Purity: >90% by SDS-PAGE & HPLC analyses
• Synonyms: Enterokinase; Human Enterokinase; Enteropeptidase; Serine protease 7; TMPRSS15 active protein

• Host: CHO Cells
• Reactivity: Human
• Purity/Purification: >90% by SDS-PAGE & HPLC analyses
• Form/Format: Lyophilized
• Sequence: Heavy chain:LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQ DKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILD KLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC P DGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWII RVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PG TIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCN FE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFY ISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSI N ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKN KILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLEN INDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIPEPCKADHFQC KNGECVPLVN LCDGHLH CED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ IS NDVCQLLG LGSGNSSKPI FSTDGGPFVK LNTAPDGHLI LTPSQQCL QD SLIRLQCNHK SCGKKLAAQD ITPK Light Chain:IVG GSNAKEG AWPWVVGLYY GGRLLCGASL VSSDWLVSAA HCVYGRNLE P SKWTAILGLH MKSNLTSPQT VPRLIDEIVI NPHYNRRRKD NDIA MMHLEF KVNYTDYIQP ICLPEENQVF PPGRNCSIAG WGTVVYQGTT ANILQEADVP LLSNERCQQQ MPEYNITENM ICAGYEEGGI DSCQG DSGGP LMCQENNRWF LAGVTSFGYK CALPNRPGVY ARVSRFTEWI QSFLH
• Sequence Length: 1019

• Biological Activity: Sequentially cleaves carboxyl side of D-D-D-D-K.

Related Product Information for TMPRSS15 active protein

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.

Product Categories/Family for TMPRSS15 active protein

Cytokines & Growth Factors

NCBI and Uniprot Product Information

• NCBI GI #: 223942069
• NCBI GeneID: 5651
• NCBI Accession #: NP_002763.2
• NCBI GenBank Nucleotide #: NM_002772.2
• UniProt Accession #: P98073; Q2NKL7
• Molecular Weight: 112,935 Da
• NCBI Official Full Name: enteropeptidase
• NCBI Official Synonym Full Names: transmembrane protease, serine 15
• NCBI Official Symbol: TMPRSS15
• NCBI Official Synonym Symbols: ENTK; PRSS7
• NCBI Protein Information: enteropeptidase; serine protease 7; enterokinase catalytic subunit; protease, serine, 7 (enterokinase)
• UniProt Protein Name: Enteropeptidase
• Protein Family: Enteropeptidase
• UniProt Gene Name: TMPRSS15
• UniProt Synonym Gene Names: ENTK; PRSS7
• UniProt Entry Name: ENTK_HUMAN

NCBI Description

This gene encodes an enzyme that converts the pancreatic proenzyme trypsinogen to trypsin, which activates other proenzymes including chymotrypsinogen and procarboxypeptidases. The precursor protein is cleaved into two chains that form a heterodimer linked by a disulfide bond. This protein is a member of the trypsin family of peptidases. Mutations in this gene cause enterokinase deficiency, a malabsorption disorder characterized by diarrhea and failure to thrive. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.

Catalytic activity: Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.

Subunit structure: Heterodimer of a catalytic (light) chain and a multidomain (heavy) chain linked by a disulfide bond.

Subcellular location: Membrane; Single-pass type II membrane protein

Probable.

Tissue specificity: Intestinal brush border.

Post-translational modification: The chains are derived from a single precursor that is cleaved by a trypsin-like protease.

Involvement in disease: Enterokinase deficiency (ENTKD) [MIM:226200]: Life-threatening intestinal malabsorption disorder characterized by diarrhea and failure to thrive.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Sequence similarities: Belongs to the peptidase S1 family.Contains 2 CUB domains.Contains 2 LDL-receptor class A domains.Contains 1 MAM domain.Contains 1 peptidase S1 domain.Contains 1 SEA domain.Contains 1 SRCR domain.

Sequence caution: The sequence CAB90389.1 differs from that shown. Reason: Erroneous gene model prediction.