Labprice Enterokinase Recombinant Protein

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.

Tested Applications: N/A
Applications: N/A
Predicted Molecular Weight: N/A
Physical state: Lyophilized
Buffer: N/A
Concentration: N/A
NCBI official symbol: TMPRSS15
Accession #: NP_002763.2
Protein GI: 223942069
NCBI gene ID#: 5651
NCBI official full name: transmembrane protease, serine 15
NCBI organism: Homo sapiens
Peptide sequence: Heavy chain: LTIKESQRG AALGQSHEAR ATFKITSGVT YNPNLQDKLS VDFKVLAFDL QQMIDEIFLS SNLKNEYKNS RVLQFENGSI IVVFDLFFAQ WVSDQNVKEE LIQGLEANKS SQLVTFHIDL NSVDILDKLT TTSHLATPGN VSIECLPGSS PCTDALTCIK ADLFCDGEVN CPDGSDEDNK MCATVCDGRF LLTGSSGSFQ ATHYPKPSET SVVCQWIIRV NQGLSIKLSF DDFNTYYTDI LDIYEGVGSS KILRASIWET NPGTIRIFSN QVTATFLIES DESDYVGFNA TYTAFNSSEL NNYEKINCNF EDGFCFWVQD LNDDNEWERI QGSTFSPFTG PNFDHTFGNA SGFYISTPTG PGGRQERVGL LSLPLDPTLE PACLSFWYHM YGENVHKLSI NISNDQNMEK TVFQKEGNYG DNWNYGQVTL NETVKFKVAF NAFKNKILSD IALDDISLTY GICNGSLYPE PTLVPTPPPE LPTDCGGPFE LWEPNTTFSS TNFPNSYPNL AFCVWILNAQ KGKNIQLHFQ EFDLENINDV VEIRDGEEAD SLLLAVYTGP GPVKDVFSTT NRMTVLLITN DVLARGGFKA NFTTGYHLGI P EPCKADHF QCKNGECVPL VNLCDGHLHC EDGSDEADCV RFFNGTTNNN GLVRFRIQSI WHTACAENWT TQISNDVCQL LGLGSGNSSK PIFSTDGGPF VKLNTAPDGH LILTPSQQCL QDSLIRLQCN HKSCGKKLAA QDITPK Light Chain: IVGGSNAKE GAWPWVVGLY YGGRLLCGAS LVSSDWLVSA AHCVYGRNLE PSKWTAILGL HMKSNLTSPQ TVPRLIDEIV INPHYNRRRK DNDIAMMHLE FKVNYTDYIQ PICLPEENQV FPPGRNCSIA GWGTVVYQGT TANILQEADV PLLSNERCQQ QMPEYNITEN MICAGYEEGG IDSCQGDSGG PLMCQENNRW FLAGVTSFGY KCALPNRPGV YARVSRFTEW IQSFLH
SWISSPROT #: P98073
Background Reference 1: N/A
Background Reference 2: N/A
Background Reference 3: N/A
Background Reference 4: N/A
Background Reference 5: N/A
Source: CHO cells
Species: Human
By Source: CHO Cells
By Species: Human
Fusion tag: N/A
Sequence: Heavy chain: LTIKESQRG AALGQSHEAR ATFKITSGVT YNPNLQDKLS VDFKVLAFDL QQMIDEIFLS SNLKNEYKNS RVLQFENGSI IVVFDLFFAQ WVSDQNVKEE LIQGLEANKS SQLVTFHIDL NSVDILDKLT TTSHLATPGN VSIECLPGSS PCTDALTCIK ADLFCDGEVN CPDGSDEDNK MCATVCDGRF LLTGSSGSFQ ATHYPKPSET SVVCQWIIRV NQGLSIKLSF DDFNTYYTDI LDIYEGVGSS KILRASIWET NPGTIRIFSN QVTATFLIES DESDYVGFNA TYTAFNSSEL NNYEKINCNF EDGFCFWVQD LNDDNEWERI QGSTFSPFTG PNFDHTFGNA SGFYISTPTG PGGRQERVGL LSLPLDPTLE PACLSFWYHM YGENVHKLSI NISNDQNMEK TVFQKEGNYG DNWNYGQVTL NETVKFKVAF NAFKNKILSD IALDDISLTY GICNGSLYPE PTLVPTPPPE LPTDCGGPFE LWEPNTTFSS TNFPNSYPNL AFCVWILNAQ KGKNIQLHFQ EFDLENINDV VEIRDGEEAD SLLLAVYTGP GPVKDVFSTT NRMTVLLITN DVLARGGFKA NFTTGYHLGI P EPCKADHF QCKNGECVPL VNLCDGHLHC EDGSDEADCV RFFNGTTNNN GLVRFRIQSI WHTACAENWT TQISNDVCQL LGLGSGNSSK PIFSTDGGPF VKLNTAPDGH LILTPSQQCL QDSLIRLQCN HKSCGKKLAA QDITPK Light Chain: IVGGSNAKE GAWPWVVGLY YGGRLLCGAS LVSSDWLVSA AHCVYGRNLE PSKWTAILGL HMKSNLTSPQ TVPRLIDEIV INPHYNRRRK DNDIAMMHLE FKVNYTDYIQ PICLPEENQV FPPGRNCSIA GWGTVVYQGT TANILQEADV PLLSNERCQQ QMPEYNITEN MICAGYEEGG IDSCQGDSGG PLMCQENNRW FLAGVTSFGY KCALPNRPGV YARVSRFTEW IQSFLH
Biology activity: Sequentially cleaves carboxyl side of D-D-D-D-K. Endotoxin level is less than 0.2 ng per µg (2EU/µg).
Purity: Greater than 90% by SDS-PAGE gel and HPLC analyses.

The lyophilized Enterokinase recombinant protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted Enterokinase stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. As with any protein, exposing Enterokinase recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

This product is for research use only.