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Human Enterokinase / PRSS7 Gene ORF cDNA clone expression plasmid, C-Myc tag

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Human TMPRSS15 cDNA Clone Product Information
NCBI RefSeq:NM_002772.1
RefSeq ORF Size:3060bp
cDNA Description:Full length Clone DNA of Homo sapiens protease, serine, 7 (enterokinase) with C terminal Myc tag.
Gene Synonym:ENTK, MGC133046, PRSS7
Species:Human
Vector:pCMV3-C-Myc
Plasmid:
Restriction Site:
Tag Sequence:Myc Tag Sequence: GAGCAGAAACTCATCTCAGAAGAGGATCTG
Sequence Description:
Sequencing primers:T7(TAATACGACTCACTATAGGG) BGH(TAGAAGGCACAGTCGAGG)
Promoter:Enhanced CMV mammalian cell promoter
Application:Stable or Transient mammalian expression
Antibiotic in E.coli:Kanamycin
Antibiotic in mammalian cell:Hygromycin
Shipping_carrier:Each tube contains lyophilized plasmid.
Storage:The lyophilized plasmid can be stored at room temperature for three months.
Myc Tag Info

A myc tag is a polypeptide protein tag derived from the c-myc gene product that can be added to a protein using recombinant DNA technology. It can be used for affinity chromatography, then used to separate recombinant, overexpressed protein from wild type protein expressed by the host organism. It can also be used in the isolation of protein complexes with multiple subunits.

A myc tag can be used in many different assays that require recognition by an antibody. If there is no antibody against the studied protein, adding a myc-tag allows one to follow the protein with an antibody against the Myc epitope. Examples are cellular localization studies by immunofluorescence or detection by Western blotting.

The peptide sequence of the myc-tag is: N-EQKLISEEDL-C (1202 Da). It can be fused to the C-terminus and the N-terminus of a protein. It is advisable not to fuse the tag directly behind the signal peptide of a secretory protein, since it can interfere with translocation into the secretory pathway.

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Background

Enterokinase, or Enteropeptidase is a type II transmembrane, which is a member of the trypsin family of serine proteases, and plays a key role in mammalian metabolism. It is synthesized as a zymogen (proenteropeptidase) that requires activation by another protease, either trypsin or possibly duodenase. Active enteropeptidase then converts the pancreatic precursor, trypsinogen, to trypsin by cleavage of the specific trypsinogen activation peptide, Asp-Asp-Asp-Asp-Lys- Ile that is highly conserved in vertebrates. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. Enterokinase consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which has the same mechanism of action as trypsin and chymotrypsin. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. Because of its high specificity towards the amino acid sequence (Asp)(4)-Lys, enterokinase is a potential tool for the cleavage of fusion proteins, which are gaining more importance in biopharmaceutical production. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins.

References
  • Light A, et al. (1989) Enterokinase (enteropeptidase): comparative aspects. Trends Biochem Sci. 14(3): 110-2.
  • Kubitzki T, et al. (2009) Application of immobilized bovine enterokinase in repetitive fusion protein cleavage for the production of mucin 1. Biotechnol J. 4(11): 1610-8.
  • Zheng XL, et al. (2009) Enteropeptidase, a type II transmembrane serine protease. Front Biosci (Elite Ed). 1: 242-9.
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    Catalog: HG10733-CM
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