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TMPRSS15 Protein

TMPRSS15 Origin: Pig Host: Yeast Active
Catalog No. ABIN1574313
  • Target See all TMPRSS15 Proteins
    TMPRSS15 (Transmembrane Protease, serine 15 (TMPRSS15))
    Biological Activity
    Active
    Origin
    • 7
    • 4
    • 4
    • 3
    • 1
    Pig
    Source
    • 6
    • 6
    • 1
    • 1
    • 1
    • 1
    • 1
    Yeast
    Characteristics
    The Enterokinase is a highly purified recombinant porcine enterokinase. The enzyme has been extensively purified and tested to ensure that there are no other contaminating proteases.
    Top Product
    Discover our top product TMPRSS15 Protein
  • Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    2 U/µL
    Storage
    -20 °C
    Storage Comment
    Store at -20°C after delivery.The enterokinase, formulated using proprietary technology, can be shipped at room temperature. It will remain stable at 37°C for one week without losing any activity.
  • Chen, Ren, Han, Mu, Li, Ma, Cui: "A cadherin-like protein from the beet armyworm Spodoptera exigua (Lepidoptera: Noctuidae) is a putative Cry1Ac receptor." in: Archives of insect biochemistry and physiology, Vol. 86, Issue 1, pp. 58-71, (2014) (PubMed).

    Petersen, Montserrat, Mujico, Loh, Beringer, van Lummel, Thompson, Mearin, Schweizer, Kooy-Winkelaar, van Bergen, Drijfhout, Kan, La Gruta, Anderson, Reid, Koning, Rossjohn: "T-cell receptor recognition of HLA-DQ2-gliadin complexes associated with celiac disease." in: Nature structural & molecular biology, Vol. 21, Issue 5, pp. 480-8, (2014) (PubMed).

    Kartner, Yao, Bhargava, Manolson: "Topology, glycosylation and conformational changes in the membrane domain of the vacuolar H+-ATPase a subunit." in: Journal of cellular biochemistry, Vol. 114, Issue 7, pp. 1474-87, (2013) (PubMed).

    Ren, Chen, Zhang, Ma, Cui, Han, Mu, Li: "A Spodoptera exigua cadherin serves as a putative receptor for Bacillus thuringiensis Cry1Ca toxin and shows differential enhancement of Cry1Ca and Cry1Ac toxicity." in: Applied and environmental microbiology, Vol. 79, Issue 18, pp. 5576-83, (2013) (PubMed).

    Luo, Ai, Zhou, Min, Liang, Zhang, Song, Liu, Zhang: "Molecular structure, expression analysis and functional characterization of APRIL (TNFSF 13) in goat (Capra hircus)." in: Gene, Vol. 485, Issue 2, pp. 63-8, (2011) (PubMed).

    Sullivan, Clements, Beddoe, Johnson, Hoare, Lin, Huyton, Hopkins, Reid, Wilce, Kabat, Borrego, Coligan, Rossjohn, Brooks: "The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition." in: Immunity, Vol. 27, Issue 6, pp. 900-11, (2007) (PubMed).

    Buchko, Robinson, Ni, Pakrasi, Kennedy: "Cloning, expression, crystallization and preliminary crystallographic analysis of a pentapeptide-repeat protein (Rfr23) from the bacterium Cyanothece 51142." in: Acta crystallographica. Section F, Structural biology and crystallization communications, Vol. 62, Issue Pt 12, pp. 1251-4, (2006) (PubMed).

  • Target
    TMPRSS15 (Transmembrane Protease, serine 15 (TMPRSS15))
    Alternative Name
    Enterokinase (TMPRSS15 Products)
    Synonyms
    CG3066 Protein, Dmel\\CG3066 Protein, MP2 Protein, PAE1 Protein, SP7 Protein, anon-Ryu Protein, proPO-AE Protein, sp7 Protein, NV14771 Protein, PRSS7 Protein, ENTK Protein, Entk Protein, Prss7 Protein, Serine protease 7 Protein, serine protease 7 Protein, transmembrane protease, serine 7 Protein, transmembrane protease, serine 15 Protein, Sp7 Protein, LOC733125 Protein, SP7 Protein, TMPRSS7 Protein, TMPRSS15 Protein, Tmprss15 Protein
    Background
    Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. Enterokinase will not cleave, however, if this lysine is followed by a proline. Enterokinase can remove fusion tags is located in the N-terminal section of proteins, useful for removing unwanted tags
    Molecular Weight
    Theoretical MW: 21,880 Da, the apparent MW on SDS-PAGE: about 40,000 Da
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