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.
TMPRSS15
Origine: Humain
Hôte: CHO Cells
Recombinant
< 90 % by SDS-PAGE gel and HPLC analyses.
Active
Restrictions
For Research Use only
Format
Liquid
Concentration
2 U/µL
Stock
-20 °C
Stockage commentaire
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." dans: 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." dans: 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." dans: 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." dans: 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)." dans: 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." dans: 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." dans: Acta crystallographica. Section F, Structural biology and crystallization communications, Vol. 62, Issue Pt 12, pp. 1251-4, (2006) (PubMed).
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
Poids moléculaire
Theoretical MW: 21,880 Da, the apparent MW on SDS-PAGE: about 40,000 Da