One unit is defined as the amount of enzyme needed to cleave 50 μg of fusion protein in 16 hours to 95 % completion at 22 °C in a buffer containing 25 mM Tris-HCl, pH 8.0.
TMPRSS15
Origine: Humain
Hôte: CHO Cells
Recombinant
< 90 % by SDS-PAGE gel and HPLC analyses.
Active
Restrictions
For Research Use only
Format
Lyophilized
Buffer
rPorcine Enterokinase, Lyophilized has been formulated using a proprietary technology, and the enzyme can be shipped at room temperature or stand at 37 °C for 7 days without losing any activity.
Stock
-80 °C
Stockage commentaire
Store at -20 °C after receiving. Reconstituted EK is stable for 24 hours at 2 °C - 8 °C. For long term storage, store it at -20 °C.
Ranok, Wongsantichon, Robinson, Suginta: "Structural and thermodynamic insights into chitooligosaccharide binding to human cartilage chitinase 3-like protein 2 (CHI3L2 or YKL-39)." dans: The Journal of biological chemistry, Vol. 290, Issue 5, pp. 2617-29, (2015) (PubMed).
Gratio, Beaufort, Seiz, Maier, Virca, Debela, Grebenchtchikov, Magdolen, Darmoul: "Kallikrein-related peptidase 4: a new activator of the aberrantly expressed protease-activated receptor 1 in colon cancer cells." dans: The American journal of pathology, Vol. 176, Issue 3, pp. 1452-61, (2010) (PubMed).
Pang, Berry, Chen, Kjer-Nielsen, Perugini, King, Wang, Chew, La Gruta, Williams, Beddoe, Tiganis, Cowieson, Godfrey, Purcell, Wilce, McCluskey, Rossjohn: "The structural basis for autonomous dimerization of the pre-T-cell antigen receptor." dans: Nature, Vol. 467, Issue 7317, pp. 844-8, (2010) (PubMed).
Hariharan, Liang, Chou, Chin: "A new model for ligand release. Role of side chain in gating the enediyne antibiotic." dans: The Journal of biological chemistry, Vol. 281, Issue 23, pp. 16025-33, (2006) (PubMed).
Buchko, Ni, Robinson, Welsh, Pakrasi, Kennedy: "Characterization of two potentially universal turn motifs that shape the repeated five-residues fold--crystal structure of a lumenal pentapeptide repeat protein from Cyanothece 51142." dans: Protein science : a publication of the Protein Society, Vol. 15, Issue 11, pp. 2579-95, (2006) (PubMed).
Enterokinase (EK) is a specific protease that cleaves a protein after lysine residue at its recognition site: Asp-Asp-Asp-Asp-Lys. Enterokinase will not work if the recognition site is followed by proline. If a fusion tag is placed at the N-terminus with an enterokinase site, enterokinase will be able to remove the fusion tag and to generate the protein exactly as you need without adding any unwanted residues. Porcine Enterokinase is a highly purified recombinant porcine enterokinase (Light Chain) expressed from P. Pastoris GS115 and is supplied in two forms for customers: a. Liquid in 50 % glycerol, b. Lyophilized (glycerol free). Synonyms: Enterokinase, EK
Poids moléculaire
Theoretical MW: 21,880 Da Apparent MW on SDS-PAGE: about 40,000 Da.