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, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Kex-2 cleaves at the carboxyl end of the recognition sequences Arg-Arg/X and Lys-Arg/X. Recombinant Yeast Kex-2 is a 60.4 kDa protease consisting of 558 amino acid residues.

Source: (BTI-Tn-5B1-4) Hi-5 Insect cells

Synonyms: Endoproteinase Lys/Arg-Arg

AA Sequence: LPVPAPPMDS SLLPVKEAED KLSINDPLFE RQWHLVNPSF PGSDINVLDL WYNNITGAGV VAAIVDDGLD YENEDLKDNF CAEGSWDFND NTNLPKPRLS DDYHGTRCAG EIAAKKGNNF CGVGVGYNAK ISGIRILSGD ITTEDEAASL IYGLDVNDIY SCSWGPADDG RHLQGPSDLV KKALVKGVTE GRDSKGAIYV FASGNGGTRG DNCNYDGYTN SIYSITIGAI DHKDLHPPYS EGCSAVMAVT YSSGSGEYIH SSDINGRCSN SHGGTSAAAP LAAGVYTLLL EANPNLTWRD VQYLSILSAV GLEKNADGDW RDSAMGKKYS HRYGFGKIDA HKLIEMSKTW ENVNAQTWFY LPTLYVSQST NSTEETLESV ITISEKSLQD ANFKRIEHVT VTVDIDTEIR GTTTVDLISP AGIISNLGVV RPRDVSSEGF KDWTFMSVAH WGENGVGDWK IKVKTTENGH RIDFHSWRLK LFGESIDSSK TETFVFGNDK EEVEPAATES TVSQYSASST SISISATSTS SISIGVETSA IPQTTTASTD PDSDPNTP

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Recombinant Kex-2 from High-5 insect cells contains the same specific activity and recognition sequence specificity as yeast derived KEX-2. 1 milligram of recombinant KEX-2 contains activity equivalent to at least 40 units of yeast derived KEX-2. Cleaves at the carboxyl side of K/R-R.

Note:

1mg will be provided as 2x500μg.