Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
Greater than 80.0% as determined by SDS-PAGE.
KLK15 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 249 amino acids (17-256a.a.) and having a molecular mass of 27.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
KLK15 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Kallikrein Related Peptidase 15, ACO Protease, Kallikrein-Like Serine Protease, Kallikrein 15, Kallikrein-15, Prostinogen, EC 3.4.21.4, EC 3.4.21.-, EC 3.4.21, HSRNASPH, ACO.
ADPQDGDKLL EGDECAPHSQ PWQVALYERG RFNCGASLIS PHWVLSAAHC QSRFMRVRLG EHNLRKRDGP EQLRTTSRVI PHPRYEARSH RNDIMLLRLV QPARLNPQVR PAVLPTRCPH PGEACVVSGW GLVSHNEPGT AGSPRSQVSL PDTLHCANIS IISDTSCDKS YPGRLTNTMV CAGAEGRGAE SCEGDSGGPL VCGGILQGIV SWGDVPCDNT TKPGVYTKVC HYLEWIRETM KRNHHHHHH.
KLK15 is located on chromosome 19, within a cluster of kallikrein genes. The gene encoding KLK15 contains multiple polyadenylation sites, and alternative splicing results in various transcript variants encoding different isoforms . The human recombinant form of KLK15 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain consisting of 249 amino acids (17-256 a.a.) with a molecular mass of approximately 27.4 kDa .
The recombinant KLK15 is expressed with a 6-amino acid His tag at the C-terminus, which facilitates its purification using chromatographic techniques . The protein is typically provided as a sterile, filtered, colorless solution in phosphate-buffered saline (PBS) with 10% glycerol, and it is recommended to store it at 4°C for short-term use or at -20°C for long-term storage .
The amino acid sequence of KLK15 includes several key regions that contribute to its enzymatic activity. The protein’s structure allows it to interact with specific substrates, leading to the cleavage of peptide bonds. The recombinant form produced in Sf9 cells retains these functional properties, making it a valuable tool for laboratory research .
KLK15 is used in various research applications, including studies on its role in cancer progression, its potential as a biomarker, and its enzymatic properties. The recombinant form allows researchers to investigate these aspects in a controlled environment, providing insights into the enzyme’s function and potential therapeutic uses .