The elastase 3A is relative to pancreatic serine proteinases and has a low level of elastolytic activity comparing to other elastases. Elastase 3A is eventually involved in the intestinal transport and metabolism of cholesterol. Elastase 3A and elastase 3B are also referred to as protease E and elastase 1, respectively. Furthermore, elastase 3A is an efficient protease that preferentially cleaves proteins after the alanine residue due to its alanine specificity. By substitution of the amino acid S217A the enzyme is rendered catalytically inactive.
MSGYGPPSSHSSSRVVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLT YQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAG DILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGC NGDAGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASHVLVPRGSAAA LE
Expression Host: human, HEK293
Formulation: PBS, pH 7,4
Format: Liquid, stored and shipped at -80°C
Purity: > 90% as determined by SDS-PAGE
Chymotrypsin-like elastases (CELAs) are pancreatic serine proteinases. This enzyme belongs to the peptidase S1 family which is subfamily of serine proteases. The human CELA3A is a member of the elastase family, which consists of the six human elastase genes. The next proteins elastase 1, 2, 2A, 2B, 3A, and 3B are structurally similar and encoded by elastase genes which are known in human. The human pancreas does not express CELA1 but secretes two CELA3 isoforms, CELA3A and CELA3B as a zymogen and has a digestive function in the intestine, very similar to other serine proteases such as trypsin, chymotrypsin and kallikrein. Peptidase S1 domain is included in the structure of CELA3A and hydrolyzing many proteins in addition to elastin. hCELA3A is the product of gene duplication and shares 92% identity in their primary structure. The amino acid S217 of CELA3A is part of the catalytic triade typical for all serin proteases. By substitution of this amino acid by a different one (S217A), the enzyme is loosing its catalytic activity.