
hCELA3A, His-Tag; inactive variant S217A
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SKU: P2020-129 trenzyme
Description
The elastase 3A is relative to pancreatic serine proteinases and has a low level of elastolytic activity comparing to other elastases. Elastase 3A is probably involved in the intestinal transport and metabolism of cholesterol. Furthermore, elastase 3A is an efficient protease that preferentially cleaves proteins after alanine residues due to its alanine specificity. Both elastase 3A and elastase 3B have been referred to as protease E and elastase 1. By substitution of the amino acid S217A the enzyme is rendered catalytically inactive.
Overview
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Product Name: hCELA3A, His-Tag; inactive variant S217A
- Catalog No.: P2020-129
- RefSeq Links: UniProt: P09093
- Synonyms: Chymotrypsin-like elastase family member 3A; Elastase IIIA; Elastase-3A; ELA3; ELA3A; Protease E; OTTHUMP00000002835; elastase 3A; pancreatic; inactive variant; catalytically inactive

Sequence Information
- Species: Homo sapiens, human
- Tags: His-Tag, C-terminal
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Sequence without tags (AA 16-270):
MSGYGPPSSHSSSRVVHGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISRDLT YQVVLGEYNLAVKEGPEQVIPINSEELFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAG DILPNKTPCYITGWGRLYTNGPLPDKLQQARLPVVDYKHCSRWNWWGSTVKKTMVCAGGYIRSGC NGDAGGPLNCPTEDGGWQVHGVTSFVSAFGCNFIWKPTVFTRVSAFIDWIEETIASHVLVPRGSAAA
LE
Product Information
- Expression Host: human, HEK293
- Formulation: PBS, pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 90% as determined by SDS-PAGE
Background Information
Chymotrypsin-like elastases (CELAs) are pancreatic serine proteinases, which belong to the peptidase S1 family, a subfamily of serine proteases. The human CELA3A is a member of the elastase family, which consists of six human elastase genes encoding the proteins elastase 1, 2, 2A, 2B, 3A, and 3B, all of which are structurally similar. Typically, elastases hydrolyze many proteins in addition to elastin. However, CELA3A has only little elastolytic activity. CELA3A is secreted by the pancreas and characterized by a digestive function in the intestine, very similar to other serine proteases such as trypsin, chymotrypsin and kallikrein. The amino acid S217 of CELA3A is part of the catalytic triade typical for all serine proteases. By substitution of this amino acid by a different one (S217A), the enzyme is loosing its catalytic activity.
SDS-PAGE/Coll. Coomassie |
Histogram of marked lane in gel picture |
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