hCELA3B, His-Tag; inactive variant S217A
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Description
The elastase 3B is relative to pancreatic serine proteinases and has a low level of elastolytic activity comparing to other elastases. Elastase 3B is probably involved in the intestinal transport and metabolism of cholesterol. Furthermore, elastase 3B 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: hCELA3B, His-Tag; inactive variant S217A
- Catalog No.: P2020-132
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RefSeq Links: UniProt: P08861
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Synonyms: Chymotrypsin-like elastase family member 3B; Elastase IIIB; Elastase-3B; Protease E; ELA3B; elastase 3B; pancreatic; inactive variant; catalytically inactive
Sequence Information
- Species: Homo sapiens, human
- Tags: His-Tag, C-terminal
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Sequence without tags (AA 18-270):
YGPPSSRPSSRVVNGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISS
SRTYQVVLGEYDRAVKEGPEQVIPINSGDLFVHPLWNRSCVACGNDIALIKLSRSAQLGDA
VQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYEHCSRWNWWGSS
VKKTMVCAGGDIRSGCNGDAGGPLNCPTEDGGWQVHGVTSFVSAFGCNTRRKPTVFTR
VSAFIDWIEETIASH
Product Information
- Expression Host: human, HEK293
- Formulation: PBS, pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 95% 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 CELA3B 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, CELA3B has only little elastolytic activity. CELA3B 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 CELA3B 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. In clinical assays, pancreatic function is analyzed by excretion of CELA3B in fecal material.
Structural model of the CELA3B protein generated by AlphaFold (https://alphafold.ebi.ac.uk)
- Jumper, J et al. Highly accurate protein structure prediction with AlphaFold. Nature (2021).
- Varadi, M et al. AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models. Nucleic Acids Research (2022).
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SDS-PAGE/Coll. Coomassie |
Histogram of marked lane in gel picture |
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