Human BCHE/Butyrylcholinesterase Protein 2505

$300.00 – $1,000.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: Glu29-Leu602

SKU: 2505parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P06276
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE
background	Butyrylcholinesterase is a serine hydrolase biochemically related to the cholinergic enzyme acetylcholinesterase. It is capable of hydrolyzing esters of choline. Butyrylcholinesterase has unique enzymatic properties and is widely distributed in the nervous system, raising the possibility of its involvement in neural function.
molecular weight	The protein has a predicted MW of 66.18 kDa. Due to glycosylation, the protein migrates to 70-110 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human BCHE/Butyrylcholinesterase Protein 2505

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Butyrylcholinesterase is a serine hydrolase biochemically related to the cholinergic enzyme acetylcholinesterase. It is capable of hydrolyzing esters of choline. Butyrylcholinesterase has unique enzymatic properties and is widely distributed in the nervous system, raising the possibility of its involvement in neural function.
Protein names Cholinesterase (EC 3.1.1.8) (Acylcholine acylhydrolase) (Butyrylcholine esterase) (Choline esterase II) (Pseudocholinesterase)
Gene names BCHE,BCHE CHE1
Protein family Type-B carboxylesterase/lipase family
Mass 9606Da
Function Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
Catalytic activity BINDING 110; /ligand="tacrine"; /ligand_id="ChEBI:CHEBI:187896"; /ligand_note="inhibitor"; /evidence="ECO:0007744\|PDB:4BDS"; BINDING 144..145; /ligand="substrate"; BINDING 466; /ligand="tacrine"; /ligand_id="ChEBI:CHEBI:187896"; /ligand_note="inhibitor"; /evidence="ECO:0007744\|PDB:4BDS"
Subellular location Secreted .
Tissues Detected in blood plasma (at protein level). Present in most cells except erythrocytes.
Structure Homotetramer; disulfide-linked. Dimer of dimers.
Post-translational modification N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type.
Target Relevance information above includes information from UniProt accession: P06276
The UniProt Consortium

Data

Activity assay with Human BCHE/Butyrylcholinesterase~-Protein

Measured by its ability to cleave Butyrylthiocholine. The specific activity is > 70000 pmoles/min/µg.

SDS-PAGE gel of Human BCHE/Butyrylcholinesterase~-Protein

Human BCHE on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.