Human GBA/glucocerebrosidase Protein 2951

$750.00 – $2,500.00

Summary

Expression: HEK293
Active: Yes (catalytic)
Amino Acid Range: Ala40-Gln536

SKU: 2951parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	NP_000148.2
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Glucocerebrosidase (GBA) mutations are the most important genetic risk factor for the development of Parkinson disease (PD). GBA encodes the lysosomal enzyme glucocerebrosidase (GCase).
molecular weight	The protein has a predicted MW of 56.69 kDa. Due to glycosylation, the protein migrates to 60-70 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human GBA/glucocerebrosidase Protein 2951
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
Glucocerebrosidase (GBA) mutations are the most important genetic risk factor for the development of Parkinson disease (PD). GBA encodes the lysosomal enzyme glucocerebrosidase (GCase).
Protein names
Lysosomal acid glucosylceramidase (Lysosomal acid GCase) (EC 3.2.1.45) (Acid beta-glucosidase) (Alglucerase) (Beta-glucocerebrosidase) (Beta-GC) (Beta-glucosylceramidase 1) (Cholesterol glucosyltransferase) (SGTase) (EC 2.4.1.-) (Cholesteryl-beta-glucosidase) (EC 3.2.1.-) (D-glucosyl-N-acylsphingosine glucohydrolase) (Glucosylceramidase b
Protein family
Glycosyl hydrolase 30 family
Mass
59716Da
Function
Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:15916907, PubMed:24211208, PubMed:32144204, PubMed:9201993). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208, PubMed:26724485, PubMed:32144204). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (Probable) (PubMed:26724485). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (PubMed:24211208, PubMed:26724485). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (PubMed:32144204). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (PubMed:33361282). {ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:27378698, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:33361282, ECO:0000269|PubMed:9201993, ECO:0000305|PubMed:32144204}.
Catalytic activity
CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:32144204, ECO:0000269|PubMed:9201993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270; Evidence={ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-galactose; Xref=Rhea:RHEA:14297, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377, ChEBI:CHEBI:18390, ChEBI:CHEBI:52639; EC=3.2.1.46; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14298; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D-glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957; Evidence={ECO:0000269|PubMed:33361282, ECO:0000305|PubMed:24211208}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside; Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58265; Evidence={ECO:0000269|PubMed:32144204, ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58266; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4E-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-(9Z-octadecenoyl)-sphing-4-enine; Xref=Rhea:RHEA:58324, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:77996, ChEBI:CHEBI:139140; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58325; Evidence={ECO:0000269|PubMed:32144204, ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58326; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1')-N-hexadecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:58316, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72959, ChEBI:CHEBI:84716; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58317; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58318; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-octanoylsphing-4E-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-octanoylsphing-4-enine; Xref=Rhea:RHEA:70303, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:45815, ChEBI:CHEBI:65222; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70304; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70305; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-N-dodecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-dodecanoylsphing-4-enine; Xref=Rhea:RHEA:70307, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72956, ChEBI:CHEBI:76297; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70308; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70309; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1)-N-octadecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-octadecanoylsphing-4-enine; Xref=Rhea:RHEA:70311, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:72961, ChEBI:CHEBI:84719; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70312; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70313; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=beta-D-glucosyl-(1<->1')-N-(15Z-tetracosenoyl)-sphing-4-enine + cholesterol = cholesteryl 3-beta-D-glucoside + N-(15Z-tetracosenoyl)-sphing-4-enine; Xref=Rhea:RHEA:70315, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:74450, ChEBI:CHEBI:76302; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70316; Evidence={ECO:0000305|PubMed:24211208}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70317; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-galactoside; Xref=Rhea:RHEA:70235, ChEBI:CHEBI:16113, ChEBI:CHEBI:18390, ChEBI:CHEBI:52639, ChEBI:CHEBI:189066; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70236; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70237; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=1-(beta-D-galactosyl)-N-dodecanoylsphing-4-enine + cholesterol = cholesteryl 3-beta-D-galactoside + N-dodecanoylsphing-4-enine; Xref=Rhea:RHEA:70255, ChEBI:CHEBI:16113, ChEBI:CHEBI:72956, ChEBI:CHEBI:73432, ChEBI:CHEBI:189066; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70256; Evidence={ECO:0000269|PubMed:32144204}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70257; Evidence={ECO:0000305|PubMed:32144204}; CATALYTIC ACTIVITY: Reaction=a beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-xyloside; Xref=Rhea:RHEA:70239, ChEBI:CHEBI:16113, ChEBI:CHEBI:52639, ChEBI:CHEBI:189067, ChEBI:CHEBI:189068; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70240; Evidence={ECO:0000269|PubMed:33361282}; CATALYTIC ACTIVITY: Reaction=beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + cholesterol = cholesteryl 3-beta-D-xyloside + N-(9Z-octadecenoyl)-sphing-4-enine; Xref=Rhea:RHEA:70251, ChEBI:CHEBI:16113, ChEBI:CHEBI:77996, ChEBI:CHEBI:189067, ChEBI:CHEBI:189081; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70252; Evidence={ECO:0000269|PubMed:33361282};
Pathway
PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485}.; PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:
Subellular location
Lysosome membrane {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Peripheral membrane protein {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:1848227}; Lumenal side {ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C promotes membrane association (PubMed:10781797). Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 (PubMed:18022370). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370}.
Structure
Interacts with saposin-C (PubMed:10781797). Interacts with SCARB2 (PubMed:18022370). Interacts with TCP1 (PubMed:21098288). May interacts with SNCA; this interaction may inhibit the glucosylceramidase activity (PubMed:23266198). Interacts with GRN; this interaction prevents aggregation of GBA1-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:21098288, ECO:0000269|PubMed:23266198, ECO:0000269|PubMed:27789271}.
Target Relevance information above includes information from UniProt accession: P04062
The UniProt Consortium

Activity assay with Human GBA/glucocerebrosidase Protein

Measured by its ability to hydrolyze 4-methylumbelliferyl-beta-D-glucopyranoside. The specific activity is >200 pmol/min/µg.

HPLC of Human GBA/glucocerebrosidase Protein

The purity of Human GBA is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human GBA/glucocerebrosidase Protein

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

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

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.