Recombinant Human GBA2 protein (GST tag N-Terminus)
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(1 Publication)
Recombinant Human GBA2 protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 927 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
KIAA1605, SPG46, AD035, GBA2, Non-lysosomal glucosylceramidase, NLGase, Beta-glucocerebrosidase 2, Bile acid beta-glucosidase GBA2, Bile acid glucosyl transferase GBA2, Cholesterol glucosyltransferase GBA2, Cholesteryl-beta-glucosidase GBA2, Glucosylceramidase 2, Non-lysosomal cholesterol glycosyltransferase, Non-lysosomal galactosylceramidase, Non-lysosomal glycosylceramidase, Beta-glucosidase 2
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human GBA2 protein (GST tag N-Terminus) (AB163631)
ab163631 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
GBA2 facilitates the metabolism of glycosphingolipids. It functions as part of lipid homeostasis ensuring the balance of ceramide levels. This enzyme plays a role in maintaining cellular functions that require precise lipid composition. Although not characterized as part of a larger complex GBA2 significantly impacts membrane dynamics and cellular signaling processes.
Pathways
GBA2 is integral to the glycosphingolipid metabolism pathway impacting cell signaling and membrane structure. Its activity influences sphingolipid metabolism connecting it with the sphingomyelinase pathway. In this context it relates to enzymes like ceramidases and sphingomyelinases which also contribute to sphingolipid breakdown and ceramide regulation.
Specifications
Form
Liquid
General info
Function
Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) to free glucose and ceramides (such as N-acylsphing-4-enine) (PubMed : 17105727, PubMed : 30308956, PubMed : 32144204). GlcCers are membrane glycosphingolipids that have a wide intracellular distribution (By similarity). They are the main precursors of more complex glycosphingolipids that play a role in cellular growth, differentiation, adhesion, signaling, cytoskeletal dynamics and membrane properties (By similarity). Involved in the transglucosylation of cholesterol, transfers glucose from GlcCer to cholesterol, thereby modifying its water solubility and biological properties (PubMed : 32144204). Under specific conditions, may catalyze the reverse reaction, transferring glucose from cholesteryl-3-beta-D-glucoside to ceramide (such as N-acylsphing-4-enine) (Probable). May play a role in the metabolism of bile acids (PubMed : 11489889, PubMed : 17080196, PubMed : 9111029). Able to hydrolyze bile acid 3-O-glucosides as well as to produce bile acid-glucose conjugates thanks to a bile acid glucosyl transferase activity (PubMed : 11489889, PubMed : 17080196, PubMed : 9111029). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the galactosyl transfer between GalCers and cholesterol in vitro with lower activity compared with their activity against GlcCers (PubMed : 32144204).
Sequence similarities
Belongs to the non-lysosomal glucosylceramidase family.
Target data
Publications (1)
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PloS one 10:e0119141 PubMed25763858
2015
Applications
Unspecified application
Species
Unspecified reactive species
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