Rabbit Polyclonal GBA2 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human GBA2 aa 700 to C-terminus.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
WB | IHC-P | |
---|---|---|
Human | Tested | Tested |
Mouse | Predicted | Predicted |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/200.00000 - 1/1000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/500.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info - | Notes - |
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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).
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
Rabbit Polyclonal GBA2 antibody. Suitable for WB, IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human GBA2 aa 700 to C-terminus.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA
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GBA2 also known as non-lysosomal glucosylceramidase is an enzyme responsible for hydrolyzing glucosylceramide into glucose and ceramide. With a molecular mass approximately 118 kDa GBA2 localizes in the endoplasmic reticulum and the cytosol. It is widely expressed in various tissues including the liver brain and testis indicating its diverse physiological roles. Unlike GBA1 which functions in lysosomal degradation GBA2 operates outside lysosomes.
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.
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.
Research has associated GBA2 with conditions such as hereditary spastic paraplegia and Niemann-Pick disease type C. Mutations or dysregulation of GBA2 can disturb lipid metabolism leading to neurological impairments observed in these disorders. Connections between GBA2 and other proteins such as NPC1 which is involved in cholesterol transport highlight its relevance in complex metabolic disorders.
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This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
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All lanes: Western blot - Anti-GBA2 antibody (ab205064) at 1/500 dilution
Lane 1: HeLa cell lysate
Lane 2: HepG2 cell lysate
Predicted band size: 105 kDa
Observed band size: 98 kDa
Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human fetal colon tissue labeling GBA2 with ab205064 at 1/100 dilution.
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