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AB88300

Anti-GBA antibody

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(2 Publications)

Mouse Polyclonal GBA antibody. Carrier free. Suitable for WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human GBA1.

View Alternative Names

GBA, GC, GLUC, GBA1, Lysosomal acid glucosylceramidase, Lysosomal acid GCase, Acid beta-glucosidase, Alglucerase, Beta-glucocerebrosidase, Beta-glucosylceramidase 1, Cholesterol glucosyltransferase, Cholesteryl-beta-glucosidase, D-glucosyl-N-acylsphingosine glucohydrolase, Glucosylceramidase beta 1, Imiglucerase, Lysosomal cholesterol glycosyltransferase, Lysosomal galactosylceramidase, Lysosomal glycosylceramidase, Beta-GC, SGTase

2 Images
Western blot - Anti-GBA antibody (AB88300)
  • WB

Unknown

Western blot - Anti-GBA antibody (AB88300)

All lanes:

Western blot - Anti-GBA antibody (ab88300) at 1 µg/mL

All lanes:

U-2 OS cell lysate at 50 µg

Predicted band size: 60 kDa

Observed band size: 60 kDa

true

Western blot - Anti-GBA antibody (AB88300)
  • WB

Unknown

Western blot - Anti-GBA antibody (AB88300)

All lanes:

Western blot - Anti-GBA antibody (ab88300) at 1 µg/mL

Lane 1:

GBA transfected 293T cell lysate at 25 µg

Lane 2:

Non-transfected 293T cell lysate at 25 µg

Predicted band size: 60 kDa

Observed band size: 60 kDa

true

Key facts

Host species

Mouse

Clonality

Polyclonal

Isotype

IgG

Carrier free

Yes

Reacts with

Human

Applications

WB

applications

Immunogen

Native Full Length Protein corresponding to Human GBA1.

P04062

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Constituents: PBS
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

GBA also known as glucosylceramidase is a lysosomal enzyme with a molecular mass of approximately 59 kDa. This enzyme breaks down glucosylceramide into glucose and ceramide. GBA is expressed predominantly in tissues with high metabolic activities such as the brain liver and spleen. Its function relies on its catalytic activity where substrates bind to its active site enabling the hydrolysis process necessary for maintaining cellular metabolism.
Biological function summary

GBA plays an important role in sphingolipid metabolism. It participates in the degradation of glycolipids within the lysosome contributing to lipid recycling. It acts independently rather than as a part of a major enzymatic complex. Through its role in degrading glucosylceramide GBA influences cellular homeostasis and bioenergetics ensuring balance in neural and systemic lipid levels.

Pathways

GBA’s enzymatic functions are integral to the glycosphingolipid metabolic pathway. It is involved in the downstream steps of the lysosomal degradation of glycosphingolipids. The pathway operates alongside other important proteins such as beta-glucosidase and CERT-related transfer proteins all of which contribute to membrane lipid organization and signal transduction processes.

GBA mutations are linked with Gaucher disease and Parkinson’s disease. In Gaucher disease deficient GBA activity leads to substrate accumulation resulting in hepatosplenomegaly and other systemic symptoms. Reduced GBA activity is also associated with increased alpha-synuclein aggregation in Parkinson’s disease implicating it in the pathogenesis of neurodegenerative disorders. The enzyme’s function in these diseases highlights its role in maintaining cellular equilibrium and signaling pathways.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

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).
See full target information GBA1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

PLoS biology 23:e3003362 PubMed40934285

2025

The mTORC2 subunit RICTOR drives breast cancer progression by promoting ganglioside biosynthesis through transcriptional and epigenetic mechanisms.

Applications

Unspecified application

Species

Unspecified reactive species

Mohammad Nafees Ansari,Somesh K Jha,Ali Khan,Kajal Rajput,Nishant Pandey,Dolly Jain,Rajeshwari Tripathi,Nihal Medatwal,Pankaj Sharma,Sudeshna Datta,Animesh Kar,Trishna Pani,Sk Asif Ali,Kaushavi Cholke,Kajal Rana,Valiya P Snijesh,Geetashree Mukherjee,Suryanarayana V S Deo,Soumen Basak,Ashutosh Mishra,Jyothi S Prabhu,Arnab Mukhopadhyay,Avinash Bajaj,Ujjaini Dasgupta

Nature cell biology 26:235-249 PubMed38267537

2024

p300 nucleocytoplasmic shuttling underlies mTORC1 hyperactivation in Hutchinson-Gilford progeria syndrome.

Applications

Unspecified application

Species

Unspecified reactive species

Sung Min Son,So Jung Park,Sophia Y Breusegem,Delphine Larrieu,David C Rubinsztein
View all publications

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