GBA Antibody [K1P17] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IHC1:600

Application
WB, IHC

Reactivity
Human, Mouse, Rat

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
60 kDa 70 kDa, 60 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
GBA Antibody [K1P17] detects endogenous levels of total GBA protein.

Clone
K1P17

Synonym(s)
GBA, GC, GLUC, GBA1, Glucosylceramidase beta 1, Imiglucerase, Lysosomal glycosylceramidase, Beta-GC, SGTase

Background
GBA (GBA1, glucocerebrosidase) is a lysosomal glycosidase in the sphingolipid catabolic pathway that hydrolyzes glucosylceramide to ceramide and glucose using a retaining mechanism with catalytic glutamate residues, which operate in the acidic lumen to form and resolve a covalent glycosyl–enzyme intermediate. The protein folds into a (β/α)₈‑like catalytic domain with auxiliary regions that support binding to the lysosomal membrane protein LIMP‑2 and formation of functional dimers, providing correct trafficking to lysosomes and a stable configuration for substrate recognition and catalysis. GBA activity decreases lysosomal glucosylceramide levels and generates ceramide that can be converted to more complex sphingolipids or further metabolized, and this enzymatic step contributes to the composition of lysosomal and cellular membranes as well as to pools of bioactive ceramide species. Changes in glucosylceramide and ceramide content influence the physical properties of lysosomal membranes and the efficiency of degradation of macromolecules delivered by endocytosis and autophagy, linking GBA activity to general lysosomal proteolysis and lipid recycling. Biallelic pathogenic variants in GBA cause Gaucher disease, which is characterized by deficient glucocerebrosidase activity, accumulation of glucosylceramide and related lipids in macrophage lysosomes, formation of lipid‑laden Gaucher cells, and enlargement and dysfunction of spleen, liver, and bone marrow. Heterozygous and homozygous GBA variants occur at higher frequency in Parkinson’s disease than in control populations, and reduced glucocerebrosidase activity is detected in brain tissue from carriers and non‑carriers with Parkinson’s disease.

Background

GBA (GBA1, glucocerebrosidase) is a lysosomal glycosidase in the sphingolipid catabolic pathway that hydrolyzes glucosylceramide to ceramide and glucose using a retaining mechanism with catalytic glutamate residues, which operate in the acidic lumen to form and resolve a covalent glycosyl–enzyme intermediate. The protein folds into a (β/α)₈‑like catalytic domain with auxiliary regions that support binding to the lysosomal membrane protein LIMP‑2 and formation of functional dimers, providing correct trafficking to lysosomes and a stable configuration for substrate recognition and catalysis. GBA activity decreases lysosomal glucosylceramide levels and generates ceramide that can be converted to more complex sphingolipids or further metabolized, and this enzymatic step contributes to the composition of lysosomal and cellular membranes as well as to pools of bioactive ceramide species. Changes in glucosylceramide and ceramide content influence the physical properties of lysosomal membranes and the efficiency of degradation of macromolecules delivered by endocytosis and autophagy, linking GBA activity to general lysosomal proteolysis and lipid recycling. Biallelic pathogenic variants in GBA cause Gaucher disease, which is characterized by deficient glucocerebrosidase activity, accumulation of glucosylceramide and related lipids in macrophage lysosomes, formation of lipid‑laden Gaucher cells, and enlargement and dysfunction of spleen, liver, and bone marrow. Heterozygous and homozygous GBA variants occur at higher frequency in Parkinson’s disease than in control populations, and reduced glucocerebrosidase activity is detected in brain tissue from carriers and non‑carriers with Parkinson’s disease.

References
https://pubmed.ncbi.nlm.nih.gov/32182893/ https://pubmed.ncbi.nlm.nih.gov/28485919/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%