Detection of Human Cytosolic beta ‑Glucosidase/GBA3 by Western Blot.
Western blot shows lysates of human liver tissue and human kidney tissue. PVDF membrane was probed with 1 µg/mL of Mouse Anti-Human Cytosolic beta ‑Glucosidase/GBA3 Monoclonal Antibody (Catalog # MAB5969) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for Cytosolic beta ‑Glucosidase/GBA3 at approximately 53 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Sterile PBS to a final concentration of 0.5 mg/mL.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Cytosolic beta-Glucosidase/GBA3
are three beta-glucosidases (GBA) in human genome. GBA1 endodes a
lysosomal membrane protein that cleaves the beta-glucosidic linkage of
glucosylceramide (1). GBA2 encodes a microsomal beta-glucosidase that
catalyzes the hydrolysis of bile acid 3-O-glucosides (2). GBA3 is a
cytosolic beta-glucosidase and is predominantly expressed in liver. GBA3
efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not
any known physiological beta-glycoside, suggesting that it may be
involved in detoxification of plant glycosides (3). GBA3 also has
significant neutral glycosylceramidase activity, suggesting that it may
be involved in a nonlysosomal catabolic pathway of glucosylceramide
metabolism (4). At the protein level, GBA3 shows significant homology
(>40%) with Klotho protein that is known for its association with
aging process (3, 4).
Tybulewicz, V.L. et al. (1992) Nature 357:407.
Matern, H. et al. (2001) J. Biol. Chem. 276:37929.
de Graaf, M. et al. (2001) Biochem. J. 356:907.
Hayashi, Y. et al. (2007) J. Biol. Chem. 282:30889.
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