|Application ||WB, IHC-P, E|
|Other Accession||NP_001121904.1, NP_066024.1|
|Calculated MW||53696 Da|
|Antigen Region||296-325 aa|
|Other Names||Cytosolic beta-glucosidase, Cytosolic beta-glucosidase-like protein 1, GBA3, CBG, CBGL1|
|Target/Specificity||This GBA3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 296-325 amino acids from the C-terminal region of human GBA3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||GBA3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. Able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. Possesses beta- glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.|
|Cellular Location||Cytoplasm, cytosol|
|Tissue Location||Present in small intestine (at protein level). Expressed in liver, small intestine, colon, spleen and kidney Down-regulated in renal cell carcinomas and hepatocellular carcinomas.|
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Provided below are standard protocols that you may find useful for product applications.
GBA3, or cytosolic beta-glucosidase (EC 184.108.40.206), is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides (de Graaf et al., 2001 [PubMed 11389701]). GBA3 also has significant neutral glycosylceramidase activity (EC 220.127.116.11), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism (Hayashi et al., 2007 [PubMed 17595169]).
Dekker, N., et al. Blood Cells Mol. Dis. (2010) In press :
Noguchi, J., et al. Biochem. Biophys. Res. Commun. 374(3):549-552(2008)
Hayashi, Y., et al. J. Biol. Chem. 282(42):30889-30900(2007)
Tribolo, S., et al. J. Mol. Biol. 370(5):964-975(2007)
Beutler, E., et al. J. Lab. Clin. Med. 144(2):65-68(2004)
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