Recombinant Human GBA3/CBGL1 Protein (His Tag) (PKSH031073)
For research use only.
| Synonyms | CBG, CBGL1, GBA3, GLUC, KLrP, MGC104276, MGC126878 |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Met 1-Leu 469 |
| Accession | NP_066024.1 |
| Calculated Molecular Weight | 55.0 kDa |
| Observed Molecular Weight | 50 kDa |
| Tag | C-His |
| Bio-activity | Measured by its ability to hydrolyze 4-methylumbelliferyl-β-D glucopyranoside. The specific activity is > 1, 500 pmoles/min/μg. |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation |
Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4 Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
| Background | Cytosolic beta-glucosidase, also known as Cytosolic beta-glucosidase-like protein 1, GBA3, CBG and CBGL1 is a cytoplasm protein which belongs to theglycosyl hydrolase 1 family and Klotho subfamily. GBA3 / CBGL1 is a glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. GBA3 / CBGL1 is present in small intestine (at protein level). GBA3 / CBGL1 is expressed in liver, small intestine, colon, spleen and kidney. GBA3 / CBGL1 is down-regulated in renal cell carcinomas and hepatocellular carcinomas. GBA3 / CBGL1 is able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. GBA3 / CBGL1 possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide. |
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