

| Catalog No. | HY377036 |
|---|---|
| Species reactivity | Human |
| Applications | ELISA, Bioactivity: FACS, Functional assay, Research in vivo |
| Host species | Human |
| Clonality | Monoclonal |
| Isotype | IgG1-kappa (fused with Homo sapiens GAA/glucosidase alpha) |
| Biological activity | Lysosomal α-Glucosidase is a γ-amylase that is essential for the degradation of glycogen in lysosomes [1] [2]. |
| Expression system | Mammalian cells |
| Target | Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter, 36 kDa nucleolar protein HNP36, ENT2, Equilibrative nucleoside transporter 2, SLC29A2, Hydrophobic nucleolar protein, 36 kDa, Equilibrative NBMPR-insensitive nucleoside transporter, Nucleoside transporter, ei-type, Delayed-early response protein 12, Solute carrier family 29 member 2, HNP36, DER12, GAA, Lysosomal alpha-glucosidase, Acid maltase, Aglucosidase alfa |
| Endotoxin level | < 10 EU/mg |
| Purity | >95% purity as determined by SDS-PAGE. |
| Purification | Protein A/G purified from cell culture supernatant. |
| Accession | Q14542 & P10253 |
| Form | Liquid |
| Storage buffer | 0.01M PBS pH 7.4 Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | VAL-1221 |
| Background | Clervonafusp alfa (VAL-1221) is a fusion protein targeting both cytosolic and lysosomal glycogen. Clervonafusp alfa is comprised of the Fab portion of a cell-penetrating antibody and recombinant human acid alpha glucosidase (rhGAA), the former utilizing the nucleoside transporter ENT-2 to gain access to the cytosol, and the latter enters lysosomes via mannose-6-phosphate receptors (M6PRs). Clervonafusp alfa can be used for late-onset Pompe disease research. |
| References | 1. Hermans MM, et al. Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites. The Biochemical journal. 1993 Feb 01;289 (Pt 3)(Pt 3):681-6. [HY377036] 2. Hoefsloot LH, et al. Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex. The EMBO journal. 1988 Jun;7(6):1697-704. [HY377036] |
| Note | For research use only. Not suitable for clinical or therapeutic use. |
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