

| Catalog No. | HA130012 |
|---|---|
| Description |
Recombinant Human Malin Protein, N-His (HA130012) expressed in E. coli, spanning Gly112-Gly395. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | Q6VVB1 |
| Protein length | Gly112-Gly395 |
| Applications | ELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress |
| Species | Homo sapiens (Human) |
| Nature | Recombinant |
| Endotoxin level | Please contact with the lab for this information. |
| Purity | >90% as determined by SDS-PAGE. |
| Predicted molecular weight | 32.57 kDa |
| Form | Lyophilized |
| Storage buffer | Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| 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 | E3 ubiquitin-protein ligase NHLRC1, EC:2.3.2.27, EPM2B, Malin, NHL repeat-containing protein 1, NHLRC1, RING-type E3 ubiquitin transferase NHLRC1 |
| Background | E3 ubiquitin-protein ligase NHLRC1 is a ~42 kDa protein. E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. |
| Note | For research use only |
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