

| Catalog No. | HX195012 |
|---|---|
| Description |
Recombinant Human SRP54 Protein, N-His (HX195012) expressed in E. coli, spanning Met1-Met504. Purity: >90% by SDS-PAGE.
Highlights
|
| Expression system | E. coli |
| Accession | P61011 |
| Protein length | Met1-Met504 |
| 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 | 57.87 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 | EC:3.6.5.4, SRP54, Signal recognition particle 54 kDa protein, Signal recognition particle subunit SRP54 |
| Background | Signal recognition particle subunit SRP54 is a ~55 kDa protein. Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane. Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes. Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA. 1. Lee, JH. et al. (2021) Science advances 7. PMID: 34020957 2. Carapito, R. et al. (2017) The Journal of clinical investigation 127, 4090-4103. PMID: 28972538 3. Bellanné-Chantelot, C. et al. (2018) Blood 132, 1318-1331. PMID: 29914977 |
| Note | For research use only |
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