| Host: | E.coli |
| Applications: | SDS-PAGE |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description : | Recombinant-Human DERP6/ELP5-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications. |
| Formulation: | Liquid in 20mM Tris-HCl buffer (pH 8.0) containing 0.15M NaCl, 20% Glycerol, 1mM DTT |
| Concentration: | 0.25 mg/mL |
| Storage Instruction: | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
| Gene Symbol: | ELP5 |
| Gene ID: | 23587 |
| Uniprot ID: | ELP5_HUMAN |
| Immunogen Region: | 1-316aa |
| Accession Number: | NP_056177 |
| Immunogen: | Human |
| Immunogen Sequence: | MGSSHHHHHH SSGLVPRGSH MGSMTPSEGA RAGTGRELEM LDSLLALGGL VLLRDSVEWE GRSLLKALVK KSALCGEQVH ILGCEVSEEE FREGFDSDIN NRLVYHDFFR DPLNWSKTEE AFPGGPLGAL RAMCKRTDPV PVTIALDSLS WLLLRLPCTT LCQVLHAVSH QDSCPGDSSS VGKVSVLGLL HEELHGPGPV GALSSLAQTE VTLGGTMGQA SAHILCRR |
| Tissue Specificity | Ubiquitously expressed with high levels in heart, brain, liver, skeletal muscle and testis. |
| Post Translational Modifications | Tyrosine-phosphorylated. |
| Function | Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. Involved in cell migration. |
| Protein Name | Elongator Complex Protein 5Dermal Papilla-Derived Protein 6S-Phase 2 Protein |
| Database Links | Reactome: R-HSA-3214847 |
| Cellular Localisation | NucleusCytoplasm |
| Alternative Protein Names | Elongator Complex Protein 5 proteinDermal Papilla-Derived Protein 6 proteinS-Phase 2 Protein proteinELP5 proteinC17orf81 proteinDERP6 proteinHSPC002 proteinMSTP071 protein |
Information sourced from Uniprot.org