Human TERT protein (Recombinant) (N-GST) (STJP003193)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human TERT-N-GST protein was developed from e.coli for the region N-GST. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | 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. |
Target Information
| Gene Symbol | TERT |
| Gene ID | 7015 |
| Uniprot ID | TERT_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Arg787-Arg1084 |
Additional Info
| Post Translational Modifications | Phosphorylation at Tyr-707 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation at Ser-227 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-457 by DYRK2 promotes ubiquitination by the EDVP complex and degradation. Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-457 by DYRK2. Ubiquitinated leads to proteasomal degradation. (Microbial infection) In case of infection by HIV-1, the EDVP complex is hijacked by HIV-1 via interaction between HIV-1 Vpr and DCAF1/VPRBP, leading to ubiquitination and degradation. |
| Function | Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis. |
| Protein Name | Telomerase Reverse TranscriptaseHest2Telomerase Catalytic SubunitTelomerase-Associated Protein 2Tp2 |
| Database Links | Reactome: R-HSA-171319Reactome: R-HSA-201722Reactome: R-HSA-9825895 |
| Cellular Localisation | NucleusNucleolusNucleoplasmChromosomeTelomereCytoplasmPml BodyShuttling Between Nuclear And Cytoplasm Depends On Cell CyclePhosphorylation StatesTransformation And Dna DamageDiffuse Localization In The NucleoplasmEnriched In Nucleoli Of Certain Cell TypesTranslocated To The Cytoplasm Via Nuclear Pores In A Crm1/Ran-Dependent Manner Involving Oxidative Stress-Mediated Phosphorylation At Tyr-707Dephosphorylation At This Site By Shp2 Retains Tert In The NucleusTranslocated To The Nucleus By Phosphorylation By Akt |
| Alternative Protein Names | Telomerase Reverse Transcriptase proteinHest2 proteinTelomerase Catalytic Subunit proteinTelomerase-Associated Protein 2 proteinTp2 proteinTERT proteinEST2 proteinTCS1 proteinTRT protein |
Information sourced from Uniprot.org