Recombinant Human Eukaryotic Translation Initiation Factor 5 (EIF5) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-09909P

Greater than 90% as determined by SDS-PAGE.
Recombinant Human Eukaryotic Translation Initiation Factor 5 (EIF5) Protein (His-SUMO)
Beta LifeScience
SKU/CAT #: BLC-09909P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Eukaryotic Translation Initiation Factor 5 (EIF5) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P55010 |
Target Symbol | EIF5 |
Synonyms | 2810011H21Rik; D12Ertd549e; EIF 5; EIF 5A; eIF-5; Eif5; Eukaryotic initiation factor 5; Eukaryotic translation initiation factor 5; IF5_HUMAN; MGC36374; MGC36509 |
Species | Homo sapiens (Human) |
Expression System | E.coli |
Tag | N-6His-SUMO |
Target Protein Sequence | MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPPPPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRMDEISDHAKVLTLSDDLERTIEERVNILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKAASVPKVETVKSDNKDDDIDIDAI |
Expression Range | 1-431aa |
Protein Length | Full Length |
Mol. Weight | 65.2kDa |
Research Area | Epigenetics And Nuclear Signaling |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F]). |
Protein Families | EIF-2-beta/eIF-5 family |
Database References |
Gene Functions References
- The down-regulation of the GCN4 expression (Gcn(-) phenotype) in the eIF5(G31R) mutant was not because of leaky scanning defects; rather was due to the utilization of upUUG initiation codons at the 5' regulatory region present between uORF1 and the main GCN4 ORF. PMID: 28385532
- overexpression of eIF5 and 5MP induces translation of ATF4 PMID: 27325740
- it is eIF5-induced GTP hydrolysis and Pi release that irreversibly trap the 48S complex, and this complex is further stabilized by eIF5B and 60S joining. PMID: 26717981
- The N-terminal tail of eIF1A mediates the interaction with eIF5 and eIF1. PMID: 24319994
- This study provides mechanistic insight into the role of eIF5-carboxyl terminal domain's dynamic interplay with eIF1 and eIF2beta. PMID: 22813744
- miR-5787 represses cell growth, in part, by targeting eIF5. PMID: 22062548
- 3-dimensional solution structure of N-terminal domain of human eIF5, has 2 subdomains, both reminiscent of nucleic-acid-binding modules. N-terminal subdomain contains "arginine finger" motif essential for GAP function. PMID: 16584190
- The carboxy-terminal domain (CTD)of eIF5 is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. PMID: 16781736