Recombinant Human EIF5 Protein (GST Tag)

Name: Recombinant Human EIF5 Protein (GST Tag)
Brand: Beta LifeScience
SKU: BLPSN-1743
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	P55010
Synonym	EIF-5, EIF-5A
Background	EIF-5A, also known as EIF5, functions in start site selection as a GTPase accelerating protein (GAP) for the eukaryotic translation initiation factor (eIF) 2-€¢GTP-€¢tRNA ternary complex within the ribosome-bound pre-initiation complex. In protein synthesis initiation, eIF2 functions in its GTP-bound state to deliver initiator methionyl-tRNA to the small ribosomal subunit and is necessary for protein synthesis in all cells. EIF-5A stabilizes the binding of GDP to eIF2 and is therefore a bi-functional protein that acts as a GDP dissociation inhibitor (GDI). EIF-5A also interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 4S ribosome subunit.
Description	A DNA sequence encoding the mature form of human EIF5 (P55010) (Met1-Asp150) was fused with the GST tag at the N-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Met1-Asp150
Molecular Weight	The recombinant human EIF5 /GST chimera consists of 384 a.a. and has a predicted molecular mass of 44.1 kDa. It migrates as an approximately 38-43 KDa band in SDS-PAGE under reducing conditions.
Purity	>95% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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	HGNC: 3299 OMIM: 601710 KEGG: hsa:1983 STRING: 9606.ENSP00000216554 UniGene: Hs.433702

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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.