Recombinant Human Eukaryotic Peptide Chain Release Factor Gtp-Binding Subunit Erf3A (GSPT1) Protein (MBP&His)

Beta LifeScience SKU/CAT #: BLC-04029P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Homo sapiens (Human) parvovirus B19 (isolate AU) GSPT1.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Homo sapiens (Human) parvovirus B19 (isolate AU) GSPT1.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Homo sapiens (Human) parvovirus B19 (isolate AU) GSPT1.
Based on the SEQUEST from database of Baculovirus host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from Baculovirus-expressed Homo sapiens (Human) parvovirus B19 (isolate AU) GSPT1.

Recombinant Human Eukaryotic Peptide Chain Release Factor Gtp-Binding Subunit Erf3A (GSPT1) Protein (MBP&His)

Beta LifeScience SKU/CAT #: BLC-04029P
Regular price $1,478.00 Sale price $349.00Save $1,129
/
Size

Submit an inquiry or email sales for a custom bulk quote. 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.

Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description Recombinant Human Eukaryotic Peptide Chain Release Factor Gtp-Binding Subunit Erf3A (GSPT1) Protein (MBP&His) is produced by our Baculovirus expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P15170
Target Symbol GSPT1
Synonyms GSPT1; ERF3AEukaryotic peptide chain release factor GTP-binding subunit ERF3A; Eukaryotic peptide chain release factor subunit 3a; eRF3a; G1 to S phase transition protein 1 homolog
Species Homo sapiens (Human) parvovirus B19 (isolate AU)
Expression System Baculovirus
Tag N-MBP&C-6His
Target Protein Sequence MELSEPIVENGETEMSPEESWEHKEEISEAEPGGGSLGDGRPPEESAHEMMEEEEEIPKPKSVVAPPGAPKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSNERYEECKEKLVPFLKKVGFNPKKDIHFMPCSGLTGANLKEQSDFCPWYIGLPFIPYLDNLPNFNRSVDGPIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDTVAPGENLKIRLKGIEEEEILPGFILCDPNNLCHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD
Expression Range 1-499aa
Protein Length Full Length
Mol. Weight 99.8 kDa
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 Involved in translation termination in response to the termination codons UAA, UAG and UGA. Stimulates the activity of ETF1. Involved in regulation of mammalian cell growth. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes.
Protein Families TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily
Database References

Gene Functions References

  1. PABP enhances the productive binding of the eRF1-eRF3 complex to the ribosome, via interactions with the N-terminal domain of eRF3a which itself has an active role in translation termination. PMID: 27418677
  2. Data found that the N-terminal glycine repeat of eRF3a influences eRF3a-PABP interaction and that eRF3a 12-GGC allele has a decreased binding affinity for PABP. PMID: 26818177
  3. GAB2, GSPT1, TFDP2 and ZFPM1 are four new susceptibility loci for testicular germ cell tumor. PMID: 26503584
  4. The survivin and eRF3 complex may function in spindle formation and segregation of chromosomes and cytokinesis. PMID: 23377885
  5. Overexpression of ID1 in two different cell lines induced STMN3 and GSPT1 at the transcriptional level, while depletion of ID1 reduced their expression. PMID: 25028095
  6. The proteolytic cleavage of eRF3a and eRF3b into p-eRF3 leads to release an amino-terminal fragment containing nuclear export signal to allow the relocalization of eRF3 into the nucleus to interact with the p14ARF. PMID: 24569073
  7. ERF3 is targeted for caspase-mediated proteolytic cleavage and degradation during DNA damage-induced apoptosis. PMID: 23054082
  8. Our results show that the presence of the longer allele of eRF3a is correlated with threefold increased risk of breast cancer development PMID: 22101789
  9. A biological role for the overlapping ERF3 PAM2 motifs in the regulation of deadenylase accessibility to PABPC1 at the 3' end of poly(A). PMID: 23019593
  10. crystal structures of the MLLE domain from PABPC1 in complex with the two PAM2 regions of eRF3 PMID: 20418951
  11. GSPT1/eRF3 is proteolytically processed into an IAP-binding protein PMID: 12865429
  12. Human translation termination factor eRF3/GSPT1 is an interacting partner of RNase L. PMID: 15908960
  13. Polyglycine expansions in eukaryotic translation release factor 3 are associated with gastric cancer susceptibility PMID: 15987717
  14. eRF3a controls the formation of the termination complex by modulating eRF1 protein stability. PMID: 15987998
  15. Further, we describe a novel complex that contains the NMD factors SMG-1 and Upf1, and the translation termination release factors eRF1 and eRF3 (SURF). an association between SURF and the EJC is required for SMG-1-mediated Upf1 phosphorylation and NMD. PMID: 16452507
  16. GSTP1 inhibits the binding of MAP kinase kinase kinase 5 (MAP3K5) to the 14-3-3 protein, a MAP3K5 inhibitor, while a novel role of GSPT1 is revealed in the regulation of apoptosis signal-regulating kinase 1 (ASK1)-mediated apoptosis. PMID: 17700517
  17. eRF3a is degraded by the proteasome when not associated with eRF1; proteasomal degradation of eRF3a controls translation termination complex formation by adjusting the eRF3a level to that of eRF1. PMID: 18083835
  18. eRF3a/GSPT1 12-GGC allele increases the susceptibility for breast cancer development. PMID: 19424636
  19. GSPT1 GGC(12) allele was present in 2.2% of colorectal cancer patients but was absent in Crohn disease patients and in the control group PMID: 19963113

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

Recently viewed