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Brand: ProteoGenix

Recombinant Human SECISBP2 Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Human
Molecular weight:
26.71 kDa

$392.00

100ug + 392 loyalty points
Ser638–Leu854
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Recombinant Human SECISBP2 Protein, N-His

Recombinant Human SECISBP2 Protein, N-His

Product name Recombinant Human SECISBP2 Protein, N-His
Origin species Human
Expression system Prokaryotic expression
Molecular weight 26.71 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Ser638-Leu854
Aliases /Synonyms SECISBP2, SECIS-binding protein 2, SBP2, Selenocysteine insertion sequence-binding protein 2
Reference ARO-P10702
Note For research use only.
Molecular Constructor
Ser638–Leu854

Title: Introduction to Recombinant Human SECISBP2 Protein

Recombinant Human SECISBP2 Protein, also known as Selenium Binding Protein 2 (SBP2), is a highly conserved protein that plays a crucial role in the synthesis of selenoproteins. Selenoproteins are a group of proteins that contain the essential trace element selenium, and are involved in various biological processes such as antioxidant defense, thyroid hormone metabolism, and immune response. In this article, we will explore the structure, activity, and applications of Recombinant Human SECISBP2 Protein.

Title: Structure of Recombinant Human SECISBP2 Protein

The SECISBP2 gene is located on chromosome 9q22.33 and encodes for a 1031 amino acid protein. The primary structure of SECISBP2 consists of an N-terminal RNA recognition motif (RRM) and a C-terminal SECIS-binding domain (SBD). The RRM is responsible for binding to specific RNA sequences, while the SBD is responsible for binding to the SECIS element, a conserved RNA secondary structure found in the 3′ untranslated region (UTR) of selenoprotein mRNAs.

The crystal structure of the human SECISBP2 protein has been solved and reveals a dimeric protein with two RRM domains and two SBD domains. The dimerization of SECISBP2 is essential for its function as it allows for simultaneous binding to both the mRNA and the SECIS element.

Title: Activity of Recombinant Human SECISBP2 Protein

Recombinant Human SECISBP2 Protein is a key component of the selenocysteine incorporation machinery. Selenocysteine is the 21st amino acid and is encoded by the UGA codon, which is normally a stop codon. The incorporation of selenocysteine into proteins requires a specialized translation machinery that includes SECISBP2.

SECISBP2 binds to the SECIS element in the 3′ UTR of selenoprotein mRNAs and recruits other factors such as the selenocysteine-specific elongation factor (EFsec) and the selenocysteine tRNA (tRNAsec). This complex then interacts with the ribosome, allowing for the insertion of selenocysteine into the growing polypeptide chain.

Title: Applications of Recombinant Human SECISBP2 Protein

Recombinant Human SECISBP2 Protein has a wide range of applications in both basic research and clinical settings. Some of the key applications of this protein include:

1. Studying the Mechanism of Selenoprotein Synthesis: Recombinant Human SECISBP2 Protein has been used to study the mechanism of selenocysteine incorporation into proteins. This has provided insights into the role of SECISBP2 in regulating selenoprotein synthesis and its potential implications in various diseases.

2. Production of Recombinant Selenoproteins: The use of Recombinant Human SECISBP2 Protein in combination with other factors such as EFsec and tRNAsec has enabled the production of recombinant selenoproteins in various expression systems. This has allowed for the study of these proteins and their potential therapeutic applications.

3. Diagnostic and Prognostic Marker: SECISBP2 has been identified as a potential diagnostic and prognostic marker for certain diseases. For example, decreased levels of SECISBP2 have been observed in patients with thyroid cancer, making it a potential biomarker for this disease.

In conclusion, Recombinant Human SECISBP2 Protein is a crucial component of the selenocysteine incorporation machinery and has various applications in both basic research and clinical settings. Its structure and activity have been extensively studied, providing valuable insights into its role in regulating selenoprotein synthesis. Further research on this protein may lead to the development of new therapies for diseases associated with selenoprotein dysfunction.

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