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Brand: ProteoGenix

Recombinant Mouse YTHDF2/HGRG8, N-GST

Host species:
Escherichia coli (E.coli)
Origin species:
Mouse
Molecular weight:
89.07 kDa

$392.00

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Met1–Lys579
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Recombinant Mouse YTHDF2/HGRG8, N-GST

Recombinant Mouse YTHDF2/HGRG8, N-GST

Product name Recombinant Mouse YTHDF2/HGRG8, N-GST
Origin species Mouse
Expression system Prokaryotic expression
Molecular weight 89.07 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 Met1-Lys579
Aliases /Synonyms YTH domain-containing family protein 2, High-glucose-regulated protein 8, Renal carcinoma antigen NY-REN-2, DF2, HGRG8, YTHDF2, CLL-associated antigen KW-14
Reference ARO-P12888
Note For research use only.
Molecular Constructor
Met1–Lys579

Introduction

Recombinant Mouse YTHDF2/HGRG8 is a protein that plays a crucial role in post-transcriptional regulation of gene expression. It belongs to the YTH domain-containing family of proteins, which are characterized by the presence of a conserved YTH domain that binds to N6-methyladenosine (m6A) modified RNA. YTHDF2 is a highly conserved protein, with homologues found in a variety of species including humans, mice, and other mammals. In this article, we will discuss the structure, activity, and application of recombinant mouse YTHDF2/HGRG8.

Structure of Recombinant Mouse YTHDF2/HGRG8

The recombinant mouse YTHDF2/HGRG8 protein is composed of 452 amino acids and has a molecular weight of approximately 52 kDa. It consists of an N-terminal YTH domain, a central low-complexity region, and a C-terminal proline-rich region. The YTH domain is responsible for binding to m6A-modified RNA, while the low-complexity region is involved in protein-protein interactions. The proline-rich region is thought to play a role in the regulation of YTHDF2 activity.

Activity of Recombinant Mouse YTHDF2/HGRG8

The main activity of recombinant mouse YTHDF2/HGRG8 is its ability to recognize and bind to m6A-modified RNA. This binding leads to the recruitment of other proteins, such as the CCR4-NOT deadenylase complex, which promotes the degradation of the target RNA. This process, known as m6A-mediated mRNA decay (MMD), is an important mechanism for regulating gene expression.

In addition to its role in MMD, YTHDF2 has also been implicated in other processes such as translation regulation and mRNA splicing. It has been shown to interact with various proteins involved in these processes, suggesting that YTHDF2 may have multiple functions in post-transcriptional gene regulation.

Application of Recombinant Mouse YTHDF2/HGRG8

Recombinant mouse YTHDF2/HGRG8 has a wide range of applications in both basic research and biotechnology. One major application is in the study of m6A-mediated gene regulation. By using recombinant YTHDF2, researchers can investigate the role of this protein in various cellular processes and its impact on gene expression.

Another important application of recombinant mouse YTHDF2/HGRG8 is in the development of therapeutics. As m6A has been linked to various diseases, including cancer and neurological disorders, targeting m6A-modified RNA with recombinant YTHDF2 could potentially lead to the development of novel treatments.

Furthermore, recombinant YTHDF2 can be used in high-throughput screening assays to identify small molecule inhibitors or activators of its binding activity. This could aid in the discovery of new drugs that target m6A-mediated gene regulation.

Conclusion

In summary, recombinant mouse YTHDF2/HGRG8 is a highly conserved protein with a crucial role in post-transcriptional gene regulation. Its ability to recognize and bind to m6A-modified RNA makes it an important player in processes such as mRNA decay, translation regulation, and mRNA splicing. Its diverse functions and potential applications in basic research and biotechnology make it a valuable tool for studying and targeting m6A-mediated gene regulation.

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