RNA-binding protein 38(RBM38)

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100ug, 50ug

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Product nameRNA-binding protein 38(RBM38)
Uniprot IDQ9H0Z9
Uniprot linkhttps://www.uniprot.org/uniprot/Q9H0Z9
Expression systemProkaryotic expression
SequenceMSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLEVLFQGPLGSTLIQRTYGLTPHYIYPPAIVQPSVVIPAAPVPSLSSPYIEYTPASPAYAQYPPATYDQYPYAASPATAASFVGYSYPAAVPQALSAAAPAGTTFVQYQAPQLQPDRMQ
Molecular weight38.3kDa
Protein delivered with Tag?N-terminal GST Tag
Purity estimated>75% by SDS-PAGE
BufferPBS, pH 7.5, 4M urea
Delivery conditionDry Ice
Delivery lead time in business daysEurope: 5-7 working days
USA & Canada: 7-10 working days
Rest of the world: 5-12 working days
Storage condition4°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)
BrandProteoGenix
Host speciesEscherichia coli (E.coli)
Fragment TypeThr132-Gln239
Protein AccessionQ9H0Z9
Spec:Entrez GeneID55544
Spec:NCBI Gene AliasesRNPC1; SEB4B; SEB4D; HSRNASEB; dJ800J21.2
NCBI ReferenceQ9H0Z9
Aliases /SynonymsCLL-associated antigen KW-5,HSRNASEB,RNA-binding motif protein 38,RNA-binding region-containing protein 1,ssDNA-binding protein SEB4,RNPC1, SEB4
ReferencePX-P4832
NoteFor research use only

Description of RNA-binding protein 38(RBM38)

Introduction

RNA-binding protein 38 (RBM38) is a key player in post-transcriptional regulation of gene expression. It is a member of the RNA recognition motif (RRM) family of proteins, which are characterized by their ability to bind to RNA molecules. RBM38 is involved in a wide range of cellular processes, including RNA splicing, mRNA stability, and translation. In this article, we will explore the structure, activity, and potential applications of RBM38, with a focus on its role as a drug target.

Structure of RBM38

RBM38 is a 36-kDa protein consisting of 333 amino acids. It is composed of three main domains: an N-terminal RRM domain, a central glycine-rich region, and a C-terminal domain. The RRM domain is responsible for RNA binding and contains two conserved RNA-binding motifs, RNP1 and RNP2. The glycine-rich region is thought to be involved in protein-protein interactions, while the C-terminal domain is important for RBM38’s regulatory activity.

Activity of this protein

RBM38 is primarily known for its role in regulating mRNA stability. It has been shown to bind to the 3′ untranslated region (UTR) of target mRNAs and promote their degradation. This activity is dependent on the presence of specific sequences, known as AU-rich elements (AREs), in the 3′ UTR. RBM38 also plays a role in alternative splicing, where it can either enhance or repress exon inclusion depending on the target gene. Additionally, RBM38 has been shown to regulate translation by binding to the 5′ UTR of target mRNAs and promoting their translation.

Role of RBM38 as a Drug Target

Given its important role in post-transcriptional gene regulation, RBM38 has emerged as a potential drug target for various diseases. One such disease is cancer, where RBM38 has been shown to act as a tumor suppressor. It is downregulated in several types of cancer, and its overexpression has been shown to inhibit tumor growth and promote apoptosis. Therefore, targeting RBM38 could be a promising strategy for cancer therapy.

Another potential application of RBM38 as a drug target is in neurodegenerative diseases. RBM38 has been shown to regulate the expression of genes involved in neuronal function and survival. Its downregulation has been observed in Alzheimer’s disease and amyotrophic lateral sclerosis (ALS). Restoring RBM38 levels could potentially improve neuronal function and slow down disease progression.

Challenges and Future Directions
Despite its potential as a drug target, there are several challenges that need to be addressed before RBM38 can be effectively targeted for therapeutic purposes. One major challenge is the identification of specific small molecule inhibitors that can selectively target RBM38 without affecting other RNA-binding proteins. Additionally, the mechanism of RBM38’s regulatory activity is not fully understood, which makes it difficult to design targeted therapies.

In the future, further research is needed to fully elucidate the role of RBM38 in various diseases and identify potential therapeutic targets. This could include studying the interaction of RBM38 with other proteins and RNA molecules, as well as exploring its potential as a biomarker for disease diagnosis and prognosis.

Conclusion

In conclusion, RNA-binding protein 38 is a multifunctional protein involved in post-transcriptional gene regulation. Its structure, activity, and potential applications as a drug target make it a promising candidate for therapeutic interventions in various diseases, including cancer and neurodegenerative disorders. Further research and development in this area could lead to the discovery of novel treatments targeting RBM38 and improving patient outcomes.

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