"mRNA"

Supplier: Prosci

RBM22 may be involved in pre-mRNA splicing.

Supplier: Bioss

Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.

Supplier: Prosci

IGF2BP1 is a member of the IGF-II mRNA-binding protein (IMP) family. The protein contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation.This gene encodes a member of the IGF-II mRNA-binding protein (IMP) family. The protein encoded by this gene contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation.This gene encodes a member of the IGF-II mRNA-binding protein (IMP) family. The protein encoded by this gene contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Bioss

Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.

Supplier: Bioss

Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.

Supplier: Prosci

IGF2BP1 is a member of the IGF-II mRNA-binding protein (IMP) family. The protein contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation.This gene encodes a member of the IGF-II mRNA-binding protein (IMP) family. The protein encoded by this gene contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. This gene encodes a member of the IGF-II mRNA-binding protein (IMP) family. The protein encoded by this gene contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Bioss

Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome.

Supplier: Bioss

Part of pre- and post-splicing multiprotein mRNP complexes. Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by bridging together sequence-specific (SR family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA 3'-end cleavage independently of the formation of an exon junction complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with low sequence specificity and has similar preference for either double- or single-stranded nucleic acid substrates.

Supplier: Prosci

EIF4G3 is probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. It is thought to be a functional homolog of EIF4G1.

Supplier: Proteintech

Introns are removed from nuclear pre-mRNA in 2-step transesterification reactions. Splicing occured in a large ribonucleoprotein particle, called the spliceosome. Spliceosomal intermediate complexes form on pre-mRNA in the order E, A, B, and C, with the catalytic reactions occurring in complex C. U2 small nuclear ribonucleoproteins are one of the proteins essential for spliceosome assembly and mRNA splicing. Functional U2 snRNP is composed of a 12S unit and 2 splicing factors, SF3A, which is composed of 3 proteins, and SF3B, which conposed of 4 proteins. SF3B3 is one of SF3B, and it's required for 'A' complex assembly formed by the stable binding of U2 snRNP to the brachpoint sequence(BPS) in pre-mRNA.

Supplier: Bioss

Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Regulates the transcription of numerous genes. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds preferentially to the 5'-[CU]CUGCG-3' motif in vitro. The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation.

Supplier: Bioss

eIF4B is required for the binding of mRNA to ribosomes. It functions in close association with eIF4F and eIF4A. It binds near the 5'-terminal cap of mRNA in the presence of eIF4F and ATP. It promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both eIF4A and eIF4F.

Supplier: Prosci

Poly (A)-binding proteins (PABPs) bind to the poly (A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.Poly (A)-binding proteins (PABPs) bind to the poly (A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules.Poly (A)-binding proteins (PABPs) bind to the poly (A) tail present at the 3-prime ends of most eukaryotic mRNAs. PABPC4 or IPABP (inducible PABP) was isolated as an activation-induced T-cell mRNA encoding a protein. Activation of T cells increased PABPC4 mRNA levels in T cells approximately 5-fold. PABPC4 contains 4 RNA-binding domains and proline-rich C terminus. PABPC4 is localized primarily to the cytoplasm. It is suggested that PABPC4 might be necessary for regulation of stability of labile mRNA species in activated T cells. PABPC4 was also identified as an antigen, APP1 (activated-platelet protein-1), expressed on thrombin-activated rabbit platelets. PABPC4 may also be involved in the regulation of protein translation in platelets and megakaryocytes or may participate in the binding or stabilization of polyadenylates in platelet dense granules. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Bioss

Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.

Supplier: Genetex

Rabbit Polyclonal antibody to SERBP1 (SERPINE1 mRNA binding protein 1)

Supplier: Prosci

NOB1 may play a role in mRNA degradation.