"mRNA"

Supplier: Bioss

Fas ligand associated factor 1; Fas ligand-associated factor 1; FBP 11; FBP11; FLAF 1; FLAF1; FNBP 3; Formin binding protein 11; Formin binding protein 3; Formin-binding protein 11; Formin-binding protein 3; HIP-10; HIP10; Huntingtin interacting protein A; Huntingtin interacting protein HYPA; Huntingtin yeast partner A; Huntingtin-interacting protein 10; Huntingtin-interacting protein A; HYPA; NY REN 6; NY REN 6 antigen; PR40A_HUMAN; Pre mRNA processing factor 40 homolog A; Pre-mRNA-processing factor 40 homolog A; PRP40 pre mRNA processing factor 40 homolog A (S cerevisiae); PRP40 pre mRNA processing factor 40 homolog A (yeast); PRP40 pre mRNA processing factor 40 homolog A; PRPF 40A; PRPF40A; Renal carcinoma antigen NY-REN-6.

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 Inc.

IREB2 is a RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase mRNAs, and in the 3'-UTR of transferrin receptor mRNA. Binding to the IRE element in ferritin results in the repression of its mRNA translation. Binding of the protein to the transferrin receptor mRNA inhibits the degradation of this otherwise rapidly degraded mRNA.

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

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: 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

Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific.

Supplier: Bioss

IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2) is also known as IGF2 mRNA-binding protein 2, IMP-2 (IGF-II mRNA-binding protein 2), VICKZ family member 2 or hepatocellular carcinoma autoantigen p62 and is a 556 amino acid protein. IGF2BP2 is expressed in a variety of tissues including heart, placenta, skeletal muscle, pancreas, fetal liver, lung, kidney, thymus and gonadal cells. IGF2BP2 is an RNA binding protein which may be involved in the regulation of mRNA translation and may also function to control the spatial localization of target mRNAs. against IGF2BP2 have been detected in patients with HCC (hepatocellular carcinoma), suggesting that IGF2BP2 may have a role in the pathogenesis of HCC. Defects in IGF2BP2 are thought to be associated with susceptibility to type 2 diabetes mellitus.

Supplier: Bioss

IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2) is also known as IGF2 mRNA-binding protein 2, IMP-2 (IGF-II mRNA-binding protein 2), VICKZ family member 2 or hepatocellular carcinoma autoantigen p62 and is a 556 amino acid protein. IGF2BP2 is expressed in a variety of tissues including heart, placenta, skeletal muscle, pancreas, fetal liver, lung, kidney, thymus and gonadal cells. IGF2BP2 is an RNA binding protein which may be involved in the regulation of mRNA translation and may also function to control the spatial localization of target mRNAs. against IGF2BP2 have been detected in patients with HCC (hepatocellular carcinoma), suggesting that IGF2BP2 may have a role in the pathogenesis of HCC. Defects in IGF2BP2 are thought to be associated with susceptibility to type 2 diabetes mellitus.

Supplier: Bioss

IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2) is also known as IGF2 mRNA-binding protein 2, IMP-2 (IGF-II mRNA-binding protein 2), VICKZ family member 2 or hepatocellular carcinoma autoantigen p62 and is a 556 amino acid protein. IGF2BP2 is expressed in a variety of tissues including heart, placenta, skeletal muscle, pancreas, fetal liver, lung, kidney, thymus and gonadal cells. IGF2BP2 is an RNA binding protein which may be involved in the regulation of mRNA translation and may also function to control the spatial localization of target mRNAs. against IGF2BP2 have been detected in patients with HCC (hepatocellular carcinoma), suggesting that IGF2BP2 may have a role in the pathogenesis of HCC. Defects in IGF2BP2 are thought to be associated with susceptibility to type 2 diabetes mellitus.

Supplier: Bioss

IGF2BP2 (insulin-like growth factor 2 mRNA binding protein 2) is also known as IGF2 mRNA-binding protein 2, IMP-2 (IGF-II mRNA-binding protein 2), VICKZ family member 2 or hepatocellular carcinoma autoantigen p62 and is a 556 amino acid protein. IGF2BP2 is expressed in a variety of tissues including heart, placenta, skeletal muscle, pancreas, fetal liver, lung, kidney, thymus and gonadal cells. IGF2BP2 is an RNA binding protein which may be involved in the regulation of mRNA translation and may also function to control the spatial localization of target mRNAs. against IGF2BP2 have been detected in patients with HCC (hepatocellular carcinoma), suggesting that IGF2BP2 may have a role in the pathogenesis of HCC. Defects in IGF2BP2 are thought to be associated with susceptibility to type 2 diabetes mellitus.

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

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5,8S rRNA 3'-end processing. Also binds to 5,8S ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.

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: 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: Bioss

RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5,8S rRNA 3'-end processing. Also binds to 5,8S ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.