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Description: Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity.

Catalog Number: 10290-280

Supplier: Bioss

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Description: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.

Catalog Number: 10392-888

Supplier: Bioss

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Description: Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.

Catalog Number: 10392-890

Supplier: Bioss

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Description: The selective RNA-binding protein FMRP forms a messenger ribonucleoprotein complex that associates with polyribosomes, implicating in regulation of translation. FMR1 is a component of the CYFIP1-EIF4E-FMR1 complex which binds to and reperss the mRNA. It also has a role in the transport of mRNA from the nucleus to the cytoplasm.

Catalog Number: 10087-082

Supplier: Proteintech

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Description: The exosome is a multi-subunit complex composed of several highly conserved proteins, some of which are 3’ to 5’ exoribonucleases. The complex is involved in a variety of cellular processes and is responsible for degrading unstable mRNAs that contain AU-rich (ARE) elements in their untranslated 3’ region. EXOSC10, also known as PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl, or PM/Scl-100, is an 885 amino acid protein that contains one HRDC domain and one 3’-5’ enonuclease domain. Localized to both the cytoplasm and the nucleus, EXOSC10 is part of the post-splicing exosome complex and is involved in mRNA surveillance, mRNA nuclear export and nonsense-mediated decay of mRNAs containing premature stop codons. against EXOSC10 have been found in patients with scleroderma and/or polymyositis (chronic diseases of the skin and muscle, respectively), suggesting that EXOSC10 may be involved in the pathogenesis of these diseases. Two isoforms of EXOSC10 exist due to alternative splicing events.

Catalog Number: 10292-826

Supplier: Bioss

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Description: Intracellular transport is critical to cellular functions and the maintenance of its integrity (membrane renewal, vesicles trafficking, cell division, mRNA transport, etc.).

Catalog Number: RL100401E80

Supplier: Rockland Immunochemical

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Description: MRTO4 is a protein sharing a low level of sequence similarity with ribosomal protein P0. While the precise function of the protein is currently unknown, it appears to be involved in mRNA turnover and ribosome assembly.This gene encodes a protein sharing a low level of sequence similarity with ribosomal protein P0. While the precise function of the encoded protein is currently unknown, it appears to be involved in mRNA turnover and ribosome assembly.

Catalog Number: 10109-656

Supplier: Prosci

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Description: CA150 is a nuclear protein that regulates transcriptional elongation and pre-mRNA splicing. It interacts with the hyperphosphorylated C-terminal domain of RNA polymerase II via multiple FF domains, and with the pre-mRNA splicing factor SF1 via a WW domain.

Catalog Number: 10454-974

Supplier: Bioss

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Description: 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.

Catalog Number: 10071-830

Supplier: Prosci

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Description: Involved in alternative pre-RNA splicing and regulation of mRNA translation by binding to AU-rich elements (AREs) located in mRNA 3' untranslated regions (3' UTRs). Possesses nucleolytic activity against cytotoxic lymphocyte target cells. May be involved in apoptosis.

Catalog Number: 10461-836

Supplier: Bioss

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Description: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.

Catalog Number: 10459-386

Supplier: Bioss

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Description: Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.

Catalog Number: 10459-390

Supplier: Bioss

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Description: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism and transport of nuclear pre-mRNA transcripts. hnRNP A1 regulates the alternative splicing of c-Src, c-H-Ras and modifies initiation of translation of the fibroblast growth factor 2 mRNA. hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells. Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus. hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production. HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm ,

Catalog Number: 10069-094

Supplier: Prosci

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Description: Gle1 Antibody: The proper expression of gene products in eukaryotic cells relies on efficient transport of mRNA molecules out of the nucleus. Gle1 is an essential mRNA export factor in both human and yeast cells. It associates with the nuclear pore complex (NPC) through hCG1 and NUP155 in mammalian cells and in conjunction with inositol hexakisphosphate (IP6), stimulates Dbp5, a member of the DEAD-box helicase family, triggering mRNP remodeling and facilitating RNA export from the nucleus. Recent evidence suggests that mutations in Gle1 causing defects in mRNA export can result in human disease. At least three isoforms of Gle1 are known to exist.

Catalog Number: 89416-852

Supplier: Prosci

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Description: HNRPDL belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. HNRPDL has two RRM domains that bind to RNAs.

Catalog Number: 10108-090

Supplier: Prosci

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Description: 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.

Catalog Number: 10406-032

Supplier: Bioss

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