"mRNA"

Supplier: ProSci Inc.

DCP2 is necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. DCP2 removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. It has higher activity towards mRNAs that lack a poly (A) tail, but has no activity towards a cap structure lacking a RNA moiety.DCP2 is a key component of an mRNA-decapping complex required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end (Fenger-Gron et al., 2005 [PubMed 16364915]).

Supplier: Bioss

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.

Supplier: Bioss

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.

Supplier: G-Biosciences

Immunotag™ Mouse Pre-mRNA-splicing regulator WTAP ELISA Kit

Supplier: ProSci Inc.

LIN28 acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. The association of LIN28 with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. IT binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. LIN28 is Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression.

Supplier: G-Biosciences

Immunotag™ Human WTAP (Pre-mRNA-splicing regulator WTAP) ELISA Kit

Supplier: Bioss

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

Supplier: Bioss

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

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

Involved in histone 3'-end pre-mRNA processing by associating with U7 snRNP and interacting with SLBP/pre-mRNA complex. Increases histone 3'-end pre-mRNA processing but has no effect on U7 snRNP levels, when overexpressed. Required for cell cycle progression from G1 to S phases.

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

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

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

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: ProSci Inc.

UPF2 is a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA surveillance. mRNA surveillance detects exported mRNAs with truncated open reading frames and initiates nonsense-mediated mRNA decay (NMD). When translation ends upstream from the last exon-exon junction, this triggers NMD to degrade mRNAs containing premature stop codons. This protein is located in the perinuclear area. It interacts with translation release factors and the proteins that are functional homologs of yeast Upf1p and Upf3p.