You Searched For: viral+rna

Catalog Number: (10277-930)

Supplier: Bioss

Description: RNA-binding protein that regulates alternative splicing events by binding to 5'-UGCAUGU-3' elements. Prevents binding of U2AF2 to the 3'-splice site. Regulates alternative splicing of tissue-specific exons and of differentially spliced exons during erythropoiesis (By similarity). RNA-binding protein that seems to act as a coregulatory factor of ER-alpha.

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Catalog Number: (76171-866)

Supplier: Boster Biological Technology

Description: Rabbit IgG polyclonal antibody for RNA-binding protein Musashi homolog 1(MSI1) detection. Tested with WB, IHC-P in Human;Mouse;Rat.

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Catalog Number: (101414-766)

Supplier: Omega Bio-Tek

Description: 200mL

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Catalog Number: (10478-486)

Supplier: Bioss

Description: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.

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Catalog Number: (10478-180)

Supplier: Bioss

Description: Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II.

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Catalog Number: (10262-024)

Supplier: Bioss

Description: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription (PubMed:19515850, PubMed:21700224). Contributes to the mRNA splicing efficiency and splice site selection (PubMed:19515850). Required for the resolution of R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site, allowing XRN2 recruitment and XRN2-mediated degradation of the downstream cleaved RNA and hence efficient RNA polymerase II (RNAp II) transcription termination (PubMed:19515850, PubMed:21700224). Required for the 3' transcriptional termination of PER1 and CRY2, thus playing an important role in the circadian rhythm regulation (By similarity). Involved in DNA double-strand breaks damage response generated by oxidative stress (PubMed:17562789). In association with RRP45, targets the RNA exosome complex to sites of transcription-induced DNA damage (PubMed:24105744). Plays a role in the development and maturation of germ cells: essential for male meiosis, acting at the interface of transcription and meiotic recombination, and in the process of gene silencing during meiotic sex chromosome inactivation (MSCI) (By similarity). May be involved in telomeric stability through the regulation of telomere repeat-containing RNA (TERRA) transcription (PubMed:21112256). Plays a role in neurite outgrowth in hippocampal cells through FGF8-activated signaling pathways. Inhibits retinoic acid-induced apoptosis (PubMed:21576111).

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Catalog Number: (10108-384)

Supplier: Prosci

Description: PNPT1 is a subunit of the exosome complex, which is involved in 3-prime-to-5-prime exoribonuclease activity for RNA processing and degradation.PNPT1 is a subunit of the exosome complex, which is involved in 3-prime-to-5-prime exoribonuclease activity for RNA processing and degradation (Raijmakers et al., 2002 [PubMed 12419256]).

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Catalog Number: (10283-926)

Supplier: Bioss

Description: LRRFIP1 is an 738 amino acid human protein whose rodent counterpart is known as Lrrfip1 (also designated FLAP in mouse). LRRFIP1 is also believed to control smooth muscle cell proliferation following arterial injury through PDGF-A repression. The N-terminus of LRRFIP1 shows high homology to the coiled-coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I, and the interaction of LRRFIP1 with the LRR of Flightless I has been confirmed. LRRFIP1 does not bind single-stranded DNA or RNA significantly and binds double-stranded DNA weakly. In contrast, LRRFIP1 binds double-stranded RNA with high affinity, and two molecules of LRRFIP1 bind the TaR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. Flightless I has a C-terminal TaR-like domain which binds Actin and therefore the association of LRRFIP1 with the LRR of Flightless I may provide a link between the Actin cytoskeleton and RNA in mammalian cells.

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Catalog Number: (10283-930)

Supplier: Bioss

Description: LRRFIP1 is an 738 amino acid human protein whose rodent counterpart is known as Lrrfip1 (also designated FLAP in mouse). LRRFIP1 is also believed to control smooth muscle cell proliferation following arterial injury through PDGF-A repression. The N-terminus of LRRFIP1 shows high homology to the coiled-coil domain of FLAP, a protein which binds the leucine-rich repeat (LRR) of Flightless I, and the interaction of LRRFIP1 with the LRR of Flightless I has been confirmed. LRRFIP1 does not bind single-stranded DNA or RNA significantly and binds double-stranded DNA weakly. In contrast, LRRFIP1 binds double-stranded RNA with high affinity, and two molecules of LRRFIP1 bind the TaR stem. The RNA binding domain has been identified and encompasses a lysine-rich motif. Flightless I has a C-terminal TaR-like domain which binds Actin and therefore the association of LRRFIP1 with the LRR of Flightless I may provide a link between the Actin cytoskeleton and RNA in mammalian cells.

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Catalog Number: (10486-240)

Supplier: Bioss

Description: Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle, that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein), also designated MEN, functions as an RNA polymerase II elongation factor that increases the rate of transcription by suppressing transient pausing by RNA polymerase II. It is also thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, with lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary. The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes that undergo translocation with the MLL gene on chromosome 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia, also designated ALL-1 and HRX) regulates embryonal and hematopoietic development.

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Supplier: MilliporeSigma

Description: Ribonuclease A, Protease-Free is a chromatographically purified, pyrimidine-specific endoribonuclease that acts on single-stranded RNA

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Catalog Number: (77439-656)

Supplier: Bioss

Description: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.

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Supplier: New England Biolabs (NEB)

Description: The NEBNext® rRNA Depletion Kit v2 features an improved probe design targeting all subunits of human pre-rRNA (5S, 5.8S, 18S, 28S, ITS, ETS), better coverage of mouse and rat mature rRNA, as well as improved enzyme formulations.

Catalog Number: (89354-924)

Supplier: Genetex

Description: Rabbit polyclonal antibody to PAF1 (PAF1, RNA polymerase II associated factor, homolog (S. cerevisiae))

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Catalog Number: (10108-440)

Supplier: Prosci

Description: RBM45 is a RNA-binding protein with binding specificity for poly (C). It May play an important role in neural development. RBM45 contains 3 RRM (RNA recognition motif) domains.

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Catalog Number: (10370-024)

Supplier: Bioss

Description: Recruited by REST to neuronal genes that contain RE-1 elements, leading to neuronal gene silencing in non-neuronal cells (By similarity). Preferentially catalyzes the dephosphorylation of 'Ser-5' within the tandem 7 residue repeats in the C-terminal domain (CTD) of the largest RNA polymerase II subunit POLR2A. Negatively regulates RNA polymerase II transcription, possibly by controlling the transition from initiation/capping to processive transcript elongation.

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