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Human Rna Binding

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Ribosomal protein L26 (RPL26) is a component of the 60S ribosomal subunit and is involved in translation (1,2). It was shown that RPL26 increases the translation of p53 mRNA by binding to its 5' untranslated region (UTR) after DNA damage. Studies found that overexpression of RPL26 enhances the binding of p53 mRNA to the ribosomes and increases p53 translation. Overexpression of RPL26 also induces cell-cycle arrest at G1 phase and increases radiation-stimulated apoptosis (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Ribosomal protein L26 (RPL26) is a component of the 60S ribosomal subunit and is involved in translation (1,2). It was shown that RPL26 increases the translation of p53 mRNA by binding to its 5' untranslated region (UTR) after DNA damage. Studies found that overexpression of RPL26 enhances the binding of p53 mRNA to the ribosomes and increases p53 translation. Overexpression of RPL26 also induces cell-cycle arrest at G1 phase and increases radiation-stimulated apoptosis (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Ribosomal protein L7a is a highly conserved ribosome protein localized to 60S ribosomal subunit (1). The protein has distinct domains that target the newly synthesized polypeptide to nucleus and the nucleoli, the site of ribosome biosynthesis (2). Ribosomal protein L7a can also interact with RNA in vitro through two distinct RNA-binding domains in the protein (3). Taken together, nucleolar localization and the ability to bind RNA suggests that ribosomal protein L7a may act as an important component for ribosome biosynthesis and function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Upf1 was identified as an active component in nonsense-mediated decay (NMD), an mRNA surveillance mechanism in eukaryotic cells that degrades mRNAs containing premature termination codons (1). Upf1 was found to be an ATP-dependent RNA helicase in the cytoplasm (2) and was later shown to be a component of cytoplasmic P-bodies (3). Upf1 phosphorylation mediates the repression of translation that accompanies NMD, allowing mRNA accessibility to the NMD machinery (4). Two other active components of NMD, Upf2 and Upf3, were also identified and described as having perinuclear and nucleocytoplasmic localization, respectively (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fibrillarin is a 2'-O-methyltransferase located in fibrillar regions and Cajal bodies of the nucleolus, where RNA transcription and pre-RNA processing take place (1,2). Fibrillarin associates with several other structural proteins as well as box C/D snoRNA to form a complex that functions in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly. This complex catalyzes site-specific 2'-O-ribose methylation of targeted nucleotides within the rRNA sequence (3,4). The sequence, structure, and function of fibrillarin are highly conserved and fibrillarin gene expression is essential for early embryonic development (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: H box/ACA-motif small nucleolar RNAs (snoRNAs) guide snoRNA proteins (snoRNPs) to uridine residues on rRNA for the conversion to pseudouridine (1). These H/ACA snoRNPs consist of four highly conserved proteins including GAR1, NHP2, NOP10, and the catalytic component dyskerin (1-3). The core snoRNPs also bind to mammalian telomerase RNA, which contains a H/ACA-like motif in the 3’ domain. This binding results in the maintenance of telomerase levels and activity (4). Defects in the snoRNPs can lead to dyskeratosis congenita, a rare, x-linked disorder characterized by a failure of the bone marrow and an increased tumor risk (5,6). Mutations in the dyskerin gene can cause defects in translation of mRNAs containing internal ribosome entry sites (IRESs), which include mRNAs to tumor suppressors p27 and p53 and anti-apoptotic factors Bcl-xL and XIAP (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: CNPase (2', 3’-cyclic nucleotide 3'-phosphodiesterase) catalyzes the in vitro hydrolysis of 2’, 3’-cyclic nucleotides to produce 2’-nucleotides. The in vivo molecular function and native substrate of this nucleotide phosphodiesterase remains under investigation (1). High CNPase expression is seen in oligodendrocytes and Schwann cells as CNPase accounts for roughly 4% of the total myelin protein in the central nervous system (2). CNPase binds to tubulin heterodimers and plays a role in tubulin polymerization, and oligodendrocyte process outgrowth (3). Typical myelination is seen in CNPase knock-out mice, but they suffer severe neurodegeneration from axonal loss and oligodendrocytes display abnormal paranodal loop structure prior to axonal degeneration. Paranodal loops typically contact the axolemma in axon-glial signaling; neurodegeneration in CNPase knock-out mice is a secondary consequence of impaired cell-cell communication (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: CNPase (2', 3’-cyclic nucleotide 3'-phosphodiesterase) catalyzes the in vitro hydrolysis of 2’, 3’-cyclic nucleotides to produce 2’-nucleotides. The in vivo molecular function and native substrate of this nucleotide phosphodiesterase remains under investigation (1). High CNPase expression is seen in oligodendrocytes and Schwann cells as CNPase accounts for roughly 4% of the total myelin protein in the central nervous system (2). CNPase binds to tubulin heterodimers and plays a role in tubulin polymerization, and oligodendrocyte process outgrowth (3). Typical myelination is seen in CNPase knock-out mice, but they suffer severe neurodegeneration from axonal loss and oligodendrocytes display abnormal paranodal loop structure prior to axonal degeneration. Paranodal loops typically contact the axolemma in axon-glial signaling; neurodegeneration in CNPase knock-out mice is a secondary consequence of impaired cell-cell communication (4).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: PDCD4 (programmed cell death protein 4) was identified as a suppressor of neoplastic transformation (1). It interacts with eukaryotic initiation factors eIF4AI and eIF4AII (2). PDCD4 colocalizes with eIF4A in the cytoplasm and inhibits the activity of eIF4A as an ATP-dependent RNA helicase (2). PDCD4 inhibits cap-dependent translation (2). Upon stimulation by mitogens, PDCD4 is phosphorylated on Ser67 by S6K1 kinase and then degraded through the ubiquitin pathway leading to enhanced translation and cell growth (3).

$260
100 µl
This Cell Signaling Technology antibody is immobilized by the covalent reaction of formylbenzamide-modified antibody with hydrazide-activated magnetic bead.PKR (D7F7) Rabbit mAb (Magnetic Bead Conjugate) is useful for immunoprecipitation assays of PKR protein.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein L (hnRNP L) belongs to a family of RNA binding multiprotein complexes (hnRNP proteins) that facilitate pre-mRNA processing and transport of mRNA from the nucleus to cytoplasm (1-3). hnRNP L binds to CA repeat elements to regulate splicing and RNA stability (4-6). Binding of hnRNP L has been shown to occur in response to stress stimuli to regulate conformational change and subsequent translation of mRNAs (7). hnRNPL can promote apoptosis by enhancing translation of p53 mRNA (8) . In the context of tumor progression, hnRNPL has been shown to bind and modify translation of critical regulators of cell cycle and apoptosis (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades poly-ubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Enhancer of mRNA decapping 3 (EDC3) was originally identified from Saccharomyces cerevisiae as a protein essential to mRNA decapping prior to 5’-3’ mRNA degradation (1). In human cells, EDC3 is found within cytoplasmic processing (P) bodies as part of complexes that include DCP1, DCP2, EDC4/Ge-1, and DDX6/RCK (2). EDC3 and DCP2 interact with TTP, an activator of AU-rich-element (ARE)-mediated decay pathway, to promote decapping and degradation of ARE mRNA (2). In addition, research studies indicate that EDC3 may play a role in the premature termination of RNA polymerase II transcription (3).