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Human Nuclear Mrna Splicing

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

Application Methods: Western Blotting

Background: SF2/ASF is a member of the Ser-Arg-rich (SR) protein family of highly conserved nuclear phosphoproteins involved in pre-mRNA splicing (1). Besides its role in nuclear pre-mRNA splicing, SF2/ASF has been shown to shuttle between the nucleus and cytoplasm, suggesting additional roles in mRNA transport and cytoplasmic events (2). SF2/ASF associates with translating ribosomes and stimulates translation (3). It also activates translation initiation by suppressing the activity of 4E-BP1, which is mediated by SF2/ASF association with mTOR and the phosphatase PP2A (4). More recent studies have demonstrated a role for SF2/ASF in microRNA processing (5).

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

Application Methods: Western Blotting

Background: SF2/ASF is a member of the Ser-Arg-rich (SR) protein family of highly conserved nuclear phosphoproteins involved in pre-mRNA splicing (1). Besides its role in nuclear pre-mRNA splicing, SF2/ASF has been shown to shuttle between the nucleus and cytoplasm, suggesting additional roles in mRNA transport and cytoplasmic events (2). SF2/ASF associates with translating ribosomes and stimulates translation (3). It also activates translation initiation by suppressing the activity of 4E-BP1, which is mediated by SF2/ASF association with mTOR and the phosphatase PP2A (4). More recent studies have demonstrated a role for SF2/ASF in microRNA processing (5).

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

Application Methods: Western Blotting

Background: Splicing factor 3b subunit 1 (SF3B1) is an integral component of the U2 small nuclear ribonucleoprotein (U2 snRNP) and plays an important role in the splicing of pre-mRNA that involves the removal of introns and the joining of exons to form mature mRNA (1-3). The assembly and proper recognition of splice sites are driven by sequences at the pre-mRNA intron-exon splice sites. The 5’ splice donor site is recognized by the U1 snRNP complex, while U2 snRNP binds to the 3’ splice site (branch point), ensuring the anchoring of the spliceosome machinery at the splice sites (3,4). Recent whole exome sequencing studies have demonstrated a high incidence of somatic mutations of SF3B1 in patients with various hematological malignancies such as chronic lymphocytic leukemia and myelodysplastic syndromes (2,3,5,6). Misregulation of pre-mRNA splicing arising from mutations of the spliceosome components such as SF3B1 is thought to contribute to changes in the expression patterns of key proteins that are involved in pathways such as cell cycle progression, cell death, and cancer metabolism (2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Splicing factor 3b subunit 1 (SF3B1) is an integral component of the U2 small nuclear ribonucleoprotein (U2 snRNP) and plays an important role in the splicing of pre-mRNA that involves the removal of introns and the joining of exons to form mature mRNA (1-3). The assembly and proper recognition of splice sites are driven by sequences at the pre-mRNA intron-exon splice sites. The 5’ splice donor site is recognized by the U1 snRNP complex, while U2 snRNP binds to the 3’ splice site (branch point), ensuring the anchoring of the spliceosome machinery at the splice sites (3,4). Recent whole exome sequencing studies have demonstrated a high incidence of somatic mutations of SF3B1 in patients with various hematological malignancies such as chronic lymphocytic leukemia and myelodysplastic syndromes (2,3,5,6). Misregulation of pre-mRNA splicing arising from mutations of the spliceosome components such as SF3B1 is thought to contribute to changes in the expression patterns of key proteins that are involved in pathways such as cell cycle progression, cell death, and cancer metabolism (2,3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The X-linked RNA binding motif protein (RBMX, hnRNP G) is a multi-functional protein that is part of a heterogeneous nuclear ribonucleoprotein complex (1,2). This widely expressed protein is involved in the control of pre-mRNA splicing as part of the spliceosome. RBMX is important for the alternative splicing of many pre-mRNAs, including those that encode for dystrophin, tropomyosin, and survival motor neuron protein (SMN) in skeletal muscle and cardiac muscle (3,4). The RBMX protein is essential for the maintenance of proper sister chromatid cohesion prior to sister chromosome segregation during mitosis (5). Research studies show that RBMX accumulates at sites of DNA damage and that the presence of RBMX is required for homologous recombination repair (6).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: PTBP1 and PTBP2 are highly related pre-mRNA binding proteins that silence the splicing of alternative exons (1,2 ). While PTBP1 is widely expressed, PTBP2, also known as neural PTB or nPTB, is expressed in post-mitotic neurons. In other cell types, PTBP2 transcripts are alternatively spliced by PTBP1, which leads to nonsense-mediated decay (3). PTBP1 and 2 bind to similar regions across the transcriptome, but PTBP1 has a stronger repressive property likely due to cofactors such as Raver1 and Matrin3 (4-6). Overexpression of PTBPs in various cancers has been observed, leading to alternative splicing of key proteins in oncogenic pathways (6-9).

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

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

Background: PTBP1 and PTBP2 are highly related pre-mRNA binding proteins that silence the splicing of alternative exons (1,2 ). While PTBP1 is widely expressed, PTBP2, also known as neural PTB or nPTB, is expressed in post-mitotic neurons. In other cell types, PTBP2 transcripts are alternatively spliced by PTBP1, which leads to nonsense-mediated decay (3). PTBP1 and 2 bind to similar regions across the transcriptome, but PTBP1 has a stronger repressive property likely due to cofactors such as Raver1 and Matrin3 (4-6). Overexpression of PTBPs in various cancers has been observed, leading to alternative splicing of key proteins in oncogenic pathways (6-9).

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

Application Methods: Western Blotting

Background: U2 small nuclear RNA auxiliary factor 1 (U2AF1) is the small (35 kDa) subunit of the U2 auxiliary factor (U2AF) that plays an essential role in the splicing of pre-mRNA to generate functional mRNA transcripts. U2AF1 forms a heterodimer with the large (65 kDa) U2AF2 subunit to create the U2 auxiliary factor that recognizes the 3' splice site and facilitates spliceosome assembly (1-3). Research studies indicate that U2AF1 binds to the 3'-splice site consensus AG dinucleotide at the intron-exon boundary while U2AF2 recognizes and binds the polyprimidine tract upstream of the 3’ splice site. These two steps ensure accurate spliceosome assembly at splice sites (4-6). Mutations in the corresponding U2AF1 gene are associated with a type of hematopoietic stem cell disorder known as myelodysplastic syndrome (MDS), which can be characterized by low blood counts, anemia, and enhanced acute myeloid leukemia risk (7-9). Somatic U2AF1 mutations frequently affect highly conserved zinc finger protein regions that result in defective pre-mRNA splicing of genes involved in cell cycle progression and RNA processing pathways, contributing to MDS pathogenesis (7,10).

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

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

Background: 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 (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). 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 (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein Q and R belong to a family of hnRNP proteins that are involved in RNA binding, RNA biosynthesis, and mRNA transport from the nucleus to the cytoplasm (1-3). These two proteins are encoded by different genes but have 83% homology. hnRNP Q has three alternative splice variants (hnRNP Q1-3) (1-3). Methylation of carboxy-terminal arginine residues is required for nuclear localization (4). hnRNP Q binds to AU-rich mRNA in conjunction with AUF1 and regulates mRNA decay (5). hnRNP Q isoforms play a crucial role in mediating nuclear function of survival of motor neuron (SMN) complex (6,7) and modulating RNA biosynthesis and hepatitis C virus replication (8). hnRNP R was identified recently and its function is still under investigation (9), however hnRNP R does not duplicate the biological function of hnRNP Q. Both hnRNP Q and R are present in cytoplasmic mRNP granules containing untranslated mRNAs (10) and both interact with SMN (11).

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

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

Background: 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 (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). 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 (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

$262
3 nmol
300 µl
SignalSilence® hnRNP A1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit hnRNP A1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: 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 (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). 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 (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

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

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: 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 (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). 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 (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein Q and R belong to a family of hnRNP proteins that are involved in RNA binding, RNA biosynthesis, and mRNA transport from the nucleus to the cytoplasm (1-3). These two proteins are encoded by different genes but have 83% homology. hnRNP Q has three alternative splice variants (hnRNP Q1-3) (1-3). Methylation of carboxy-terminal arginine residues is required for nuclear localization (4). hnRNP Q binds to AU-rich mRNA in conjunction with AUF1 and regulates mRNA decay (5). hnRNP Q isoforms play a crucial role in mediating nuclear function of survival of motor neuron (SMN) complex (6,7) and modulating RNA biosynthesis and hepatitis C virus replication (8). hnRNP R was identified recently and its function is still under investigation (9), however hnRNP R does not duplicate the biological function of hnRNP Q. Both hnRNP Q and R are present in cytoplasmic mRNP granules containing untranslated mRNAs (10) and both interact with SMN (11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear cap-binding protein subunit 1 (NCBP1), also known as cap-binding protein 80 (CBP80), plays a role in nuclear pre-mRNA splicing (1,2). It has also been shown to function in the nonsense-mediated decay (NMD) of mRNAs where translation is prematurely terminated (3). NCBP1/CBP80 increases the efficiency of NMD by promoting the interaction of two active NMD components Upf1 and Upf2 (4).

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

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).

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

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).

$270
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein A2/B1 (hnRNP A2/B1) 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 (1). Alternative splicing produces transcripts that encode two homologous hnRNP proteins, hnRNPA2 and hnRNPB1, from a single gene sequence (2). Studies demonstrate hnRNP A2/B1 splicing repression across multiple targets (3,4) and that both proteins can bind and protect telomere repeat sequences from DNase digestion (5,6). Altered expression of hnRNP B1 is seen in several forms of cancer, including squamous cell carcinoma, adenocarcinoma, and various forms of lung cancer (7). Over expression of hnRNP B1 may be associated with inhibition of DNA-PK activity and impaired DNA repair during early stages of cancer development (8). Autoantigens to hnRNP A2/B1 (termed RA33) are associated with rheumatoid arthritis, systemic lupus erythromatosus and mixed connective tissue disease (9-11).

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

Application Methods: Immunoprecipitation, 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

Application Methods: Immunoprecipitation, 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).