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Product listing: eIF4A (C32B4) Rabbit mAb, UniProt ID P38919 #2013 to LARP1 (D8J4F) Rabbit mAb, UniProt ID Q6PKG0 #70180

$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

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

Background: Eukaryotic initiation factor 4B (eIF4B) is thought to assist the eIF4F complex in translation initiation. In plants, eIF4B is known to interact with the poly-(A) binding protein, increasing its poly-(A) binding activity (1). Heat shock and serum starvation cause dephosphorylation of eIF4B at multiple sites with kinetics similar to those of the corresponding inhibition of translation, while phosphorylation of eIF4B following insulin treatment correlates well with an observed increase in translation (2-5). Multiple kinases, including p70 S6 kinase, can phosphorylate eIF4B in vitro, and at least one serum-inducible eIF4B phosphorylation site is sensitive to rapamycin and LY294002 (6). Recently, Ser406 was identified as a novel phosphorylation site regulated by mitogens (7), and the phosphorylation of this site is dependent on MEK and mTOR activity (7). This phosphorylation is shown to be essential for the translational activity of eIF4B (7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated eIF4E (C46H6) Rabbit mAb #2067.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

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

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

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

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

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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

Application Methods: Western Blotting

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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

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

Background: A variety of factors contribute to the initiation of translation. Eukaryotic translation initiation factor 4H (eIF4H) was purified to near homogeneity from rabbit reticulocyte lysate and shown to stimulate translation in an assay deficient in eIF4F and eIF4B (1). eIF4H induces the RNA-dependent ATP hydrolysis catalyzed by the initiation factors eIF4A and eIF4B (1,2). eIF4H was further shown to stimulate the initial rate and extent of eIF4A-mediated mRNA secondary structure unwinding (3). Interaction between eIF4H and the herpes simplex virus shutoff protein (Vhs) appears to be important for Vhs-mediated degradation of mRNA (4). Deletion of a large region of chromosome 7, including the corresponding eIF4H gene, results in Williams-Beuren Syndrome (WBS), an autosomal dominant disorder that can present with cardiovascular problems, mental retardation and distinctive facial features (5).

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

Application Methods: Western Blotting

Background: Eukaryotic translation initiation factor 5 (eIF5) is crucial for the assembly of translation initiation complex and plays an important role in protein synthesis (1). eIF5 interacts with the 43S initiation complex to stimulate hydrolysis of GTP bound to eIF2 (1-3). Studies suggest that eIF5 functions as the GTPase-activating protein (GAP) in the hydrolysis of GTP-bound eIF2 (4,5). This hydrolysis leads to the release of initiation factors from the 40S ribosomal subunit, which is a necessary step in the formation of the 80S initiation complex (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 5A (eIF5A) is an mRNA-binding protein that is involved in translation elongation and plays an important role in promoting translation of polyproline motifs (1-4). The eIF5A (eIF5A1) and eIF5A2 genes encode the two vertebrate eIF5A isoforms. While eIF5A1 is expressed constitutively in all tissues, eIF5A2 is mainly expressed in gonads. eIF5A and eIF5A2 are the only identified proteins that contain the distinctive amino acid hypusine, which is generated posttranslationally from lysine through a highly conserved polyamine metabolism pathway. eIF5A function and hypusine modification are both essential for cell proliferation, as knock down of eIF5A expression or blocking eIF5A hypusine modification suppresses cancer cell proliferation (5-7). Interestingly, eIF5A is an identified component of a tumor suppressor network of the polyamine-hypusine axis. Co-suppression of both eIF5A and adenosylmethionine decarboxylase 1 (AMD1) promotes lymphomagenesis in mice, while heterozygous deletions of the corresponding AMD1 and eIF5A genes often occur together in human lymphomas (8).

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

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

Background: Eukaryotic initiation factor 6 (eIF6) is reqiured for the 60S ribosomal subunit assembly in the nucleolus (1). In the cytoplasm, this protein is bound to 60S ribosome subunits and prevents them from joining 40S ribosome subunits to form 80S ribosomes (2). eIF6 is also shown to associate with the RNA-induced silencing complex (RISC) (3). Deletion of eIF6 abolishes the miRNA-mediated gene silencing (3). eIF6 may play its essential role in miRNA-mediated silencing by inhibiting translation initiation or ribosome recycling (3).

$305
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated ELAVL1/HuR (D9W7E) Rabbit mAb #12582.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The ELAVL (embryonic lethal, abnormal vision and Drosophila-like) family of proteins includes ELAVL1/HuR, ELAVL2/HuB, ELAVL3/HuC and ELAVL4/HuD (1). ELAVL1/HuR is ubiquitously expressed whereas expression of the other three members is neuronal-specific (1). ELAVL/Hu proteins are highly conserved RNA-binding proteins (1). Besides three RNA recognition motifs, these proteins also contain nuclear localization signals that enable them to shuttle between nucleus and cytoplasm (2). Upon inhibition of transcription by actinomycin D, ELAVL1/HuR relocates from nucleus to cytoplasm where it binds the AU-rich elements within 3' UTRs to stabilize mRNAs (3, 4). ELAVL1/HuR is suggested to increase translation by binding to mRNAs (5,6). In addition, ELAVL1/HuR interacts with microRNAs (miRNAs) (7).

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

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

Background: The ELAVL (embryonic lethal, abnormal vision and Drosophila-like) family of proteins includes ELAVL1/HuR, ELAVL2/HuB, ELAVL3/HuC and ELAVL4/HuD (1). ELAVL1/HuR is ubiquitously expressed whereas expression of the other three members is neuronal-specific (1). ELAVL/Hu proteins are highly conserved RNA-binding proteins (1). Besides three RNA recognition motifs, these proteins also contain nuclear localization signals that enable them to shuttle between nucleus and cytoplasm (2). Upon inhibition of transcription by actinomycin D, ELAVL1/HuR relocates from nucleus to cytoplasm where it binds the AU-rich elements within 3' UTRs to stabilize mRNAs (3, 4). ELAVL1/HuR is suggested to increase translation by binding to mRNAs (5,6). In addition, ELAVL1/HuR interacts with microRNAs (miRNAs) (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Import and export through the nuclear envelope (NE) via facilitated translocation is important for many cellular processes including protein synthesis and miRNA biogenesis (1). Exportin 5 (XPO5) is a member of the importin β family of proteins (2) and functions in tRNA export in a sequence dependent fashion. More recently, it has been shown to export pre-miRNA by a RanGTPase-driven process from the nucleus to the cytoplasm, where pre-miRNA processing occurs to produce mature miRNAs (1,3). Study of the miRNA biosynthesis pathway is essential toward understanding the process of oncogenesis as global downregulation of miRNAs and the resulting alterations in expression of tumor suppressor and oncogenic proteins is a common phenotype of cancers cells (3,4). Research studies have shown that disruption of exportin 5 functions in many types of cancers including breast and lung, where pre-miRNA accumulates in the nucleus and miRNA maturation is impaired (2,3).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fragile X syndrome, a frequent cause of inherited mental retardation, often results from expansion of the CGG trinucleotide repeat in the gene that encodes the fragile X mental retardation protein (FMRP) (1). FMRP (also known as FMR1) and its two autosomal homologs (FXR1 and FXR2) all bind RNA and play a role in the pathogenesis of fragile X syndrome (1-3). Each of these related proteins can associate with one another as well as form homodimers (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). In Drosophila, dFMRP associates with Argonaute 2 (Ago2) and Dicer and coimmunoprecipitates with miRNA and siRNA. These results suggest that fragile X syndrome is related to abnormal translation caused by a defect in RNAi-related pathways (5). In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fragile X syndrome is a genetic disorder characterized by a spectrum of physical and behavioral features and is a frequent form of inherited mental retardation (1). X-linked FMRP (FMR-1) and its two autosomal homologs, FXR1 and FXR2, are polyribosome-associated RNA-binding proteins that are involved in the pathogenesis of fragile X syndrome (1-3). Each of the fragile X proteins can self-associate, as well as form heteromers with the other two related proteins (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). The Drosophila homolog of FMRP (dFMRP) associates with Argonaute 2 (Ago2) and Dicer and can coimmunoprecipitate with miRNA and siRNA (5). These results suggest that fragile X syndrome is related to abnormal translation caused by defects in RNAi-related pathways. In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fragile X syndrome is a genetic disorder characterized by a spectrum of physical and behavioral features and is a frequent form of inherited mental retardation (1). X-linked FMRP (FMR-1) and its two autosomal homologs, FXR1 and FXR2, are polyribosome-associated RNA-binding proteins that are involved in the pathogenesis of fragile X syndrome (1-3). Each of the fragile X proteins can self-associate, as well as form heteromers with the other two related proteins (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). The Drosophila homolog of FMRP (dFMRP) associates with Argonaute 2 (Ago2) and Dicer and can coimmunoprecipitate with miRNA and siRNA (5). These results suggest that fragile X syndrome is related to abnormal translation caused by defects in RNAi-related pathways. In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) 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). The A/B subfamily of hnRNP includes A1, A2/B1, A3, and A0. hnRNP A0 is phosphorylated at Ser84 by MAPKAPK-2 in response to LPS treatment in mouse macrophage cells, which might play a key role in stimulating translation of the TNF-α message (2).

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

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

Background: Heterogeneous nuclear ribonucleoprotein A0 (hnRNP A0) 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). The A/B subfamily of hnRNP includes A1, A2/B1, A3, and A0. hnRNP A0 is phosphorylated at Ser84 by MAPKAPK-2 in response to LPS treatment in mouse macrophage cells, which might play a key role in stimulating translation of the TNF-α message (2).

$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

Application Methods: Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein C1/C2 (hnRNP C1/C2) has multiple biological functions including transcriptional regulation, DNA repair, and RNA processing. hnRNP C1/C2 acts as a ‘molecular ruler’ in the mRNA processing pathway, committing nascent transcripts from the chromatin template to the mRNA export pathway once the nascent transcript becomes longer than 200-300 nucleotides (1). hnRNP C1/C2 associates with SWI/SNF and NurD family members to form the locus control region (LCR)-associated remodeling complex (LARC), which binds to β-globin gene promoter to prevent transcriptional silencing. Studies indicate that without hnRNP C1/C2, LARC does not associate with its target DNA sequence (2,3). hnRNP C1/C2 and other hnRNP family members interact with DNA damage response (DDR) proteins (4). hnRNP proteins regulate double stranded break (DSB) repair by promoting either homologous recombination (HR) or non-homologous end joining (NHEJ) (4). hnRNP C1/C2 downregulates the expression of miR-21, which leads to the increased expression of programmed cell death 4 (PDCD4) protein in glioblastoma multiforme (GBM) (5). Research studies have shown that silencing of hnRNP C1/C2 renders GBM cells more susceptible to apoptosis (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein K (hnRNP K) 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 K contains three unique structural motifs termed KH domains that bind poly(C) DNA and RNA sequences (4,5). Intricate architecture enables hnRNP K to facilitate mRNA biosynthesis (6), transcriptional regulation (7), and signal transduction. Research studies have shown that cytoplasmic hnRNP K expression is increased in oral squamous cell carcinoma and pancreatic cancer, and may be a potential prognostic factor (8,9). hnRNP K coordinates with p53 to regulate its target gene transcription in response to DNA damage. Proteasome degradation of hnRNP K is mediated by E3 ligase MDM2 (10). The interaction between hnRNP K and c-Src leads to hnRNP K phosphorylation, which allows for hnRNP K activation of silenced mRNA translation (11).

$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, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin-like growth factor-II mRNA-binding proteins (IMPs) belong to a family of zipcode-binding proteins (1,2). Three members of this family, IMP1, IMP2, and IMP3, have been identified (1,2). They contain two RNA recognition motifs, four K homology domains, and were found to function in mRNA localization, turnover, and translation control (1,2). Research studies have implicated these proteins in a variety of physiological and pathological processes, such as growth and development (3), testicular neoplasia (4), and melanocytic neoplasia (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Insulin-like growth factor-II mRNA-binding proteins (IMPs) belong to a family of zipcode-binding proteins (1,2). Three members of this family, IMP1, IMP2, and IMP3, have been identified (1,2). They contain two RNA recognition motifs, four K homology domains, and were found to function in mRNA localization, turnover, and translation control (1,2). Research studies have implicated these proteins in a variety of physiological and pathological processes, such as growth and development (3), testicular neoplasia (4), and melanocytic neoplasia (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: KHSRP, also known as KSRP, is a KH domain-containing AU-rich element (ARE) binding protein (1). It recruits degradation machinery and activates mRNA turnover (2). This protein was previously shown to function as a regulator for splicing (3). KHSRP associates with both the Drosha and Dicer multiprotein complexes (4), and controls the biogenesis of some microRNAs by binding to the terminal loops of these microRNA precursors (3). KHSRP is found in neural and non-neural cell types in both the nucleus and the cytoplasm (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: La antigen is recognized by antibodies in patients with autoimmune disorders such as systemic lupus erythematosus and Sjögren's syndrome (1). La antigen binds to the 5'-noncoding region of poliovirus RNA and is an IRES trans-acting factor (1,2). Depletion of La antigen reduces the function of poliovirus IRES in vivo (3). La antigen, when phosphorylated at Ser366, has been shown to associate with nuclear precursor tRNAs and facilitate their processing (4). The nonphosphorylated La antigen interacts with the mRNAs that have 5'-terminal oligopyrimidine (5'TOP) motifs to control protein synthesis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: La-related protein 1 (LARP1) is a ubiquitously expressed RNA binding protein that promotes both global and specific mRNA translation in cells (1). LARP1 belongs to the La-related protein family and contains two RNA binding domains, a La motif (LAM), and a neighboring RNA recognition motif-like (RRM-L) domain (1). Research studies indicate that LARP1 acts downstream of mTORC1 to facilitate cell proliferation and growth by promoting global mRNA translation and translation of mRNAs containing a 5'Terminal Oligo-Pyrimidine (5'TOP) motif, which code for translational machinery components (2,3). At the molecular level, LARP1 associates with 5'TOP mRNAs and multiple translation machinery components to positively regulate translation (2,4). Additional studies show that LARP1 expression is upregulated in hepatocellular carcinoma (HCC) patients and that high LARP1 expression in HCC negatively correlates with survival rate (5).