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Product listing: RPL5 (D5Q5X) Rabbit mAb, UniProt ID P46777 #51345 to XBP-1s (E7M5C) Mouse mAb, UniProt ID P17861-2 #47134

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Ribosomal protein L5 (RPL5) is one of several proteins that comprise the 60S ribosomal subunit. RPL5 binds 5S rRNA and the nucleolar RPL11 protein to form the 5S ribonucleoprotein particle (RNP) that is incorporated into the large 60S ribosomal subunit (1). An RP-MDM2-p53 protein complex that contains ribosomal proteins RPL5, RPL11, and RPL23 acts as a nucleolar stress sensor that binds and inhibits MDM2 ubiquitin ligase activity and enhances p53-mediated transcriptional activity (2,3). RPL5 cooperates with RPL11 to influence ribosome biogenesis through regulating expression of the transcription factor c-Myc, which acts as the master regulator of ribosome biogenesis (4). Mutations in the corresponding RPL5 gene are associated with Diamond-Blackfan anemia, which is a form of red blood cell aplasia, and some cases of pediatric T-cell acute lymphoblastic leukemia (5,6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

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

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$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 S6 Ribosomal Protein (5G10) Rabbit mAb #2217.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (5G10) Rabbit mAb #2217.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$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: 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).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: p70 S6 kinase is a mitogen activated Ser/Thr protein kinase downstream of phosphoinositide-3 kinase (PI3K) and the target of rapamycin, FRAP/mTOR. p70 S6 kinase is required for cell growth and cell cycle progression (1,2). SKAR is a recently discovered substrate of S6K1. SKAR exists in two isoforms, α and β, the latter having a 29 amino acid truncation. Phosphorylation of SKAR is mitogen-induced and sensitive to rapamycin. Reduction in SKAR protein levels results in decreased cell size, further implicating SKAR in cell growth control (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Survival of Motor Neuron 1 (SMN1) is essential for the maturation of small nuclear ribonucleoproteins (snRNPs) (1,2). SMN1 plays a role in the assembly of spliceosomal snRNPs in the cytoplasm, together with the Gemin proteins, and may also participate in the transport of snRNPs into the nucleus (3-6). SMN1 also participates in the maturation and turnover of snRNPs in nuclear foci Gemini bodies (gems) (7). In addition to the maturation of spliceosomal snRNPs, SMN1 has also been proposed to directly regulate pre-mRNA splicing (8). Researchers have found mutations and deletions of the SMN1 gene are found in 95% of Spinal Muscular Atrophy (SMA) neuromuscular disorder cases (1,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Symplekin is necessary for 3’-end cleavage and polyadenylation of mRNAs, histone 3’-end processing and polyadenylation in the cytoplasm (1-5). It is thought to act as a scaffolding protein that brings together factors involved in mRNA 3’-end processing (1,2). Symplekin also plays a role in transcription initiation and termination by RNA polymerase II (RNAPII) through bridging the interaction between the polyadenylation machinery and RNAPII (3,6,7). In addition to its role in mRNA 3’-end processing, research studies have shown that symplekin localizes at epithelial cell tight junctions where it may help to regulate tight junction assembly, thereby maintaining the integrity of the epithelial monolayer and cell polarity (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Transcription factor 11 (TCF11) is a basic leucine zipper transcription factor. It is also referred to as Nuclear factor E2-related factor 1 (NRF1). TCF11 was initially reported to activate erythroid-specific, human globin gene expression (1). It plays an essential role during embryonic development (2). It also associates with other transcription factors, such as Jun proteins, to transcriptionally control antioxidant response element (ARE)-mediated expression in response to antioxidants and xenobiotics (3-5). TCF11 has been shown to regulate proteasomal degradation and mediate the proteasome recovery pathway after proteasome inhibition (6,7). TCF11 is ubiquitously expressed (8) and several isoforms have been reported. The 120 kDa form exists in the endoplasmic reticulum (ER) membrane under normal conditions. Upon proteasome inhibition, TCF11 translocates to the nucleus (9). The 65 kDa N-terminal-truncated form is constitutively localized to the nucleus (10,11). TCF11 protein levels are regulated by ubiquitination and proteasomal-mediated degradation (12); proteasome inhibitors stabilize TCF11.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Transcription factor EB (TFEB) is a member of the Myc-related, bHLH leucine-zipper family of transcription factors that drives the expression of a network of genes known as the Coordinated Lysosomal Expression and Regulation (CLEAR) network (1,2). TFEB specifically recognizes and binds regulatory sequences within the CLEAR box (GTCACGTGAC) of lysosomal and autophagy genes, resulting in the up-regulated expression of genes involved in lysosome biogenesis and function, and regulation of autophagy (1,2). TFEB is activated in response to nutrient deprivation, stimulating translocation to the nucleus where it forms homo- or heterooligomers with other members of the microphthalmia transcription factor (MiTF) subfamily and resulting in up-regulation of autophagosomes and lysosomes (3-5). Recently, it has been shown that TFEB is a component of mammalian target of rapamycin (mTOR) complex 1 (mTORC1), which regulates the phosphorylation and nuclear translocation of TFEB in response to cellular starvation and stress (6-9). During normal growth conditions, TFEB is phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation promotes association of TFEB with 14-3-3 family proteins and retention in the cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it increases transcription of CLEAR and autophagy genes (10). TFEB has also been shown to be activated in a nutrient-dependent manner by p42 MAP kinase (Erk2). TFEB is phosphorylated at Ser142 by Erk2 in response to nutrient deprivation, resulting in nuclear localization and activation, and indicating that pathways other than mTOR contribute to nutrient sensing via TFEB (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factor EB (TFEB) is a member of the Myc-related, bHLH leucine-zipper family of transcription factors that drives the expression of a network of genes known as the Coordinated Lysosomal Expression and Regulation (CLEAR) network (1,2). TFEB specifically recognizes and binds regulatory sequences within the CLEAR box (GTCACGTGAC) of lysosomal and autophagy genes, resulting in the up-regulated expression of genes involved in lysosome biogenesis and function, and regulation of autophagy (1,2). TFEB is activated in response to nutrient deprivation, stimulating translocation to the nucleus where it forms homo- or heterooligomers with other members of the microphthalmia transcription factor (MiTF) subfamily and resulting in up-regulation of autophagosomes and lysosomes (3-5). Recently, it has been shown that TFEB is a component of mammalian target of rapamycin (mTOR) complex 1 (mTORC1), which regulates the phosphorylation and nuclear translocation of TFEB in response to cellular starvation and stress (6-9). During normal growth conditions, TFEB is phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation promotes association of TFEB with 14-3-3 family proteins and retention in the cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it increases transcription of CLEAR and autophagy genes (10). TFEB has also been shown to be activated in a nutrient-dependent manner by p42 MAP kinase (Erk2). TFEB is phosphorylated at Ser142 by Erk2 in response to nutrient deprivation, resulting in nuclear localization and activation, and indicating that pathways other than mTOR contribute to nutrient sensing via TFEB (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: THEX1 (3’hExo) is a 3’ exonuclease that may play a role in the degradation of histone mRNA transcripts (1). A recently identified member of the DEDDh 3' exonuclease family, THEX1 binds the conserved stem-loop structure found at the 3’ end of mRNA in vitro (2). The binding of THEX1 to mRNA requires the presence of a terminal ACCCA sequence and is enhanced by the concurrent binding of stem-loop binding protein (SLBP). Cleavage of histone mRNA by THEX1 exonuclease may help produce the rapid turnover of histone mRNA transcripts associated with the completion of DNA replication (3). Additional evidence suggests that THEX1 may be responsible for excising the remaining few 3’ nucleotides following cleavage by a different enzyme (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: THEX1 (3’hExo) is a 3’ exonuclease that may play a role in the degradation of histone mRNA transcripts (1). A recently identified member of the DEDDh 3' exonuclease family, THEX1 binds the conserved stem-loop structure found at the 3’ end of mRNA in vitro (2). The binding of THEX1 to mRNA requires the presence of a terminal ACCCA sequence and is enhanced by the concurrent binding of stem-loop binding protein (SLBP). Cleavage of histone mRNA by THEX1 exonuclease may help produce the rapid turnover of histone mRNA transcripts associated with the completion of DNA replication (3). Additional evidence suggests that THEX1 may be responsible for excising the remaining few 3’ nucleotides following cleavage by a different enzyme (4).

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

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

Background: mRNA export is a process that is tightly coupled to mRNA splicing (1-4). Splicing and packaging of mRNAs in the form of an mRNA-protein complex (mRNP) leads to the recruitment of the mRNA export adaptor THOC4/ALY, via its interaction with the splicing factor UAP56, forming a large complex termed the transcription-export complex (TREX) (1,2,5). THOC4/ALY then directly interacts with NXF1/TAP, a part of the heterodimer that targets the mRNP to the nuclear pore complex, resulting in the shuttling of mRNP out of the nucleus and into the cytoplasm (1-3,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: T-cell intracellular antibody 1 (TIA-1) is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins that was originally found to induce DNA fragmentation in digitonin-permeabilized thymocytes (1). TIA-1 protein has about 80% identity to the related TIAR protein, both of which possess three amino-terminal RRM domains and a glutamine-rich carboxyl terminus (1,2). Alternative splicing is responsible for generating at least two isoforms of TIA-1 and TIAR (3,4). Several research studies indicate that TIA-1 and TIAR play a role in apoptosis, cellular stress, and inflammation. Importantly, TIA-1 and TIAR translocate from the nucleus to stress granules in response to a variety of environmental stresses (5-8). Stress granules function as sites of translational repression in response to potentially damaging conditions. mRNA transcripts targeted by TIA-1 and TIAR include TNF-α, COX-2, cytochrome c, GADD45α, and HIF-1α (8-13).

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

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

Background: TIAR is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins (1,2). It functions as a translational repressor under conditions of cellular damage (3,4). In response to cellular stress, TIAR associates with eIF1, eIF3, and the 40S ribosomal subunit and forms noncanonical preinitiation complexes that are translationally inactive (3,4). TIAR then aggregates with its family member TIA1 and facilitates the accumulation of the translationally inactive preinitiation complexes into discrete cytoplasmic foci called stress granules. The two major isoforms of TIAR are the products of alternative mRNA splicing (5,6).

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

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

Background: TIAR is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins (1,2). It functions as a translational repressor under conditions of cellular damage (3,4). In response to cellular stress, TIAR associates with eIF1, eIF3, and the 40S ribosomal subunit and forms noncanonical preinitiation complexes that are translationally inactive (3,4). TIAR then aggregates with its family member TIA1 and facilitates the accumulation of the translationally inactive preinitiation complexes into discrete cytoplasmic foci called stress granules. The two major isoforms of TIAR are the products of alternative mRNA splicing (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tristetraprolin (TTP), also known as NUP475, G0S24, RNF162A, TIS11, and ZFP36, is a CCCH tandem zinc-finger protein that binds to adenosine and uridine (AU)-rich elements (AREs) within 3'-untranslated regions of mRNA and leads to their rapid degradation (1-6). Expression of TTP is rapidly induced by mitogens and growth factors including insulin, phorbol ester, cytokines, and lipopolysaccharide (LPS). In addition, numerous phosphorylation sites on TTP can regulate its stability, nuclear to cytosolic trafficking, as well as controlling its ARE-binding activity. Many of the target mRNAs for TTP, such as TNF-α, have critical roles in inflammation and cancer (2), and mice deficient in TTP develop a systemic autoimmune inflammatory syndrome along with excessive TNF-α levels (7). Furthermore, suppression of TTP expression has been identified as a negative prognostic indicator for some cancers (8).

$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: 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: 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

Application Methods: Western Blotting

Background: Following protein synthesis, secretory, intra-organellar, and transmembrane proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. The accumulation of unfolded proteins within the ER triggers an adaptive mechanism known as the unfolded protein response (UPR) that counteracts compromised protein folding (1). The transmembrane serine/threonine kinase IRE1, originally identified in Saccharomyces cerevisiae, is a proximal sensor for the UPR that transmits the unfolded protein signal across the ER membrane (2-4). The human homolog IRE1α was later identified and is ubiquitously expressed in human tissues (5). Upon activation of the unfolded protein response, IRE1α splices X-box binding protein 1 (XBP-1) mRNA through an unconventional mechanism using its endoribonuclease activity (6). This reaction converts XBP-1 from an unspliced XBP-1u isoform to the spliced XBP-1s isoform, which is a potent transcriptional activator that induces expression of many UPR responsive genes (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Following protein synthesis, secretory, intra-organellar, and transmembrane proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. The accumulation of unfolded proteins within the ER triggers an adaptive mechanism known as the unfolded protein response (UPR) that counteracts compromised protein folding (1). The transmembrane serine/threonine kinase IRE1, originally identified in Saccharomyces cerevisiae, is a proximal sensor for the UPR that transmits the unfolded protein signal across the ER membrane (2-4). The human homolog IRE1α was later identified and is ubiquitously expressed in human tissues (5). Upon activation of the unfolded protein response, IRE1α splices X-box binding protein 1 (XBP-1) mRNA through an unconventional mechanism using its endoribonuclease activity (6). This reaction converts XBP-1 from an unspliced XBP-1u isoform to the spliced XBP-1s isoform, which is a potent transcriptional activator that induces expression of many UPR responsive genes (6).