20% off purchase of 3 or more products* | Learn More >>

Monoclonal Antibody Mrna 3'-end Processing

$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).

$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: 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, 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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Poly(A)-binding protein 2 (PABP2, PAPBN1) is a nuclear RNA-binding protein involved in the post-transcriptional processing of RNA molecules (1). The PABP2 protein enhances RNA polyadenylation by stimulating poly(A) polymerase (PAP) activity and facilitating the interaction between PAP and the cleavage and specificity factor (CPSF) to regulate poly(A) tail length (2-4). The role that PABP2 plays in regulating poly(A) tail formation and site selection may be important in influencing the length of the 3’ untranslated region (UTR), which can alter transcript stability and translation by RNA binding proteins and miRNAs (1,5). Mutations in the corresponding PABPN1 gene can result in oculopharyngeal muscular dystrophy (OPMD), an autosomal dominant muscle disorder characterized by weakness in proximal limb muscles, ptosis, and dysphagia (1,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: S-adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) is a member of S-adenosylhomocysteine hydrolase family, which participates in the metabolism of S-adenosyl-L-homocysteine (1). Two Drosophila homologs of S-adenosylhomocysteine hydrolase-like proteins, dAhcyL1 and dAhcyL2, were identified as novel components of methionine metabolism (2). dAhcyL1 and dAhcyL2 function as dominant-negative regulators of S-adenosylhomocysteine hydrolase (2). Global down-regulation of both dAhcyL1 and dAhcyL2 extended life span (2). In addition, brain-specific down regulation of dAhcyL1 extended life span (2). AHCYL1 is also known as inositol 1,4,5-trisphosphate receptor (IP3R) binding protein released with IP3 (IRBIT) (1, 3). This protein binds to the endoplasmic reticulum calcium release channel IP3R and represses its acitivity (1, 3). As a multifunctional regulator, AHCYL1/IRBIT can also form a complex with and suppress the activity of ribonucleotide reductase, thereby influencing the balance of deoxynucleotide triphosphates essential for DNA replication and genomic integrity (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CDC73 (HPRT2) is a putative tumor suppressor protein thought to bind RNA polymerase II to help inhibit cell cycle progression (1,2). Commonly referred to as parafibromin, CDC73 is expressed in endocrine tissues, kidney, heart, and skeletal muscle and is localized to both nuclear and cytoplasmic compartments (3). CDC73 acts as a Wnt signaling regulator as it binds the carboxy-terminal region of β-catenin (4). Mutations in the corresponding gene cause an endocrine disorder known as hyperparathyroidism 2, which is characterized by hypercalcemia, bone resorption, and the development of jaw tumors (5).

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

Application Methods: Western Blotting

Background: The PAF (RNA polymerase II (RNAPII) associated factor) complex was initially identified in yeast and is comprised of subunits PAF1, Leo1, Ctr9, Cdc73, RTF1 and Ski8 (1,2). The PAF complex plays an important role in transcription initiation and elongation by RNAPII by regulating the establishment of proper histone modifications such as histone H2B ubiquitination and the recruitment of the histone chaperone FACT (facilitates chromatin transcription) (3-5). The PAF complex also plays a role in mRNA processing and maturation by interacting with and recruiting the cleavage and polyadenylation specificity factor and cleavage stimulation factor complexes via the Cdc73 subunit (6,7). In addition, the Ski8 subunit of the PAF complex is part of the hSKi complex that regulates RNA surveillance, suggesting an important function of the complex in coordinating events associated with proper RNA maturation during transcription (1,5).

$305
50 tests
100 µl
Cell Signaling Technology Antibody conjugated to Alexa Fluor ® 488 fluorescent dye and tested in-house for direct Flow Cytometric analysis of human cells. The unconjugated antibody, #4135, reacts with human and mouse. CST expects that Cyclin B1 (V152) Mouse mAb (Alexa Fluor®488 conjugate) will also recognize Cyclin B1 in these species.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$305
50 tests
100 µl
Cell Signaling Technology Antibody conjugated to Alexa Fluor®647 fluorescent dye and tested in-house for direct Flow Cytometric analysis of human cells. The unconjugated antibody #4135 reacts with, among others, human, mouse and hamster Cyclin B1. CST expects that Cyclin B1 Mouse mAb (Alexa Fluor®647 conjugate) will also recognize Cyclin B1 in these species.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Western Blotting

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

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

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

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).