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Product listing: Pbx1 Antibody, UniProt ID P40424 #4342 to Phospho-(Ser) Arg-X-Tyr/Phe-X-pSer Motif Antibody #2981

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Pbxs (Pre-B cell leukemia transcription factors) belong to the Three Amino Acid Loop Extension (TALE) family of homeodomain containing protein (1). Pbx1 has two isoforms, Pbx1a and 1b, that are divergent in sequence at the carboxy terminus, which is a result of alternative mRNA splicing. Unlike other homeoselector genes that have restricted expression in development Pbx genes are ubiquitously expressed in both fetal and adult tissue (1). Human pre-B cell acute leukemias are frequently associated with a t(1;19)(q23;p13.3) translocation that results in a fusion between the E2A and Pbx1 genes (2,3). Pbx1 genes are not normally expressed in lymphoid tissues, and the E2A-Pbx1 fusion protein is a potent transcription factor that drives aberrant gene expression.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The proprotein convertases (PCs) are enzymes that activate precursor proteins through proteolytic cleavage within the secretory pathway. PCs comprise several enzymes that are basic amino acid-specific proteinases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7), as well as nonbasic amino acid convertases (S1P and PC9) (1). PCs have a common structure that includes an N-terminal signal peptide for secretory pathway targeting; a pro-domain that is thought to act as an intramolecular chaperone; a catalytic domain containing the active site; a P-domain that contributes to the overall folding of the enzyme by regulating stability, calcium-, and pH-dependence; and a C-terminal domain that interacts with the membrane (2). PCs act in a tissue- and substrate-specific fashion to generate an array of bioactive peptides and proteins from precursors, both in the brain and the periphery (3).

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

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

Background: PCK2 (PEPCK2 or PEPCK-M) encodes an isoform of phosphoenolpyruvate carboxykinase (PEPCK) that is found in the mitochondria of renal and hepatic tissues (1). PEPCK is involved in gluconeogenesis, the process of generating glucose from non-carbohydrate substrates such as lactate and glycerol (2). PEPCK catalyzes the reaction whereby oxaloacetate becomes phosphoenolpyruvate, a rate limiting step in the metabolic process (2). The predominant function of PCK2 is to process the lactate that is continually produced by red blood cells in the liver and kidney (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The centrosome is composed of a pair of centrioles surrounded by electron-dense pericentriolar material and functions as the microtubule-organizing center responsible for microtubule nucleation and spindle organization during cell cycle progression (1). Percentriolar material 1 (PCM-1) is a large, 228 kDa protein associated with the centrosome in a cell cycle dependent manner (2). PCM-1 localizes to small cytoplasmic granules called centrosomal satellites (3). PCM-1 is required for the assembly of several centrosomal proteins including centrin, pericentrin, ninein, NEK2, and CEP250 (4-8). Chromosomal translocations involving genes encoding PCM-1 and the tyrosine kinases Ret and Jak2 are associated with some cancers, including papillary thyroid carcinoma and myeloid leukemia (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The centrosome is composed of a pair of centrioles surrounded by electron-dense pericentriolar material and functions as the microtubule-organizing center responsible for microtubule nucleation and spindle organization during cell cycle progression (1). Percentriolar material 1 (PCM-1) is a large, 228 kDa protein associated with the centrosome in a cell cycle dependent manner (2). PCM-1 localizes to small cytoplasmic granules called centrosomal satellites (3). PCM-1 is required for the assembly of several centrosomal proteins including centrin, pericentrin, ninein, NEK2, and CEP250 (4-8). Chromosomal translocations involving genes encoding PCM-1 and the tyrosine kinases Ret and Jak2 are associated with some cancers, including papillary thyroid carcinoma and myeloid leukemia (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Three distinct PCTAIRE isoforms (PCTAIRE 1, PCTAIRE 2 and PCTAIRE 3) have been identified in humans and belong to the CDK family of serine/threonine protein kinases. These proteins have a core kinase domain flanked by unique amino- and carboxy-terminal domains. CDK proteins are known to regulate the cell cycle. All three PCTAIRE isoforms are abundantly expressed and catalytically active in post-mitotic brain, suggesting that they may function in processes other than cell division (1). PCTAIRE 1 is a cytoplasmic phosphoprotein whose kinase activity peaks in G2 and S phase (2). While one study indicates that noncovalent interactions with a regulatory component (such as a cyclin) are necessary for catalytic activity of PCTAIRE 1, others show that the monomeric protein is fully active (3). The Cdk5/p25 complex phosphorylates PCTAIRE 1 at Ser95, enhancing its kinase activity (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Platelet derived growth factor (PDGF) proteins function as dimeric isoforms (i.e., PDGF AA, PDGF AB, PDGF BB, PDGF CC and PDGF DD) that bind receptor tyrosine kinases and activate cytoplasmic SH2 domain-containing proteins to control multiple signaling pathways that regulate angiogenesis, cell growth, actin reorganization, migration and differentiation (1). PDGFA-associated protein 1 (PDAP1) was originally identified as a novel, PDGF-associated protein found in a rat retinal tumor cell line (2). While copurified with PDGFA, PDAP1 interacts with PDGFB at a slightly higher affinity than with PDGFA (2). Although the exact function of PDAP1 is unclear, it has been shown to both increase PDGFA-induced incorporation of [3H]thymidine in Swiss 3T3 cells and decrease PDGFB growth factor activity (2). Ubiquitously expressed PDAP1 is highly conserved among species (2,3) and is phosphorylated in vitro by several kinases, including PKC, PKA, CKI and CKII. Among this group, CKII seems to be the major kinase that phosphorylates PDAP1 in intact cells (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The superfamily of phosphodiesterases (PDEs) catalyses the hydrolysis of 3',5'-cyclic nucleotides into the corresponding nucleotide 5'-monophosphates. PDE5 is a cGMP-specific enzyme that contains two cGMP binding sites in its amino-terminal regulatory domain (1). Elevation of cGMP levels causes activation of PKG, which phosphorylates PDE5 at Ser102 (2). Phosphorylation of PDE5 stimulates its enzymatic activity and enhances cGMP binding affinity in the regulatory domain, leading to a decrease in intracellular cGMP levels (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The superfamily of phosphodiesterases (PDEs) catalyses the hydrolysis of 3',5'-cyclic nucleotides into the corresponding nucleotide 5'-monophosphates. PDE5 is a cGMP-specific enzyme that contains two cGMP binding sites in its amino-terminal regulatory domain (1). Elevation of cGMP levels causes activation of PKG, which phosphorylates PDE5 at Ser102 (2). Phosphorylation of PDE5 stimulates its enzymatic activity and enhances cGMP binding affinity in the regulatory domain, leading to a decrease in intracellular cGMP levels (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

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

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

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

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

Application Methods: Western Blotting

Background: Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (1,2) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (3). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: PDLIM2, also known as Mystique, contains an amino-terminal PDZ domain and a carboxy-terminal LIM domain. PDLIM2 was orginally found to be associated with cytoskeletal proteins in epithelial cells to promote cell attachment and migration (1,2). Subsequent studies have shown that PDLIM2 can also inhibit NF-κB activity by acting as a nuclear ubiquitin E3 ligase for p65 (3). PDLIM2 is suppressed in cancer cell lines by DNA methylation (4,5). Expression of PDLIM2 can inhibit anchorage-independent growth and tumor formation.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: PEA-15 is a 15 kDa phosphoprotein expressed abundantly in astrocytes and fibroblasts as well as in tissues, including the lung and eye (1). The protein has been shown to coordinate cell growth, death, and glucose utilization (2-4). The amino-terminal DED domain of PEA-15 mediates its binding to FADD or Erk and further regulates the Erk and apoptosis signaling pathways. PEA-15 can be phosphorylated at two serine residues, Ser104 and Ser116, located within the carboxy terminus. Phosphorylation at these sites regulates binding to Erk and FADD (2,3).

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

Application Methods: Western Blotting

Background: Presenilin Enhancer 2 (PEN2) is a small integral membrane glycoprotein that contains two recognized transmembrane domains. Both the N- and C-terminal domains are oriented into the lumen of the endoplasmic reticulum (1). PEN2, along with Presenilin 1, Presenilin 2, Nicastrin, and APH-1 form the protein complex γ-secretase (2). The proteinase BACE catalyses the initial step in APP processing by cleaving and releasing soluble APPβ (3). The remaining membrane bound APP is then cleaved by the γ-secretase complex, causing the release of amyloid β-peptide, the main constituent of amyloid plaques. These plaques are a hallmark of Alzheimer’s disease pathology (2). In addition to APP, the γ-secretase complex cleaves several other proteins and necessary presenilin-dependent signaling cascades, including the Notch pathway (4). It was found that PEN2 is an important part of the γ-secretase complex, and knocking it down results in reduced amounts of the complex, resulting in a loss of γ-secretase activity (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Phosphofructokinase (PFK) catalyzes the phosphorylation of fructose-6-phosphate in glycolysis (1). There are three isozymes: muscle-type, liver-type, and platelet-type (2,3). Platelet-type phosphofructokinase (PFKP) is expressed in various cell types (4,5). Research studies have shown that genetic variations in PFKP are associated with individuals born small for gestational age that are prone to obesity and diabetes later in adulthood (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: 6-phosphogluconate dehydrogenase (PGD or 6PGD) catalyzes the conversion of 6-phosphogluconate and NADP+ to ribulose 5-phosphate and NADPH in the pentose phosphate pathway (1). Research studies show that knockdown of PGD results in the induction of senescence and inhibition of growth of lung cancer cells (2). Additional research suggests that PGD influences the migration of some cancer cells by regulating c-Met phosphorylation state (3). Furthermore, it was shown that the glycolytic enzyme PGAM1 substrate (3-phosphoglycerate) regulates the pentose phosphate pathway by deactivating PGD/6PGD (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The prohibitins, called PHB1 and PHB2, are highly conserved proteins that are present in multiple compartments in eukaryotic cells. PHB1 is 30kDa tumor suppressor protein involved in cell cycle control (1). PHB1 has been found in mitochondria, the nucleus and the plasma membrane, as well as extracellularly in circulation (2). In mitochondria prohibitins mainly exist as membrane-bound ring complexes and function as chaperones maintaining mitochondrial protein stability during protein synthesis and transportation (3,4). In the nucleus prohibitins interact with transcription factors such as Rb and p53 to regulate target gene transcription (2,5). Extracellular prohibitin can bind and activate C3 to enhance complement activation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). Polycomb group proteins regulate cell proliferation and senescence through repression of the p16Ink4a and p19Arf genes, and are essential in maintaining adult hematopoietic, neural stem cells, and embryonic stem cells (3-5). PcG proteins are found in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. DNA-binding transcription factors recruit the EED-EZH2 complex to genes, which methylates histone H3 on Lys27 (6). Methylation of Lys27 facilitates the recruitment of the PRC1 complex, which ubiquitinylates histone H2A on Lys119 (7). PRC1 is composed of BMI1 and RING1A, which enhance the E3 ubiquitin ligase activity of the RING1B catalytic subunit (8). Polyhomeotic-like 1 (PHC1) is one of several additional PRC1 complex proteins that are required to maintain the silenced state of PRC1 target genes and mediate proper anterior-posterior specification during development (9). Mutations in the corresponding PHC1 gene correlate with an autosomal recessive form of primary microcephaly characterized by low-to-normal cognitive function and impaired DNA repair (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PHD1 (Egln2), PHD-2 (Egln1), and PHD3 (Egln3) are members of the Egln family of proline hydroxylases. They function as oxygen sensors that catalyze the hydroxylation of HIF on prolines 564 and 402, initiating the first step of HIF degradation through the VHL/ubiquitin pathway (1,2). PHD1 is highly expressed in a wide array of tissues whereas PHD2 and PHD3 are expressed mainly in heart and skeletal muscle (1,3). The mRNA levels of PHD are upregulated by HIF through the hypoxia-response element under low oxygen conditions (4-7). These three enzymes also exhibit different peptide specificity target proteins, PHD1 and PHD2 can hydroxylate both proline 402 and proline 564, but PHD3 can only hydroxylate proline 564 (2,8). In addition to HIF, PHD enzymes have also has been shown to catalyze the hydroxylation of RNA polymerase subunits and myogenin (3,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: PHD finger protein 19 (PHF19), also known as polycomb-like protein 3 (PCL3), is a polycomb group protein that functions as an accessory subunit of the polycomb repressor complex 2 (PRC2), which represses target gene expression through methylation of histone H3 at lysine 27 by the EZH2 methyltransferase (1). PHF19 recruits PRC2 to target genes by binding trimethylated histone H3 lysine 36, a mark of active chromatin, via its Tudor domain (2-4). PHF19 associates with PRC2 and the histone H3 lysine 36 demethylases NO66 and FBXL10, and is required to recruit PRC2 and NO66/FBXL10 to stem cell genes during differentiation, resulting in PRC2-mediated trimethylation of histone H3 lysine 27, loss of trimethylated histone H3 lysine 36, and transcriptional silencing (2-4). Thus, PHF19 is critical for the proper transition of stem cell genes from the active to inactive state during differentiation of embryonic stem cells.

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

Application Methods: Western Blotting

Background: Plant homeodomain-like finger 6 (PHF6) is a 41 kDa transcriptional repressor that was first identified as a mutated gene in Börjeson-Forssman-Lehmann syndrome (BFLS), an X-linked intellectual disability disorder (1,2). Somatic loss-of-function mutations in the PHF6 gene have also been linked to T-cell acute lymphoblastic leukemia (T-ALL) and acute myeloid leukemia (AML) (3-5). Structurally, PHF6 contains two nuclear localization sequences, one nucleolar localization sequence, and two plant homeodomain (PHD)-like zinc fingers (6,7). Unlike other PHD proteins, the PHD domains of PHF6 are considered to be imperfect and have not been shown to directly bind to histones; however, the isolated second PHD domain (PHD2) has been shown to bind dsDNA directly (7). A more recent study finds that PHF6 interacts with histones via protein-protein interactions, and that this association is independent of DNA and enriched in the presence of the activating marks H3K27ac and H3K4me3 (8). PHF6 interacts with PAF1 and other subunits of the PAF1 transcription elongation complex, and knockdown of either PHF6 or PAF1 adversely affects proper neuronal positioning and migration in mouse cerebral cortex (9). PHF6 has also been shown to associate with members of the nucleosome remodeling and deacetylation (NuRD) chromatin remodeling complex, including CHD4, HDAC1, and RBBP4, where it is likely involved in transcriptional repression of developmental genes (10). PHF6 plays a critical role in regulating hematopoiesis, particularly by regulating chromatin accessibility to lineage-specific transcription factors. Studies suggest that PHF6 promotes B-cell lineage differentiation through the expression of B-cell specific genes, while simultaneously suppressing T-cell lineage differentiation (8). Indeed, a CRISPR-Cas9 knockout study shows that PHF6 is required for growth of B-ALL cells, while mice transplanted with PHF6-deficient B-ALL cells develop T-ALL phenotypes (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate (1).Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells (2-4), which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers (5,6). Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo (5). Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells (7).

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

Application Methods: Western Blotting

Background: Pleckstrin homology-like domain family A member 3 (PHLDA3) is one of three relatively small, similar proteins that share a common pleckstrin homology (PH) domain. Expression of PHLDA3 and the related PHLDA1 occurs in several fetal and adult tissues, in contrast to the more restricted expression of PHLDA2 seen in mouse tissues (1). PHLDA3 is one of several proteins induced following treatment of tumor cells with cisplatin, an anti-cancer drug that cross-links DNA and promotes apoptosis through activation of the tumor suppressor p53 (2). Additional evidence that PHLDA3 is involved in promoting apoptosis through p53 came from a study examining the opposing effects of p53 and Akt in tumor development. Tumor suppressor p53 binds the PHLDA3 promoter to induce transcription. Induced overexpression of PHLDA3 increases apoptosis while deletion of PHLDA3 results in increased Akt activity and a reduction in p53-mediated apoptosis. PHLDA3 appears to compete with the PH domain of Akt, preventing Akt activation and promotion of Akt-induced cell survival pathways (3).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: The 14-3-3 proteins are a highly conserved family of proteins involved in the regulation of cell survival, apoptosis, proliferation and checkpoint control (1-5). Biological regulation by 14-3-3 is mediated through phosphorylation-dependent protein-protein interactions (6). Two different phospho-Ser-containing motifs are found within nearly all known 14-3-3 binding proteins (7). Motif 1 (Arg/Lys and Ser at positions -3 and -2, phospho-Ser at position 0, and Pro at position +2) is found in critical regulatory proteins including Bad, cdc25C, FKHRL1, PKC and c-Raf (5,7). Phospho-(Ser) 14-3-3 Binding Motif Polyclonal and (4E2) Monoclonal Antibodies provide powerful tools for the discovery and characterization of potential 14-3-3 binding proteins containing this motif and for high throughput drug discovery.

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Mouse

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: The 14-3-3 proteins are a highly conserved family of proteins involved in the regulation of cell survival, apoptosis, proliferation and checkpoint control (1-5). Binding of 14-3-3 is mediated through phospho-serine-containing proteins (6). Two different phospho-serine containing motifs are found using a degenerate phospho-serine-oriented peptide library technique, RSXS*XP and RXY/FXS*XP (6). Motif 2 (RXY/FXS*XP) is found in critical regulatory proteins including cdc25A, cdc25B, PKCgamma, IRS-1 and BCR (6). Although Phospho-(Ser) Arg-X-Tyr/Phe-X-pSer Motif Antibody binds 14-3-3 binding motif 2 with no requirement for proline in the +2 position, it provides a powerful tool for the discovery and characterization of potential 14-3-3 binding motif 2-containing proteins or other proteins with the RXY/FXS* motif.