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Monoclonal Antibody Metal Ion Binding

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

Application Methods: Western Blotting

Background: Initiation of eukaryotic DNA replication is a stringently regulated process that requires the cooperation of many proteins and protein complexes to occur efficiently, at the origins of replication, and once per cell cycle. The initiation of DNA replication requires a protein complex composed of two DNA polymerase α subunits and a pair of primase subunits. Primase activity catalyzes de novo synthesis of an RNA/DNA primer (initiator DNA) on the leading and lagging strands, while polymerase activity extends the initiator DNA (1). The 48 and 58 kDa primase subunits cooperate in the synthesis of small RNA primers. p48 is the catalytically active subunit (2), while p58 couples p48 to the polymerase to allow the transfer of primers to the active site. The p58 subunit may also play a role in regulation of primer length (3,4).

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

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain of several proteins has been shown to catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into seven separate families (3). The JMJD1 (Jumonji domain-containing protein 1) family, also known as JHDM2 (JmjC domain-containing histone demethylation protein 2) family, contains four members: hairless (HR), JMJD1A/JHDM2A, JMJD1B/JHDM2B, and JMJD1C/JHDM2C. Hairless is expressed in the skin and brain and acts as a co-repressor of the thyroid hormone receptor (4-6). Mutations in the hairless gene cause alopecia in both mice and humans (4,5). JMJD1A is expressed in meiotic and post-meiotic male germ cells, contributes to androgen receptor-mediated gene regulation, and is required for spermatogenesis (7-9). It has also been identified as a downstream target of OCT4 and STAT3 and is critical for the regulation of self-renewal in embryonic stem cells (10,11). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (12). JMJD1C (also known as TRIP8) is a co-factor of both the androgen and thyroid receptors and has a potential link to autism (13-15). Members of the JMJD1/JHDM2 family have been shown to demethylate mono-methyl and di-methyl histone H3 (Lys9) (3,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: SET and MYND domain containing protein 3 (SMYD3) is a member of the SET domain-containing family of protein methyltransferases and is localized to both the nucleus and cytoplasm (1-3). Several histone substrates have been identified for SMYD3; however, the data is controversial. In one study, SMYD3 has been shown to methylate histone H3 Lys4 (both di- and tri-methylation) and interact with RNA polymerase II to activate transcription (1). A second study has shown that SMYD3 preferentially methylates histone H4 Lys20 and interacts with nuclear receptor corepressor complex (NCOR) to repress transcription (2). A third study has shown that SMYD3 preferentially methylates histone H4 Lys5 (mono-, di-, and tri-methylation) (3). In addition, SMYD3 has been shown to methylate the endothelial growth factor receptor 1 (VEGFR1) on Lys831 and stimulate its kinase activity (4). Regardless of the preferred protein substrates, it is clear that SMYD3 functions as an oncogene. Research studies have shown SMYD3 is highly over-expressed in liver, breast, and rectal carcinomas. Over-expression of SMYD3 in multiple cell lines enhances proliferation, adhesion, and migration, while reduced expression results in significant suppression of cell growth (1,5-10). In addition, multiple cancer cell lines express both full length SMYD3 and a cleaved form of SMYD3 lacking the N-terminal 34 amino acids, and the cleaved form shows increased methyltransferase activity toward histone H3 (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Six transmembrane epithelial antigen of the prostate 1 (STEAP1) is a transmembrane protein abundantly expressed in normal prostate epithelial cells (1). It is a metalloreductase that reduces Fe3+ to Fe2+ and Cu2+ to Cu1+ (2). STEAP1 is also reportedly overexpressed in multiple tumor types, and has been used as a cell surface biomarker for prostate cancer and Ewing's sarcoma (3-6). Peptides derived from STEAP1 protein have been shown to induce an antigen-specific cytotoxic T lymphocyte (CTL) response that can kill tumor cells expressing STEAP1 (7). These finding are the basis for research studies examining the efficacy of antibody-drug conjugates (ADCs) targeting STEAP1 (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain of several proteins has been shown to catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into seven separate families (3). The JMJD1 (Jumonji domain-containing protein 1) family, also known as JHDM2 (JmjC domain-containing histone demethylation protein 2) family, contains four members: hairless (HR), JMJD1A/JHDM2A, JMJD1B/JHDM2B, and JMJD1C/JHDM2C. Hairless is expressed in the skin and brain and acts as a co-repressor of the thyroid hormone receptor (4-6). Mutations in the hairless gene cause alopecia in both mice and humans (4,5). JMJD1A is expressed in meiotic and post-meiotic male germ cells, contributes to androgen receptor-mediated gene regulation, and is required for spermatogenesis (7-9). It has also been identified as a downstream target of OCT4 and STAT3 and is critical for the regulation of self-renewal in embryonic stem cells (10,11). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (12). JMJD1C (also known as TRIP8) is a co-factor of both the androgen and thyroid receptors and has a potential link to autism (13-15). Members of the JMJD1/JHDM2 family have been shown to demethylate mono-methyl and di-methyl histone H3 (Lys9) (3,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain of several proteins has been shown to catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into seven separate families (3). The JMJD1 (Jumonji domain-containing protein 1) family, also known as JHDM2 (JmjC domain-containing histone demethylation protein 2) family, contains four members: hairless (HR), JMJD1A/JHDM2A, JMJD1B/JHDM2B, and JMJD1C/JHDM2C. Hairless is expressed in the skin and brain and acts as a co-repressor of the thyroid hormone receptor (4-6). Mutations in the hairless gene cause alopecia in both mice and humans (4,5). JMJD1A is expressed in meiotic and post-meiotic male germ cells, contributes to androgen receptor-mediated gene regulation, and is required for spermatogenesis (7-9). It has also been identified as a downstream target of OCT4 and STAT3 and is critical for the regulation of self-renewal in embryonic stem cells (10,11). JMJD1B is a more widely expressed family member and is frequently deleted in myeloid leukemia (12). JMJD1C (also known as TRIP8) is a co-factor of both the androgen and thyroid receptors and has a potential link to autism (13-15). Members of the JMJD1/JHDM2 family have been shown to demethylate mono-methyl and di-methyl histone H3 (Lys9) (3,8).

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

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 2 (eIF2)-associated glycoprotein, p67/methionine aminopeptidase 2 (MetAP2) is one of the three known MetAPs responsible for the co-translational processing of the N-terminal initiator methionine from nascent proteins in cells. MetAP2 regulates the rates of global protein synthesis by controlling the levels of eIF2α phosphorylation (1). MetAP2 has also been shown to bind Erk1/2 to inhibit their activation and activity, thus connecting the protein synthesis machinery with the cell signaling pathway mediated by Erk1/2 MAP kinases (2-4). Although MetAP2 is characterized as having aminopeptidase activity that removes the N-terminal methionine from nascent peptides in vitro, mounting evidence suggests that MetAP2 has no methionine aminopeptidase activity. Rather, MetAP2 possesses auto-proteolytic activity that can be inhibited by several small molecule inhibitors including anti-angiogenic drugs, fumagillin and its derivatives (5). It has also been demonstrated that O-GlcNAcylation of MetAP2 plays a major role in its stability, eIF2α binding, and maintenance of eIF2α phosphorylation (6).MetAP2 knockout mice show embryonic lethality, suggesting its role in embryonic development and survival at the initiation of gastrulation (7). It is likely that lowering the levels of MetAP2 in mammalian cells causes cell growth inhibition and leads to apoptosis due to the high levels of eIF2α phosphorylation that inhibits global protein synthesis (8). During pathological or various stress conditions, MetAP2 dissociates from eIF2 subunits possibly due to its deglycosylation-induced autoproteolytic cleavage. As a result, eIF2α becomes hyperphosphorylated and global protein synthesis is inhibited. eIF2 complex-dissociated MetAP2 also displays a higher affinity toward Erk1/2, which results in the blockade of Erk1/2 activity. Thus, MetAP2 mediates cooperation between cell signaling and protein synthesis machinery to regulate cell growth and proliferation during physiological and pathological conditions (9). Research studies have shown higher expression of MetAP2 in human cancers, supporting the contention that MetAP2 plays a role in oncogenesis. For example, investigators have reported high MetAP2 expression in follicular lymphomas, large B-cell lymphomas, and Burkitt's lymphomas (10). Elevated expression of MetAP2 has also been reported in human colorectal adenocarcinomas (11).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Prostate specific membrane antigen (PSMA, also known as FOLH1), a type II transmembrane protein of the M28 family, has both folate hydrolase and N-acetylated-alpha-linked acidic dipeptidase activity. PSMA was originally identified in the LNCaP cell line, which was derived from a prostate adenocarcinoma lymph node metastasis (1,2). PSMA is an established prostate cancer marker (3); however, it is expressed in other tissues, including kidney, liver, and urinary bladder (4), and it is associated with tumor neovasculature (5) as well. Research studies suggest that PSMA is both a potential diagnostic readout and therapeutic target (6-8).

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

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

Background: Arginase-2 is a mitochondrial enzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea (1). Research studies have shown that in acute myeloid leukemia (AML) patients, arginase-2 is released from AML blasts to the plasma, leading to the suppression of T-cell proliferation (2). It was also shown that arginase-2 is required for the immunosuppressive properties of neonatal CD71(+) erythroid cells, which inhibits neonatal host defense against infection (3). In addition, the expression of arginase-2 in dendritic cells is repressed by microRNA-155 during maturation (4). This repression is essential for T-cell activation and response (4).

$327
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 700 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Smad1 (Ser463/465)/ Smad5 (Ser463/465)/ Smad9 (Ser465/467) (D5B10) Rabbit mAb #4858.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Mitochondria continuously divide and fuse. This dynamic process is highly regulated in response to various physiological cues (1,2). The GTPase OPA1 mediates the fusion of the mitochondrial inner membrane. Constitutive proteolytic processes mediated by OMA1 (S1 site) and YME1L (S2 site) convert long isoforms (L-OPA1) into short isforms (S-OPA1). The balance between L-OPA1 and S-OPA1 is required to maintain a normal morphology of mitochondria (3,4).OMA1 is synthesized as a precursor and processed into a mature form (5,6). OMA1 is constitutively active and cleaves L-OPA1 at the S1 site. However, various stress stimuli can further activate OMA1 and result in the rapid and complete conversion of L-OPA1 into S-OPA1, which inhibits fusion and causes mitochondrial fragmentation (7).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-amylase catalyzes the cleavage of 1, 4-α-D-glucosidic bonds in oligosaccharides and polysaccharides (1). The enzyme is normally produced and secreted in salivary glands (salivary α-amylase or AMY1) and pancreas (pancreatic α-amylase or AMY2A) (1). Studies reported the release of an ectopically expressed α-amylase in certain tumors (1). Furthermore, a new type of α-amylase (carcinoid α-amylase or AMY2B) was identified in a lung carcinoid tissue (2-4). The ectopic expression of α-amylase in a neuroendocrine tumor was also reported (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Alpha-fetoprotein (AFP) is a 65 kDa glycoprotein found in the mammalian fetal liver, yolk sac, and GI tract. While AFP expression in adult cells is low, it is aberrantly expressed in adult liver cancer cells (1,2). The tumor suppressor gene p53 and β-catenin are both involved in the regulation of AFP expression. In normal adult cells, p53 binds to the repressor region of the AFP gene, thereby blocking transcription. Mutations in both p53 and β-catenin are associated with aberrant expression of AFP. Research studies have shown that elevated serum AFP levels are predictive of hepatocellular carcinoma (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Bassoon (BSN), named such to underline its presumptive role in orchestrating events of the synaptic vesicle cycle (1), is a very large coiled-coil protein and is one of the core components of the cytomatrix at the active zones of both excitatory and inhibitory synapses (2). BSN is a scaffold protein that is a component of the synaptic ribbon, an electron-dense structure anchored at the active zone that tethers synaptic vesicles. Genetic disruption of BSN displaces the anchoring of ribbons to the active zones of photoreceptors and cochlear inner hair cells (3), and this displacement of the ribbons substantially impairs synaptic transmission, suggesting that, when present, BSN is important for the vesicle cycle (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: MOB1 was first identified in yeast as a protein that binds to Mps with essential roles in the completion of mitosis and the maintenance of ploidy (1). Its Drosophila and mammalian homologs, Mats and MOB1, respectively, are involved in the Hippo signaling tumor suppressor pathway, which plays a critical role in organ size regulation and which has been implicated in cancer development (2-5). There are two MOB1 proteins in humans, MOB1α and MOB1β, that are encoded by two different genes but which have greater than 95% amino acid sequence identity (6). Both forms bind to members of the nuclear Dbf2-related (NDR) kinases, such as LATS1/2 and NDR1/2, thereby stimulating kinase activity (7-9). This binding is promoted by the phosphorylation of MOB1 at several threonine residues by MST1 and/or MST2 (5,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Prostate specific membrane antigen (PSMA, also known as FOLH1), a type II transmembrane protein of the M28 family, has both folate hydrolase and N-acetylated-alpha-linked acidic dipeptidase activity. PSMA was originally identified in the LNCaP cell line, which was derived from a prostate adenocarcinoma lymph node metastasis (1,2). PSMA is an established prostate cancer marker (3); however, it is expressed in other tissues, including kidney, liver, and urinary bladder (4), and it is associated with tumor neovasculature (5) as well. Research studies suggest that PSMA is both a potential diagnostic readout and therapeutic target (6-8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).