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Product listing: VDAC2 Antibody, UniProt ID P45880 #9412 to Phospho-BAP1 (Ser592) Antibody, UniProt ID Q92560 #9373

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Voltage-dependent anion channel (VDAC), ubiquitously expressed and located in the outer mitochondrial membrane, is generally thought to be the primary means by which metabolites diffuse in and out of the mitochondria (1). In addition, this channel plays a role in apoptotic signaling. The change in mitochondrial permeability characteristic of apoptosis is mediated by Bcl-2 family proteins, which bind to VDAC, altering the channel kinetics (2). Homodimerization of VDAC may be a mechanism for changing mitochondrial permeability and supporting release of cytochrome c (3). In mammalian cells, there are three VDAC isoforms, VDAC1, which is the most widely expressed isoform, as well as VDAC2 and VDAC3 (4,5).

$248
200 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunofluorescence (Paraffin), Immunohistochemistry (Paraffin), Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: Tyrosine phosphorylation plays a key role in cellular signaling (1). Research studies have shown that in cancer, unregulated tyrosine kinase activity can drive malignancy and tumor formation by generating inappropriate proliferation and survival signals (2). Antibodies specific for phospho-tyrosine (3,4) have been invaluable reagents in these studies. The phospho-tyrosine monoclonal antibodies developed by Cell Signaling Technology are exceptionally sensitive tools for studying tyrosine phosphorylation and monitoring tyrosine kinase activity in high throughput drug discovery.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

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

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

Background: DDX6, also known as RCK and p54, was identified as a proto-oncogene product and is a member of the ATP-dependent DEAD box helicase family (1,2). This protein interacts with translation initiation factor eIF4E in the cytoplasmic P-bodies (3) and represses mRNA translation (4). DDX6 is a component of the miRNA induced silencing complex (miRISC) and interacts with Argonaute 1 (Ago1) and Argonaute 2 (Ago2) proteins in vitro and in vivo (5), functioning in miRNA-mediated translational repression (5). Depletion of DDX6 leads to the disruption of cytoplasmic P-bodies indicating that it is required for P-body formation (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Cullins are proteins that function as molecular scaffolds for modular ubiquitin ligases typified by the SCF (Skp1-CUL1-F-box) complex (1-3). The substrate selectivity of these E3 ligases is dictated by a specificity module that binds cullins. In the SCF complex, this module is composed of Skp1, which binds directly to CUL1, and a member of the F-box family of proteins such as Skp2 (1-4). CUL3 has been shown to be required for embryonic development in mammals and Caenorhabditis elegans (5-7) but until recently, its substrate specificity adaptor had yet to be elucidated. It is now recognized that substrate adaptors for CUL3-based ubiquitin ligase complexes contain a conserved BTB/POZ (Pox virus and Zinc finger) domain. This domain, which was initially identified in the Drosophila transcriptional repressors broad complex, tramtrack, and bric-a-brac is present in more than 190 human proteins. BTB proteins contain a variety of putative protein-protein interaction domains, including MATH domains, zinc finger repeats, and kelch repeats (8).There are several lines of evidence suggesting that Kelch-like 12 protein (KLHL12) is a substrate-specific adaptor for the CUL3-based ubiquitin ligase complex. Analysis of the amino acid sequence of KLHL12 reveals an amino-terminal BTB motif, a central linker region, and a carboxy-terminal kelch domain composed of kelch repeats. Furthermore, KLHL12 has been shown to negatively regulate Wnt signaling by binding Disheveled and targeting it for ubiquitin-dependent proteasomal degradation (9). More recently, KLHL12 was shown to drive the assembly of large COPII vesicles by promoting the monoubiquitination of the COPII component Sec31. As a result, CUL3-KLHL12-dependent ubiquitination is essential for collagen export, a step that is required for integrin-dependent mouse embryonic stem cell division (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$262
3 nmol
300 µl
SignalSilence® Stat6 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Stat6 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human, Mouse

Background: Upon activation by Janus kinases, Stat6 translocates to the nucleus where it regulates cytokine-induced gene expression. Stat6 is activated via phosphorylation at Tyr641 and is required for responsiveness to IL-4 and IL-13 (1-4). In addition, Stat6 is activated by IFN-α in B cells, where it forms transcriptionally active complexes with Stat2 and p48 (5,6). Protein phosphatase 2A is also involved in regulation of IL-4-mediated Stat6 signaling (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$262
3 nmol
300 µl
SignalSilence® CK2α siRNA I (Rodent Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit CK2α expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Mouse

Background: CK2 (formerly called Casein Kinase II) is a highly conserved protein kinase with more than 300 substrates regulating cell growth, cell death, and cell survival. CK2 has been implicated in the response to UV irradiation-induced DNA damage, targeting XRCC1 (1) and BRCA1 (2) as well as regulating p53 tumor suppressor protein functions (3). Furthermore, CK2 plays a key role in NF-κB activation (4). UV irradiation stimulates CK2-mediated phosphorylation of several carboxy-terminal residues within IκBα, resulting in IκBα proteasomal degradation and the release and nuclear translocation of active NF-κB. CK2 is also dysregulated in many cancers (5) and neurodegenerative diseases such as Alzheimer's and Parkinson's diseases (6). Structurally, CK2 is a multimeric protein complex consisting of two catalytic subunits (α or α') and two regulatory β subunits (7). CK2 is distributed ubiquitously and is apparently constitutively active (7). While cell cycle-dependent Ser-Pro phosphorylation sites have been identified on CK2α and CK2β, Tyr255 phosphorylation by the Src-related kinase c-Fgr seems to have the greatest effect on CK2α activity (8,9).

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

Application Methods: Western Blotting

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Collapsin Response Mediator Protein-2 (CRMP-2) is expressed at high levels in the developing nervous system and plays a critical role in axonal outgrowth by specifying axon/dendrite fate and establishing neuronal polarity (1,2). CRMP-2 enhances axon elongation and branching by binding to tubulin heterodimers to promote microtubule assembly (3). GSK-3β inactivates CRMP-2 by phosphorylating it at Thr514. CRMP-2 is primed following phosphorylation at Ser522 by CDK5 and at Thr518 by GSK-3β (2). Phosphorylation of CRMP-2, which decreases tubulin binding ability, can be inhibited by NT-3 and BDNF through the PI3 kinase/Akt pathway (2). CRMP-2 also mediates semaphorin-induced growth cone collapse (4). Hyperphosphorylation of CRMP-2 is found in Alzheimer disease plaques with concurrent elevated GSK-3β activity in these patients (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Collapsin Response Mediator Protein-2 (CRMP-2) is expressed at high levels in the developing nervous system and plays a critical role in axonal outgrowth by specifying axon/dendrite fate and establishing neuronal polarity (1,2). CRMP-2 enhances axon elongation and branching by binding to tubulin heterodimers to promote microtubule assembly (3). GSK-3β inactivates CRMP-2 by phosphorylating it at Thr514. CRMP-2 is primed following phosphorylation at Ser522 by CDK5 and at Thr518 by GSK-3β (2). Phosphorylation of CRMP-2, which decreases tubulin binding ability, can be inhibited by NT-3 and BDNF through the PI3 kinase/Akt pathway (2). CRMP-2 also mediates semaphorin-induced growth cone collapse (4). Hyperphosphorylation of CRMP-2 is found in Alzheimer disease plaques with concurrent elevated GSK-3β activity in these patients (5).

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

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

Background: The MAPK and CDK families of serine/threonine protein kinases play important roles in cell signaling and cell cycle control. These kinases phosphorylate threonine or serine followed by a proline residue (1-6). To facilitate the study and discovery of new MAPK and CDK substrates, Cell Signaling Technology has developed antibodies that bind to phospho-threonine or phospho-serine followed by proline.

$262
3 nmol
300 µl
SignalSilence® SirT6 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit SirT6 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: The Silent Information Regulator (Sir2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of this family is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT6, a mammalian homolog of Sir2, is a nuclear, chromatin-associated protein that promotes the normal maintenance of genome integrity mediated by the base excision repair (BER) pathway (2-4). The BER pathway repairs single-stranded DNA lesions that arise spontaneously from endogenous alkylation, oxidation, and deamination events. SirT6 deficient mice show increased sensitivity to DNA-damaging agents, including the alkylating agents MMS and H2O2 (2). In addition, these mice show genome instability with increased frequency of fragmented chromosomes, detached centromeres, and gaps (2). SirT6 may regulate the BER pathway by deacetylating DNA Polβ or other core components of the pathway (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Specificity protein 1 (SP1) is a ubiquitously expressed transcription factor belonging to the family of C2H2-type zinc finger containing DNA-binding proteins. SP1 binds GC-rich motifs with high affinity and regulates the expression of numerous mammalian genes (1,2). It interacts with many other transcription factors, such as c-Myc, EGR1, and Stat1, and with basal transcription machinery components. SP1 interacts with chromatin-modifying factors, such as histone deacetylases (HDACs) and p300 in chromatin remodeling. Transcriptional activity and stability of SP1 are regulated by post-translational modification, including phosphorylation, acetylation, ubiquitination, and glycosylation (3). Glycosylation of SP1 following insulin treatment leads to increased nuclear localization, while glucagon treatment increases cytoplasmic SP1 levels (4-6). Investigators have found high levels of SP1 in patients with Alzheimer's disease (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Small non-coding RNAs are important regulators of gene expression in higher eukaryotes (1,2). Several classes of small RNAs, including short interfering RNAs (siRNAs) (3), microRNAs (miRNAs) (4), and Piwi-interacting RNAs (piRNAs) (5), have been identified. MicroRNAs are about 21 nucleotides in length and have been implicated in many cellular processes such as development, differentiation, and stress response (1,2). MicroRNAs regulate gene expression by modulating mRNA translation or stability (2). MicroRNAs function together with the protein components in the complexes called micro-ribonucleoproteins (miRNPs) (2). Among the most important components in these complexes are Argonaute proteins (1,2). There are four members in the mammalian Argonaute family and only Argonaute 2 (Ago2) possesses the Slicer endonuclease activity (1,2). Argonaute proteins participate in the various steps of microRNA-mediated gene silencing, such as repression of translation and mRNA turnover (1).

$122
20 µl
$248
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: Much of the dynamic behavior of cellular proteins, including the regulation of molecular interactions (1), subcellular localization (2), and transcriptional regulation (3) is controlled by a variety of post-translational modifications (4). Antibodies specific for these post-translational modifications are invaluable tools in the quest to understand normal and pathogenic molecular and cellular behavior.General protein modification antibodies are designed to react with modified amino acid residues (e.g. phospho-threonine, phospho-tyrosine, acetyl-lysine, nitro-tyrosine) independently of the sequence in which they are embedded. This ability to recognize modified residues in a "context-independent" fashion gives these antibodies broad reactivities, presumably conferring upon them the ability to react with hundreds of distinct proteins. This broad pattern of reactivity makes these antibodies especially valuable in multiplex analyses and target discovery programs.

The Rab Family Antibody Sampler Kit provides an economical means to evaluate the presence and status of Rab proteins in cells. This kit provides enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.
The Cytokeratin Antibody Sampler Kit provides an economical means to evaluate the presence and status of selected keratin proteins. The kit provides enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

The TCF/LEF Family Antibody Sampler Kit provides an economical means of detecting total protein from the TCF/LEF1 family members. The kit contains enough primary and secondary antibodies to perform two Western blots with each antibody.
$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Mouse, Rat

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

Background: Much of the dynamic behavior of cellular proteins, including the regulation of molecular interactions (1), subcellular localization (2), and transcriptional regulation (3) is controlled by a variety of post-translational modifications (4). Antibodies specific for these post-translational modifications are invaluable tools in the quest to understand normal and pathogenic molecular and cellular behavior.General protein modification antibodies are designed to react with modified amino acid residues (e.g. phospho-threonine, phospho-tyrosine, acetyl-lysine, nitro-tyrosine) independently of the sequence in which they are embedded. This ability to recognize modified residues in a "context-independent" fashion gives these antibodies broad reactivities, presumably conferring upon them the ability to react with hundreds of distinct proteins. This broad pattern of reactivity makes these antibodies especially valuable in multiplex analyses and target discovery programs.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: RanBP3 was originally identified as RanGTP binding protein located in the nucleus and involved in the nuclear exporting process (1). It functions as a cofactor for CRM1 nuclear export by binding to CRM1, stabilizing the RanGTP-CRM1-cargo interaction and promoting complex association with nuclear pore proteins (2,3). In the absence of Ran-bound GTP, RanBP3 prevents binding of CRM1 complex to the nuclear pore complex. In addition to CRM1, RanBP3 also has been shown to bind to RanGEF-RCC1 and increase the guanine nucleotide exchange activity of RCC1 for RanGTP-CRM1-Cargo (1,4). In some cases, as with β-catenin and Smad2/3, RanBP3 binding may mediate the target protein nuclear export in a Ran-dependent, but CRM1-independent manner (5,6). RanBP3 is phosphorylated at Ser58 through the PI3K/Akt or ERK/RSK pathway. This phosphorylation is important for RanBP3 function in nuclear export, likely due to stimulation of RCC1 activity (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, 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).

$122
20 µl
$303
100 µl
$717
300 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, Xenopus

Application Methods: Immunohistochemistry (Paraffin), 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BAP1 (BRCA1-Associated Protein 1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its N-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its C-terminal segment (1). Frequent gene locus rearrangement, deletion and null mutation of BAP1 have been found in lung and breast cancers (1,2). Mutation analysis in vivo in cancer cell line survival and in animal tumorigenesis indicate that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinyled BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the compex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinylate HCF-1, thereby controlling its stability (6).Phosphorylation of Ser592 on BAP1 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (7).