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Product listing: PathScan® Phospho-ALK (Tyr1604) Chemiluminescent Sandwich ELISA Kit, UniProt ID Q9UM73 #7020 to Phospho-PKC Substrate Motif [(R/K)XpSX(R/K)] MultiMab™ Rabbit mAb mix #6967

$489
96 assays
1 Kit
The PathScan® Phospho-ALK (Tyr1604) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-ALK (Tyr1604), phospho-EML4-ALK or phospho-NPM-ALK fusion proteins with a chemiluminescent readout. Chemiluminescent ELISAs often have a wider dynamic range and higher sensitivity than conventional chromogenic detection. This chemiluminescent ELISA, which is offered in low volume microplates, shows increased signal and sensitivity while using a smaller sample size. A phospho-ALK (Tyr1604) rabbit antibody has been coated onto the microwells. After incubation with cell lysates, only phospho-ALK (Tyr1604) and phospho-ALK fusion proteins are captured by the coated antibody. Following extensive washing, an ALK mouse mAb is added to detect the captured phospho-ALK (Tyr1604) and phospho-ALK fusion proteins. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. Chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of phospho-ALK (Tyr1604) or phospho-ALK fusion proteins.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Anaplastic lymphoma kinase (ALK) is a tyrosine kinase receptor for pleiotrophin (PTN), a growth factor involved in embryonic brain development (1-3). In ALK-expressing cells, PTN induces phosphorylation of both ALK and the downstream effectors IRS-1, Shc, PLCγ, and PI3 kinase (1). ALK was originally discovered as a nucleophosmin (NPM)-ALK fusion protein produced by a translocation (4). Investigators have found that the NPM-ALK fusion protein is a constitutively active, oncogenic tyrosine kinase associated with anaplastic lymphoma (4). Research literature suggests that activation of PLCγ by NPM-ALK may be a crucial step for its mitogenic activity and involved in the pathogenesis of anaplastic lymphomas (5).A distinct ALK oncogenic fusion protein involving ALK and echinoderm microtubule-associated protein like 4 (EML4) has been described in the research literature from a non-small cell lung cancer (NSCLC) cell line, with corresponding fusion transcripts present in some cases of lung adenocarcinoma. The short, amino-terminal region of the microtubule-associated protein EML4 is fused to the kinase domain of ALK (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: NeuroD is a member of the basic helix-loop-helix (bHLH) family of transcription factors. These proteins function by forming heterodimers with E-proteins and binding to the canonical E-box sequence CANNTG (1,2). Neuronal activity results in CaMKII-mediated phosphorylation of NeuroD at Ser336, which is necessary for formation and growth of dendrites (3,4). NeuroD is also phosphorylated at Ser274 though the results are context dependent as phosphorylation by Erk stimulates NeuroD activity in pancreatic β-cells while phosphorylation by GSK-3β inhibits NeuroD in neurons (3). NeuroD is crucially important in both the pancreas and developing nervous system, and plays a large role in the development of the inner ear and mammalian retina (3). Mice lacking NeuroD become severely diabetic and die shortly after birth due to defects in β-cell differentiation (2,3,5,6). The lack of NeuroD in the brain results in severe defects in development (5). Human mutations have been linked to a number of types of diabetes including type I diabetes mellitus and maturity-onset diabetes of the young (1,3).

$40
30 ml
PathScan® Sandwich ELISA Lysis buffer is used to create cell extract for ELISA applications.
$195
1 units
The Magnetic Separation Rack is designed for quick and easy small-scale isolation of immunocomplexes from chromatin immunoprecipitations (ChIP assays) using SimpleChIP® Enzymatic Chromatin IP Kit (Magnetic Beads) #9003 or ChIP-Grade Protein G Magnetic Beads #9006. The rack holds up to six 1.5-2.0 ml tubes and contains three neodymium rare earth permanent magnets. Rare earth magnets are extremely powerful and should be kept away from mechanical/electrical instruments which may be damaged by high magnetic fields.
APPLICATIONS

Application Methods: Chromatin IP, Immunoprecipitation

Dithiothreitol (DTT) from Cell Signaling Technology is offered in a convenient 192.8 mg lyophilized format, allowing for preparation of a fresh stock solution. This DTT reagent contains no detectable DNase or RNase activity and is suitable for use in molecular biology or protein biochemistry applications that require reduction of protein disulfide bonds.SDS-PAGE sample buffers are routinely supplemented with 10-50 mM DTT to cleave protein disulfide bonds. Lower concentrations of DTT are routinely used to stabilize enzymes or other proteins that posses free sulfhydryl groups, which is useful in chromatin immunoprecipitation (ChIP) assays.
$108
250 PCR reactions
500 µl
SimpleChIP® Mouse RPL30 Intron 2 Primers contain a mix of forward and reverse PCR primers that are specific to intron 2 of the mouse RPL30 gene. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®. The RPL30 gene is actively transcribed in all cell types and its promoter is highly enriched for histone modifications associated with active transcription, such as histone H3 Lys4 tri-methylation and general histone acetylation. This gene promoter shows very low levels of histone modifications associated with heterochromatin, such as histone H3 Lys9 and Lys27 tri-methylation.
REACTIVITY
Mouse

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$108
250 PCR reactions
500 µl
SimpleChIP® Human RPL30 Exon 3 Primers contain a mix of forward and reverse PCR primers that are specific to exon 3 of the human RPL30 gene. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®. The RPL30 gene is actively transcribed in all cell types and its promoter is highly enriched for histone modifications associated with active transcription, such as histone H3 Lys4 tri-methylation and general histone acetylation. This gene promoter shows very low levels of histone modifications associated with heterochromatin, such as histone H3 Lys9 or Lys27 tri-methylation.
REACTIVITY
Human

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$29
5 x 1ml
5 ml
EDTA (Ethylenediaminetetraacetic acid) is a common laboratory chelating agent of divalent cations, such as Ca2+ and Mg2+. Ultrapure 0.5 M EDTA, pH 8.0 from Cell Signaling Technology contains no detectable DNase, RNase, or protease activity. The convenient 1 ml vials reduce the likelihood of contamination that can occur with larger volume containers. It is suitable for use in molecular biology or protein biochemistry applications that require the chelation of divalent metal cations.This product is used in our SimpleChip® chromatin immunoprecipitation (ChIP) assays to stop the metal-dependant enzymatic digestion of cross-linked DNA by micrococcal nuclease once the reaction is complete. It can be added to cell lysis buffers for use as a metalloprotease inhibitor. Working concentrations are typically 1-5 mM in this application.
$58
50 ml
$191
250 ml
TMB Substrate used is ready to use for ELISA detection. Reaction between the substrate and immobilized horseradish peroxidase (HRP) conjugated secondary antibodies in the ELISA wells produces a blue colored solution. Color intensity and development time will vary depending on assay sensitivity and conditions. After reaching the desired color intensity, the reaction is terminated by addition of an acidic STOP solution which changes the solution color from blue to yellow. While the results will remain stable for one hour following termination, the plate should be analyzed promptly on a microwell reader at 450 nm. TMB is light sensitive and is therefore packaged in amber bottles to protect the solution from direct sunlight. Recommended storage temperature is 4ºC.
REACTIVITY
All Species Expected
$64
5 ml each
$205
25 ml each
LumiGLO®* chemiluminescent substrate is a luminol-based system designed for use with our Phototope®-HRP detection assays utilizing peroxidase-labeled antibodies immobilized on membranes. In the presence of hydrogen peroxide, horseradish peroxidase (HRP) converts luminol to an excited intermediate dianion. This dianion emits light on return to its ground state. Light emission is maximal immediately after exposure of the substrate to HRP and continues for 0.5-1 hour. Light can be captured on X-ray film, typically by exposure for a few seconds. Maximum sensitivity can be obtained by longer exposure. *Avoid repeated exposure to skin (see enclosed Material Safety Data Sheet or refer to our website for further information).
APPLICATIONS

Application Methods: Western Blotting

Background: Chemiluminescence systems have emerged as the best all-around method for western blot detection. They eliminate the hazards associated with radioactive materials and toxic chromogenic substrates. The speed and sensitivity of these methods are unequalled by traditional alternatives, and because results are generated on film, it is possible to record and store data permanently. Blots detected with chemiluminescent methods are easily stripped for subsequent reprobing with additional antibodies. HRP-conjugated secondary antibodies are utilized in conjunction with specific chemiluminescent substrates to generate the light signal. HRP conjugates have a very high turnover rate, yielding good sensitivity with short reaction times.

$64
2 x 25 ml
50 ml
$211
10 x 25 ml
250 ml
STOP Solution is a proprietary solution used to terminate the peroxidase/TMB reaction for ELISA applications. The TMB substrate reacts with immobilized horseradish peroxidase (HRP) conjugated secondary antibodies to produce a blue solution. Color intensity is an indication of analyte level. After attaining the desired intensity, the reaction is terminated by addition of STOP Solution. Upon addition of STOP Solution the color turns from blue to yellow. Absorbance at 450 nm can be read immediately, and the reaction is stable for one hour.
REACTIVITY
All Species Expected
$108
250 PCR reactions
500 µl
SimpleChIP® Human Timeless Intron 1 Primers contain a mix of forward and reverse PCR primers that are specific to intron 1 of the human Timeless gene. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®. Timeless was discovered in Drosophila where it was found to play a role in circadian rhythms. In humans, the Timeless protein exhibits cell cycle checkpoint activity and maintains genomic stability during DNA replication.
REACTIVITY
Human

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$262
3 nmol
300 µl
SignalSilence® ULK1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit ULK1 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: Two related serine/threonine kinases, UNC-51-like kinase 1 and 2 (ULK1, ULK2), were discovered as mammalian homologs of the C. elegans gene UNC-51 in which mutants exhibited abnormal axonal extension and growth (1-4). Both proteins are widely expressed and contain an amino-terminal kinase domain followed by a central proline/serine rich domain and a highly conserved carboxy-terminal domain. The roles of ULK1 and ULK2 in axon growth have been linked to studies showing that the kinases are localized to neuronal growth cones and are involved in endocytosis of critical growth factors, such as NGF (5). Yeast two-hybrid studies found ULK1/2 associated with modulators of the endocytic pathway, SynGAP and syntenin (6). Structural similarity of ULK1/2 has also been recognized with the yeast autophagy protein Atg1/Apg1 (7). Knockdown experiments using siRNA demonstrated that ULK1 is essential for autophagy (8), a catabolic process for the degradation of bulk cytoplasmic contents (9,10). It appears that Atg1/ULK1 can act as a convergence point for multiple signals that control autophagy (11), and can bind to several autophagy-related (Atg) proteins, regulating phosphorylation states and protein trafficking (12-16).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination is an important posttranslational modification that regulates protein function and fate (1). Ubiquitin (Ub) can be conjugated to target proteins in either monomeric or polymeric forms. There are several different lysine residues within Ub that can be used as conjugation sites for poly-Ub chain formation. Different poly-Ub linkages mediate different functions of the target protein ranging from alterations in protein function to degradation (2). UBE2N/Ubc13 is a ubiquitin-E2-conjugating enzyme that catalyzes K63-linked poly-Ub chain formation (1,2). UBE2N forms a heterodimer with MMS2 or Uev1A to exert its E2 ligase function. The UBE2N/MMS2 and UBE2N/Uev1A heterodimers catalyze different modes of target protein ubiquitination to mediate various signaling pathways (3-5) including: DNA damage and recombination, p53 and check point control, the cell cycle (6-10), immunoreceptor signaling (11,12), and endocytosis (13). Most recently, UBE2N was shown to play an important role in inflammatory signaling by promoting K63-linked ubiquitination and activation of IKK downstream of the IL-1β receptor (14). Furthermore, interaction of UBE2N with the Triad1 E3 protein-ubiquitin ligase was shown to play an important role in myelopoiesis (15).

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

Application Methods: Western Blotting

Background: Damaged DNA-Binding Protein (DDB) consists of a 127 kDa subunit (DDB-1) and a 48 kDa subunit (DDB-2) that contribute to the formation of the UV-damaged DNA-binding protein complex (UV-DDB) (1-3). In conjunction with CUL4A and ROC-1, the UV-DDB complex forms an E3 ubiquitin ligase that recognizes a broad spectrum of DNA lesions such as cyclobutane pyrimidine dimers, 6-4 photoproducts, apurinic sites and short mismatches. The complex polyubiquitinates components of the nucleotide excision repair pathway (4-6). Loss of DDB activity has been identified in a subset of xeroderma pigmentosum complementation group E (XP-E) patients and has been linked to the deficient repair of cyclobutane pyrimidine dimers in cells derived from these patients (7-10).

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

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

Background: The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The receptor for advanced glycation end products (RAGE) is member of the immunoglobulin (Ig) superfamily. It can be expressed as full-length, membrane-bound RAGE isoform 1 or as a secreted sRAGE protein that lacks a transmembrane domain (1). RAGE is detected during early developmental stages and in the lung under normal physiological conditions (2) and is upregulated at sites of inflammation (3). Advanced glycation end products (AGEs) and a variety of other ligands interact with this receptor (1). Ligand binding activates full-length RAGE and initiates downstream signaling pathways that include activation of NF-κB, which leads to production of pro-inflammatory cytokines and inflammation (4). Activation of these pathways has been implicated in various disease states including Alzheimer disease, diabetes, arthritis, and atherosclerosis (4). Soluble RAGE can competitively bind RAGE ligands in the extracellular environment, which prevents ligand interaction with full-length RAGE at the cell surface (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-NDRG1 (Thr346) (D98G11) XP® Rabbit mAb #5482.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

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.

$131
1 ml
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Anti-rabbit IgG F(ab') 2 Fragment (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of antibodies raised in rabbit.
APPLICATIONS

Application Methods: Immunoprecipitation

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Mastermind-like (MAML) family of proteins are homologs of Drosophila Mastermind. The family is composed of three members in mammals: MAML1, MAML2, and MAML3 (1,2). MAML proteins form complexes with the intracellular domain of Notch (ICN) and the transcription factor CSL (RBP-Jκ) to regulate Notch target gene expression (3-5). MAML1 also interacts with myocyte enhancer factor 2C (MEF2C) to regulate myogenesis (6). MAML2 is frequently found to be fused with Mucoepidermoid carcinoma translocated gene 1 (MECT1, also know as WAMTP1 or TORC1) in patients with mucoepidermoid carcinomas and Warthin's tumors (7).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cleaved PARP (Asp214) (D64E10) XP® Rabbit mAb #5625.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The human checkpoint protein Rad17 and its fission and budding yeast orthologues (Schizosaccharomyces pombe Rad17 and Saccharomyces cerevisiae Rad24, respectively) are involved in the activation of checkpoint signals in response to DNA damage or disruption of DNA synthesis (1-4). Treatment of human cells with genotoxic agents induces ATM/ATR-dependent phosphorylation of Rad17 at Ser635 and Ser645. Rad17 phosphorylation is a critical early event during checkpoint signaling in DNA-damaged cells (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: BMPR2 is a type II serine/threonine receptor kinase that binds to an array of secreted bone morphogenetic proteins (BMPs). BMPs belong to the superfamily of TGF-β ligands that modulate gastrulation, neurogenesis, chondrogenesis, interdigital cell death, and bone morphogenesis (1-5). In contrast to the TGF-β type II receptor, BMPR2 contains an extended carboxyl-terminal region that interacts with multiple signaling molecules to modulate the responsiveness of target genes to BMPs (6,7). BMP signaling requires oligomerization of both type I and type II receptors to elicit a functional response of target genes. BMP binding to type I and II receptors induces Smad1/5/8 phosphorylation which is required for the activation of target genes (7). In vitro and in vivo evidence suggests that defects in BMPR2 may contribute to pulmonary hypertension, inflammation, and endothelial injury (8,9).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: TACE (TNF-α converting enzyme), also known as ADAM17, is a transmembrane metalloprotease that plays a key role in the cleavage of a number cell surface molecules in a process known as “shedding". TACE is abundantly expressed in many adult tissues, but in fetal development expression is differentially regulated (1). An important substrate of TACE is pro-TNF-α (1). Increased expression of TACE is associated with several pathological conditions including osteoarthritis and rheumatoid arthritis, where the pro-inflammatory effects of increased TNF-α contribute to disease pathogenesis (2,3). Regulation of other important molecules by TACE such as EGFR and Notch has recently been documented. TACE is responsible for the shedding of EGFR ligands such as amphiregulin and TNF-α. Some tumors have hyperactivated EGFR due to upregulated TNF-α production and upregulated TACE, making TACE a potential target for drug development (4). TACE activates Notch in a ligand-independent manner and has been shown to play a role in the development of the Drosophila nervous system (5). TACE has also been proposed to act as α-secretase for amyloid precursor protein (APP) (6), and to be involved in the renewal and proliferation of neural stem cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: PAR2 (F2RL1) belongs to the PAR (Protease-activated Receptor) family of G protein-coupled receptors. These membrane receptors are activated through N-terminal cleavage of the receptor by a serine protease such as thrombin, trypsin, or matrix metalloproteinases (1,2). This cleavage exposes the ‘tethered-ligand’ fragment of the receptor, which binds to a second extracellular loop of the receptor and leads to receptor activation. PAR2 is specifically activated by trypsin or trypsin-like proteases. Activated PAR2 stimulates phosphoinositide hydrolysis and calcium mobilization, interacts with β-arrestin, and eventually leads to ERK activation (3). PAR2 expression and activation are mainly associated with inflammatory diseases (3), but may also play a role in cancer development (4,5).

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

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

Background: The Rab8 GTPase is a member of the Ras superfamily that functions in protein transport and membrane restructuring (1). Studies show that Rab8 is localized to the trans Golgi network (TGN), basolateral membrane, and vesicular structures where it helps regulate target protein transport between TGN and the basolateral membrane (1-3). Overexpression studies and mutation analysis of Rab8 and its associated Rab8GEF indicate additional roles in actin and microtubule remodeling during polarized membrane transport and membrane protrusion formation (4-6). Rab8 associates with myosin Vb and is required for translocation of GLUT4 following insulin stimulation in muscle (7,8). Control of target protein vesicle transport by Rab8 also regulates MT1-MMP activity during extracellular matrix formation and JRAB/MICAL-L2 at tight junction formation (9,10).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: Although protein kinase C (PKC) family members are involved in a number of signal transduction processes including secretion, gene expression, proliferation, and muscle contraction, many PKC substrates continue to be unidentified (1,2). Isozymes of PKC are subdivided into conventional PKCs (cPKC), novel PKCs (nPKC), and atypical PKCs (aPKC). PKCα, βI, βII, and γ isoforms belong to the cPKC group (1). When activated, cPKC isozymes phosphorylate substrates containing Ser or Thr, with Arg or Lys at the -3, -2, and +2 positions, and a hydrophobic amino acid at position +1 (1-3).