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Product listing: TLE1/2/3/4 Antibody, UniProt ID Q04724 #4681 to β-Amyloid Antibody Sampler Kit, UniProt ID P05067 #85314

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Transducin-like enhancer of split proteins (TLE1, TLE2, TLE3, TLE4, and TLE6) are mammalian homologs of Drosophila Groucho (1). TLEs contain several WD-repeats implicated in protein-protein interaction (2,3). TLEs are transcriptional co-repressors that bind to many transcription factors such as LEF1, Runx1, Oct-1, hepatocyte nuclear factor 3-β as well as histone H3 (4-7). TLEs are differentially expressed during animal development and may have overlapping as well as distinct functions (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzymes (DUB) action (1,2). There are five DUB subfamilies including the USP, UCH, OTU, MJD and JAMM enzymes. USP28 is an important member of the USP subfamily (3). USP28 can bind to and deubiquinate several target proteins in DNA-damage pathway, resulting in their stability, including p53BP1 and Chk2 (4). USP28 also plays an important role in Myc related signaling by binding through FBW7α to Myc . It catalyzes the deubiquitinylation of Myc, thereby promoting its stabilization and contributing to tumor-cell growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Maspin (SERPINB5) was discovered as a mammary tumor suppressor that is expressed in normal mammary epithelium but lost in most breast cancer cell lines (1). While maspin is related to the serpin family of serine protease inhibitors, it may not function as a protease inhibitor (2). It plays an essential role in embryonic development through critical roles in cell adhesion (3). While the precise mechanism of maspin signaling is unclear (4), the tumor suppressing activity of maspin has been attributed to its ability to inhibit cell invasion/metastasis (5,6) and angiogenesis (7), while promoting apoptosis (8). Nuclear translocation of active IKKα has been shown to repress maspin transcription and promote prostate cancer metastasis (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA double-strand breaks (DSBs) are potentially hazardous lesions that can be induced by ionizing radiation (IR), radiomimetic chemicals, or DNA replication inhibitors. Cells sense and repair DSBs via two distinct but partly overlapping signaling pathways, nonhomologous end joining (NHEJ) and homologous recombination (HR). Defects in both pathways have been associated with human disease, including cancer (1). The DNA repair and recombination protein RAD54-like (Rad54, RAD54L) is a Swi2/Snf2 family DNA helicase that is involved in homologous recombination DNA repair. Rad54 is a double-stranded DNA-dependent ATPase that translocates in a processive manner along double-stranded DNA. The Rad54 helicase interacts with the Rad51 recombinase to regulate its DNA binding and strand exchange activities during homologous recombination (2-4). Mutations in the corresponding RAD54L gene are associated with multiple forms of human cancer, including non-Hodgkin's lymphoma, breast cancer, and parathyroid adenoma (5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Interferon-induced transmembrane protein (IFITM) family members are composed of short amino- and carboxy-termini, two transmembrane domains, and a cytoplasmic domain (1). There are four family members in humans: IFITM1, IFITM2, IFITM3, and IFITM5 (2,3). Mice have two additional family members, IFITM6 and IFITM7 (2,3). Basal expression of IFITM proteins is observed in some cells and expression can also be induced by type I and type II interferons (4-6). The primary function of IFITM family proteins appears to be viral restriction, as IFITM proteins inhibit cytosolic entry of viruses by preventing fusion of viral and host membranes (7,8). The mechanism by which IFITM proteins inhibit fusion is unclear. Although IFITM proteins are present on both the plasma membrane and intracellular membranes, they most effectively restrict viral fusion in late endosomes and lysosomes (8,9). In addition, different family members exhibit specific viral preferences (9). For example, IFITM3 is most effective at restricting influenza A infection, while IFITM1 is more successful in controlling filoviruses and SARS (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The Drosophila piwi gene was identified as being required for the self-renewal of germ-line stem cells (1). Piwi homologs are well conserved among various species including Arabidopsis, C. elegans, and human (1). Miwi and Mili proteins are both mouse homologs of Piwi and contain a C-terminal Piwi domain (2). Miwi and Mili bind to Piwi-interacting RNAs (piRNAs) in male germ cells and are essential for spermatogenesis in mouse (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cathepsin B (CSTB), part of the papain family of proteases, is a widely expressed lysosomal cysteine endopeptidase (1,2). Cathepsin B is produced from a larger precursor form, pro-cathepsin B, which runs at approximately 44 kDa on SDS-PAGE, and is proteolytically processed and glycosylated to form a mature two-chain protein containing a heavy chain (running at 27 and 24 kDa) and a light chain (5 kDa). High levels of cathepsin B are found in macrophages and osteoclasts, as well as various types of cancer cells, including lung, colon, prostate, breast, and stomach. In addition, expression of cathepsin B has been associated with multiple sclerosis (3), rheumatoid arthritis (4), and pancreatitis (5). While generally localized to lysosomes, in cancer alterations can lead to its secretion (6). Its role in tumor progression is thought to involve promotion of basement membrane degradation, invasion and metastasis (7,8). Expression can correlate with poor prognosis for a variety of forms of cancer (9-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cathepsin B (CSTB), part of the papain family of proteases, is a widely expressed lysosomal cysteine endopeptidase (1,2). Cathepsin B is produced from a larger precursor form, pro-cathepsin B, which runs at approximately 44 kDa on SDS-PAGE, and is proteolytically processed and glycosylated to form a mature two-chain protein containing a heavy chain (running at 27 and 24 kDa) and a light chain (5 kDa). High levels of cathepsin B are found in macrophages and osteoclasts, as well as various types of cancer cells, including lung, colon, prostate, breast, and stomach. In addition, expression of cathepsin B has been associated with multiple sclerosis (3), rheumatoid arthritis (4), and pancreatitis (5). While generally localized to lysosomes, in cancer alterations can lead to its secretion (6). Its role in tumor progression is thought to involve promotion of basement membrane degradation, invasion and metastasis (7,8). Expression can correlate with poor prognosis for a variety of forms of cancer (9-13).

$108
250 PCR reactions
500 µl
SimpleChIP® Human GAPDH Exon 1 Primers contain a mix of forward and reverse PCR primers that are specific to exon 1 of the human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) 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 GAPDH gene is actively transcribed in all cell types and the exon 1 region is highly enriched for histone modifications associated with active transcription, such as histone H3 Lys4 tri-methylation and general histone acetylation. The exon 1 region 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.

$115
100 µl
The extract is prepared from whole heart tissue of adult mice, and is intended for use as a positive control in western blotting applications. The protein concentration is 2 mg/ml.The extract was prepared from whole tissue by homogenization in 1X RIPA buffer (#9806, 10X) (20 mM Tris-HCl pH 7.5, 150 mM NaCl, 1% NP-40, 1% sodium deoxycholate, 1 mM sodium EDTA, 1 mM EGTA, 1 μg/ml leupeptin, 1 mM β-glycerophosphate, 1 mM sodium orthovanadate, 2.5 mM sodium pyrophosphate), 1 mM PMSF (#8553, 34.84 mg), 1X Protease/Phosphatase Inhibitor Cocktail (#5872, 100X).The extract was subsequently sonicated and insoluble cell debris removed by centrifugation. The extract was then boiled for 5 min in 1X SDS sample buffer + DTT (#7722, Blue Loading Buffer Pack) (62.5 mM Tris-HCl pH 6.8, 10% glycerol, 2% SDS, 0.01% bromophenol blue, 42 mM DTT) to denature the proteins.
APPLICATIONS

Application Methods: Western Blotting

$109
200 ml
10X Wash Buffer, Phosphate Buffered Saline (PBS) is for use in immunfluorescence and flow cytometry assays. Cell Signaling Technology recommends using this wash buffer according to our protocols for IF and FLOW approved antibodies to ensure accurate and reproducible results.1X Wash Buffer contains 137 mM NaCl, 2.6 mM KCl, 10 mM Na2HPO4, 1.76 mM KH2PO4, 0.005% sodium azide, pH 8.0. The product is free of calcium and magnesium salts.
APPLICATIONS

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

$114
10 blots
Nonphosphorylated Rb-C Fusion Protein (5 µg/ml): Rb-C is expressed as a recombinant fusion protein of Rb residues 701–928 and maltose binding protein serves as a negative control. Supplied in SDS Sample Buffer.Phosphorylated Rb-C Fusion Protein (5 µg/ml): Rb-C is expressed as a recombinant fusion protein of Rb residues 701–928 and maltose binding protein prepared by in vitro kinase reaction with cdc2 serves as a positive control. Supplied in SDS Sample Buffer.Note: This truncated Rb recombinant protein is not recognized by Phospho-Rb (Ser608) Antibody #2181 or Rb (D20) Rabbit mAb #9313.
APPLICATIONS

Application Methods: Western Blotting

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

Molecular Weight:807.89 g/mol

Background: Docetaxel belongs to the taxane family of antitumor and antileukemic agents (1). A microtubule-stabilizing agent, docetaxel acts as an inhibitor of cellular functions that require microtubule dynamics including cell division, and is now in use as a treatment for breast, prostate and lung cancer (2).

Molecular Weight:315.76 g/mol

Background: Tyrphostin AG 1478 is a tyrosine kinase inhibitor specifically selective to EGFR (ErbB1), with an IC50 of about 3 nM in vitro (1,2). Treatment of cell with 50-150 nM of AG 1478 can substantially block EGFR activiation in vivo (3). In addition to EGFR, AG 1478 also inhibits ErbB4 activation induced by radiation in cancer cells (4). Testing of AG 1478 alone or in combination with other treatments to assess anti-tumor and anti-fibrotic effectiveness has yielded promising results (5-8).

$489
96 assays
1 Kit
CST's PathScan® Total TrkA Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects transfected levels of total TrkA protein. A TrkA Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-TrkA proteins are captured by the coated antibody. Following extensive washing, a TrkA Rabbit Antibody is added to detect both the captured phospho- and nonphospho-TrkA protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total TrkA protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The family of Trk receptor tyrosine kinases consists of TrkA, TrkB, and TrkC. While the sequence of these family members is highly conserved, they are activated by different neurotrophins: TrkA by NGF, TrkB by BDNF or NT4, and TrkC by NT3 (1). Neurotrophin signaling through these receptors regulates a number of physiological processes, such as cell survival, proliferation, neural development, and axon and dendrite growth and patterning (1). In the adult nervous system, the Trk receptors regulate synaptic strength and plasticity. TrkA regulates proliferation and is important for development and maturation of the nervous system (2). Phosphorylation at Tyr490 is required for Shc association and activation of the Ras-MAP kinase cascade (3,4). Residues Tyr674/675 lie within the catalytic domain, and phosphorylation at these sites reflects TrkA kinase activity (3-6). Point mutations, deletions, and chromosomal rearrangements (chimeras) cause ligand-independent receptor dimerization and activation of TrkA (7-10). TrkA is activated in many malignancies including breast, ovarian, prostate, and thyroid carcinomas (8-13). Research studies suggest that expression of TrkA in neuroblastomas may be a good prognostic marker as TrkA signals growth arrest and differentiation of cells originating from the neural crest (10).

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

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).

$489
96 assays
1 Kit
PathScan® Phospho-FGF Receptor 1 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated FGFR1 protein. A FGFR1 Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-FGFR1 proteins are captured by the coated antibody. Following extensive washing, Phospho-Tyrosine Mouse Detection Antibody is added to detect captured tyrosine-phosphorylated FGFR1 proteins. Anti-mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of tyrosine-phosphorylated FGFR1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

The Lysine Methyltransferase Antibody Sampler Kit provides a fast and economical means to evaluate endogenous levels of lysine methyltransferases. The kit contains enough primary antibody to perform two western blot experiments per primary antibody.
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

Background: TBK1 (TANK-binding kinase 1)/NAK (NF-κB activating kinase) is an IκB kinase (IKK)-activating kinase and can activate IKK through direct phosphorylation (1). TBK1 was identified through association with the TRAF binding protein, TANK, and found to function upstream of NIK and IKK in the activation of NF-κB (2). TBK1 induces IκB degradation and NF-κB activity through IKKβ. TBK1 may mediate IKK and NF-κB activation in response to growth factors that stimulate PKCε activity (1). TBK1 plays a pivotal role in the activation of IRF3 in the innate immune response (3).

$489
96 assays
1 Kit
The PathScan® Acetylated Histone H3 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of acetylated lysines on Histone H3. A Histone H3 Antibody has been coated onto the microwells. After incubation with cell lysates, Histone H3 is captured by the coated antibody. Following extensive washing, an Acetylated-Lysine Rabbit mAb is added to detect the acetylated lysines on the Histone H3 protein. Anti-Rabbit IgG, HRP linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of acetylated Histone H3.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).

$489
96 assays
1 Kit
CST's PathScan® Total PDGF Receptor α Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total PDGF receptor α protein. A PDGF receptor α Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, both phospho and nonphospho PDGF receptor α proteins are captured by the coated antibody. Following extensive washing, Biotinylated PDGF Receptor α Rabbit mAb is added to detect both the captured phospho and nonphospho PDGF receptor α protein. HRP-linked Streptavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of total PDGF receptor α protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

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

The UV Induced DNA Damage Response Antibody Sampler Kit offers an economical means of investigating proteins involved in the cellular response to UV-induced DNA damage. The kit contains enough primary and secondary antibody to perform two western blot experiments per primary.
$489
96 assays
1 Kit
The PathScan® Total PD-L1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of PD-L1 protein. A rabbit antibody toward intracellular PD-L1 has been coated onto the microwells. After incubation with cell lysates, PD-L1 protein is captured by the coated antibody. Following extensive washing, a mouse detection antibody toward extracellular PD-L1 is added to detect the captured PD-L1 protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for the developed color is proportional to the quantity of PD-L1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

$489
(96 assays) Low Volume Microplate
1 Kit
The PathScan® Phospho-Stat3 (Tyr705) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-Stat3 (Tyr705) protein 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 smaller sample volume. A Stat3 antibody has been coated on the microwells. After incubation with cell lysates, phospho and nonphospho-Stat3 proteins are captured by the coated antibody. Following extensive washing, a phospho-Stat3 mouse mAb is added to detect the captured phospho-Stat3 (Tyr705) protein. 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-Stat3 (Tyr705) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$489
96 assays
1 Kit
CST's PathScan® Phospho-MEK1 (Ser217/221) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-MEK1 (Ser217/221) protein. MEK1 Mouse mAb has been coated onto the microwells. After incubation with cell lysates, total MEK1 protein (phospho- and nonphospho-) is captured by the coated antibody. Following extensive washing, a Phospho-MEK1/2 Antibody is added to detect the captured phospho-MEK1 protein. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-MEK1 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$489
96 assays
1 Kit
The PathScan® Phospho-Stat3 (Ser727) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Stat3 protein phosphorylated at Ser727. A Stat3 rabbit mAb has been coated onto the microwells. After incubation with cell lysates, Stat3 (phospho or nonphospho) protein is captured by the coated antibody. Following extensive washing, a phospho-Stat3 (Ser727) mouse mAb is added to detect the captured phospho-Stat3 protein. Anti-mouse IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of Stat3 phosphorylated at Ser727.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

The β-Amyloid Antibody Sampler Kit provides an economical means of detecting APP and APP unmodified/modified fragments using total and fragment-specific antibodies. The kit includes enough antibody to perform two western blot experiments with each primary antibody.

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 an amyloid domain, which can be processed and released by 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). Several fragments corresponding to progressive APP processing at alternative cleavage sites have been identified (2). These include Aβ (1-37), Aβ (1-39), Aβ (1-40), and Aβ (1-42) (2). These fragments can also be N-terminally modified to generate pyroglutamate-3 Aβ (pE3-peptide) (3). Fragment-specific and pan-Aβ antibodies are used to detect and examine relative levels of individual Aβ fragments.