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Product listing: PathScan® Phospho-FLT3 (panTyr) Sandwich ELISA Kit, UniProt ID P36888 #7761 to Troponin I (D6F8) Rabbit mAb, UniProt ID P19429 #13083

$489
96 assays
1 Kit
CST's PathScan® Phospho-FLT3 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated FLT3 protein. A FLT3 rabbit antibody has been coated on the microwells. After incubation with cell lysates, FLT3 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse detection antibody is added to detect captured tyrosine-phosphorylated FLT3 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 FLT3 protein phosphorylated on tyrosine.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: FMS-related tyrosine kinase 3 (FLT3, also called Flk2), is a member of the type III receptor tyrosine kinase family, which includes c-Kit, PDGFR and M-CSF receptors. FLT3 is expressed on early hematopoietic progenitor cells and supports growth and differentiation within the hematopoietic system (1,2). FLT3 is activated after binding with its ligand FL, which results in a cascade of tyrosine autophosphorylation and tyrosine phosphorylation of downstream targets (3). The p85 subunit of PI3 kinase, SHP2, GRB2 and Shc are associated with FLT3 after FL stimulation (4-6). Tyr589/591 is located in the juxtamembrane region of FLT3 and may play an important role in regulation of FLT3 tyrosine kinase activity. Somatic mutations of FLT3 consisting of internal tandem duplications (ITDs) occur in 20% of patients with acute myeloid leukemia (7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Pan-Actin (D18C11) Rabbit mAb #8456.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility (1). α-cardiac and α-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, α- and γ-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate the contractile potential of muscle cells (1). Actin exists mainly as a fibrous polymer, F-actin. In response to cytoskeletal reorganizing signals during processes such as cytokinesis, endocytosis, or stress, cofilin promotes fragmentation and depolymerization of F-actin, resulting in an increase in the monomeric globular form, G-actin (2). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (2). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (3). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cas9 (7A9-3A3) Mouse mAb #14697.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the Streptococcus pyogenes CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA) followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).

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

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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).

$115
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye under optimal conditions and tested in-house for direct flow cytometric analysis of human cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

Molecular Weight:428.4 g/mol

Background: Wortmannin is a very potent, specific and direct inhibitor of PI3 kinase, originally derived from fungus (1,2). The inhibition is irreversible and noncompetitive. Wortmannin does not inhibit PI4 kinase, protein kinase C or protein tyrosine kinase (3).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, 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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Bcl-2 (124) Mouse mAb #15071.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Bcl-2 exerts a survival function in response to a wide range of apoptotic stimuli through inhibition of mitochondrial cytochrome c release (1). It has been implicated in modulating mitochondrial calcium homeostasis and proton flux (2). Several phosphorylation sites have been identified within Bcl-2 including Thr56, Ser70, Thr74, and Ser87 (3). It has been suggested that these phosphorylation sites may be targets of the ASK1/MKK7/JNK1 pathway and that phosphorylation of Bcl-2 may be a marker for mitotic events (4,5). Mutation of Bcl-2 at Thr56 or Ser87 inhibits its anti-apoptotic activity during glucocorticoid-induced apoptosis of T lymphocytes (6). Interleukin-3 and JNK-induced Bcl-2 phosphorylation at Ser70 may be required for its enhanced anti-apoptotic functions (7).

The Phospho-IKKalpha/beta (Ser176/180) Antibody Sampler Kit contains reagents to examine protein levels of IKKalpha when phosphorylated at Ser176/180 and IKKbeta when phosphorylated at Ser177/181. The kit contains primary and secondary antibodies to perform two Western blots with each antibody.

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: GTPase immune-associated proteins (GIMAP), also known as immune-associated nucleotide-binding (IAN) proteins, are evolutionarily conserved GTP-binding proteins involved in lymphocyte development, inflammation, and autoimmune diseases (reviewed in 1,2). Human GTPase IMAP family member 5 (GIMAP5, hIan5) is the homolog of the rat Ian4 protein that is mutated in severe cases of T-cell lymphopenia and insulin-dependent diabetes in Biobreeding diabetes-prone (BB-DP) rats (3,4). GIMAP5 protein is preferentially expressed in CD4- and CD8-positive T-cells as well as B-cell lymphomas (4). Research studies using GIMAP5-deficient mice show that GIMAP5 protein is critical for survival of peripheral T-cells, hematopoietic stem cells, and progenitor cells (5-7). Additional studies indicate that GIMAP5 deficiency leads to a loss of immunological tolerance (8). Polymorphisms in the human GIMAP5 gene are associated with systemic lupus erythematosus and type I diabetes (9-11). Potential mechanisms for GIMAP5 control of cell survival include regulation of Bcl-2 family proteins, mitochondrial integrity, lysosomal function, and calcium regulation (7, 12-15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: TFII-I (also known as SPIN and BAP-135) is a mutifunctional transcription factor that facilitates basal transcriptional machinery assembly at the core promotor region, as well as the assembly of the transcriptional activator complex at upstream regulatory sites (1). Four isoforms of TFII-I (alpha, beta, gamma, and delta) form homo- or heteromeric complexes, which may perform different functions on different promoters (1). In B cells, cross-linking of BCR (B cell receptors) leads to TFII-I phosphorylation at Tyr248 by Btk (2). This phosphorylation disrupts the association of Btk and TFII-I and enhances TFII-I transcriptional activity and nuclear localization (2). In nonlymphoid cells, TFII-I is phosphorylated at Tyr248 by Src dependent kinase or JAK2 (3,4). PKG (cGMP-dependent kinase) interacts with and phosphorylates TFII-I at Ser371 and 743, which also promotes TFII-I transcription activity (5). TFII-I activity is also modulated by HDAC3 (Histone Deacetylase 3) through a physical interaction between the two proteins (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Regulation of actin dynamics at the leading edge of the cell drives cell adhesion, migration, and invasion. These processes are crucial for normal development, immune cell function, angiogenesis and cell division, and are dysregulated in diseases such as metastatic cancer (1, 2).Lamellipodin (Lpd) is a member of the Mig-10/RIAM/lamellipodin (MRL) family of adaptor proteins. Lamellipodin regulates the formation of lamellipodia at the leading edge through its interaction with and recruitment of actin-modulating proteins such as Ena/VASP (3) and the Scar/WAVE complex (4). Lamellipodin and Mena cooperate with endophilin to regulate EGFR endocytosis (5). MRL proteins can also form complexes with talin and activated integrins, guiding the formation of cell protrusions and the direction of cell migration (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). In addition to p53, mammalian cells contain two p53 family members, p63 and p73, which are similar to p53 in both structure and function (2). While p63 can induce p53-responsive genes and apoptosis, mutation of p63 rarely results in tumors (2). Research investigators frequently observe amplification of the p63 gene in squamous cell carcinomas of the lung, head and neck (2,3). The p63 gene contains an alternative transcription initiation site that yields a truncated ΔNp63 lacking the transactivation domain, and alternative splicing at the carboxy-terminus yields the α, β, and γ isoforms (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Endonuclease G (EndoG) is a nuclear-encoded mitochondrial nuclease that has been reported to function in apoptosis, DNA recombination and cell proliferation (1-5). EndoG is expressed as a precursor protein containing an amino-terminal mitochondrial targeting sequence which is removed when the protein is imported into the mitochondria (1). During apoptosis EndoG is released from the mitochondria, translocates to the nucleus and cooperates with other nucleases to trigger DNA fragmentation associated with the apoptotic process (3,6,7).

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

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

Background: Rab7 and Rab9 are members of the Ras superfamily of small Rab GTPases (1). Both proteins are located in late endosomes, but exert different functions. Rab7 associates with the RIPL effector protein to control membrane trafficking from early to late endosome and to lysosomes (2,3). Rab7 also helps to regulate growth receptor endocytic trafficking and degradation (3,4), and maturation of phagosome and autophagic vacuoles (4-6). Rab9 interacts with its effector proteins p40 and TIP47 (7,8) to promote the MPR (mannose 6-phosphate receptor)-associated lysosomal enzyme transport between late endosomes and the trans Golgi network (9,10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$489
96 assays
1 Kit
The PathScan® Phospho-TrkB (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects transfected levels of TrkB when phosphorylated on tyrosine residues. A TrkB mouse antibody has been coated onto the microwells. After incubation with cell lysates, TrkB (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a biotinylated phospho-tyrosine detection antibody is added to detect tyrosine phosphorylation of the captured TrkB protein. HRP-linked streptavidin 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 TrkB phosphorylated on tyrosines.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).

The Mutant Ras Antibody Sampler Kit provides an economical means of detecting common mutation in the Ras protein. The kit contains enough primary and secondary antibodies to perform at least two western blot experiments.

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6). Additional oncogenic mutations of Ras have been observed at varying frequencies at codons 12, 13, and 61. The Gly12 to Val12 (G12V) mutation has been detected in a number of different cancers, including colorectal and thyroid cancer (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Bik/Nbk (Bcl-2-interacting killer/natural born killer) is a potent pro-apoptotic protein belonging to a group of Bcl-2 family members that includes Bad, Bid, Bim, Hrk, and Noxa, containing a BH3 domain but lacking other conserved domains, BH1 or BH2 (1,2). Functionally, Bik is able to bind to and antagonize anti-apoptotic Bcl-2 family members including Bcl-2, Bcl-xL, and viral homologs E1B-19K and EBV-BHFR1. The BH3 domain of Bik is essential for its apoptotic activity and interaction with survival proteins (3). Phosphorylation of Bik is correlated with an increase in its pro-apoptotic activity (4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: SET7/SET9 is a member of the SET domain-containing family, and can specifically methylate Lys4 on histone H3 (1). Like most other lysine-directed histone methyltransferases, it contains a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste and Trithorax proteins. 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). Methylation of histone H3 Lys4 enhances transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (4,5). In addition, methylation of lysine 4 blocks transcriptional repression by inhibiting the binding of the NURD histone deacetylation complex to the amino-terminal tail of histone H3 and interfering with SUV39H1-mediated methylation of histone H3 Lys9 (1). SET7/SET9 is highly active on free histone H3, but only very weakly methylates H3 within nucleosomes (1). Besides histones, SET7/SET9 also methylates Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein (6,7). Methylation of TAF10 stimulates transcription in a promoter-specific manner by increasing the affinity of TAF10 for RNA polymerase II, which may potentiate pre-initiation complex formation (6). Methylation of p53 at Lys372 increases protein stability and leads to upregulation of target genes such as p21. Thus the loss of SET7/SET9 may represent another mechanism for the inactivation of p53 in human cancers (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: FTO (fat mass and obesity-associated protein) is the first obesity gene product identified by genome-wide association studies and it is associated with the largest effect size for this class of proteins (1-4). Multiple single-nucleotide polymorphisms (SNPs) in the first intron of the FTO gene have been associated with increased body weight and obesity. Further studies reported that FTO risk alleles were associated with an increase in energy intake, a reduction of activity, and possibly an increased daily fat intake (4).FTO is a DNA and RNA demethylase that catalyzes the oxidative demethylation of thymidine and uracil. Among its targets is an mRNA subset involved in regulation of learning, reward behavior, motor functions, and feeding (5). Loss of the FTO gene in mice leads to postnatal growth retardation and a significant reduction in adipose tissue. Mice deficient in the FTO gene have lean body mass due to increased energy expenditure and systemic activation of sympathetic neurons, while overexpression of FTO in mice leads to increased food intake and results in obesity. These results demonstrate that FTO is functionally involved in energy homeostasis (6-8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: 4F2hc is a transmembrane protein that belongs to the solute carrier family. 4F2hc forms heterodimeric complexes with various amino acid transporters such as LAT1 and LAT2 and regulates uptake of amino acids (1-5). 4F2hc is one of the earliest expressed antigens on the surface of activated human lymphocytes (6), hence it is also named CD98. 4F2hc is expressed in all cell types with the exception of platelets, and is expressed at highest levels in the tubules of the kidney and the gastrointestinal tract (7,8). It is localized at the plasma membrane when associated with LAT1 or LAT2 (9) and at the apical membrane of placenta (10). Research studies have shown that 4F2hc is highly expressed in various tumors including glioma (11), ovarian cancer (12), and astrocytomas (13), and it has been implicated in tumor progression and correlated with poor outcome in patients with pulmonary neuroendocrine tumors (14). 4F2hc is also involved in integrin trafficking through association with β1 and β4 integrins, and regulates keratinocyte adhesion and differentiation (15).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated E-Cadherin (4A2) Mouse mAb #14472.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Chk1 kinase acts downstream of ATM/ATR kinase and plays an important role in DNA damage checkpoint control, embryonic development, and tumor suppression (1). Activation of Chk1 involves phosphorylation at Ser317 and Ser345 by ATM/ATR, followed by autophosphorylation of Ser296. Activation occurs in response to blocked DNA replication and certain forms of genotoxic stress (2). While phosphorylation at Ser345 serves to localize Chk1 to the nucleus following checkpoint activation (3), phosphorylation at Ser317 along with site-specific phosphorylation of PTEN allows for re-entry into the cell cycle following stalled DNA replication (4). Chk1 exerts its checkpoint mechanism on the cell cycle, in part, by regulating the cdc25 family of phosphatases. Chk1 phosphorylation of cdc25A targets it for proteolysis and inhibits its activity through 14-3-3 binding (5). Activated Chk1 can inactivate cdc25C via phosphorylation at Ser216, blocking the activation of cdc2 and transition into mitosis (6). Centrosomal Chk1 has been shown to phosphorylate cdc25B and inhibit its activation of CDK1-cyclin B1, thereby abrogating mitotic spindle formation and chromatin condensation (7). Furthermore, Chk1 plays a role in spindle checkpoint function through regulation of aurora B and BubR1 (8). Research studies have implicated Chk1 as a drug target for cancer therapy as its inhibition leads to cell death in many cancer cell lines (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).