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Product listing: Lyn (5G2) Mouse mAb, UniProt ID P07948 #4576 to IDO (D5J4E™) Rabbit mAb (PE Conjugate), UniProt ID P14902 #10312

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Lyn, one of the Src family members, is predominantly expressed in hematopoietic cells (1). Two tyrosine residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family. Autophosphorylation of Tyr396 (equivalent to Tyr416 of Src), located in the catalytic domain, correlates with enzyme activation. Csk-mediated phosphorylation of the carboxy-terminal Tyr507 (equivalent to Tyr527 of Src) inactivates the kinase. Tyrosine phosphorylation and activation of Lyn occurs upon association with cell surface receptors such as the B cell Ag receptor (BCR) and CD40 (2-4). Studies using knockout mice have shown that the net effect of Lyn deficiency is to render B cells hypersensitive to BCR stimulation (5-7), suggesting that the most critical role for Lyn in vivo is in the down-regulation of B cell responses. Lyn is also involved in controlling the migration and development of specific B cell populations (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: ABCG2 (BCRP1/ABCP/MXR) is a member of the ATP-binding cassette transporter family that functions as ATP-dependent transporters for a wide variety of chemical compounds and are associated with drug-resistance in cancer cells (1-6). ABCG2 is a heavily glycosylated transmembrane protein with six transmembrane spanning regions consistent with it functioning as a half-transporter. The ABC family can exist as either full-length transporters or as half-transporters that form functional transporters through homo- or heterodimerization. High expression of ABCG2 was found in placenta as well as cell lines selected for resistance to a number of chemotherapeutic drugs, including mitoxantrone, doxorubicin, topotecan and flavopiridol. In rodents, the highest expression of ABCG2 was found in kidney (8). ABCG2 expression has also been observed in stem cell populations, particularly in hematopoietic and neuronal stem cells and is downregulated with differentiation (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Calpain is a thiol proteinase that is functionally active as a heterodimer composed of a small regulatory subunit and one of at least two large catalytic subunits (calpain 1 or calpain 2). In vitro, calpain 1 (mu-calpain) requires micromolar levels of calcium, while calpain 2 (M-calpain) requires millimolar levels of calcium for activation (1). Calpastatin negatively regulates autoproteolytic cleavage of calpain 1 between Gly27 and Leu28 in a calcium dependent manner (2). In particular, calpastatin binds and inhibits calpain when calcium levels are high and is released when calcium levels go down. Calpastatin contains five domains, a unique N-terminal domain L with no inhibitory effects and four homologous domains (CAST 1-4) that can inhibit heterodimeric calpain 1 and 2 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Dog, Human, Monkey

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

Background: Protein phosphatase 1 (PP1) is a ubiquitous eukaryotic protein serine/threonine phosphatase involved in the regulation of various cell functions. Substrate specificity is determined by the binding of a regulatory subunit to the PP1 catalytic subunit (PP1c). It is estimated that over fifty different regulatory subunits exist (1).The myosin phosphatase holoenzyme is composed of three subunits: PP1c, a targeting/regulatory subunit (MYPT/myosin-binding subunit of myosin phosphatase), and a 20 kDa subunit of unknown function (M20). MYPT binding to PP1cδ alters the conformation of the catalytic cleft and increases enzyme activity and specificity (2). Two MYPT isoforms that are 61% identical have been described. MYPT1 is widely expressed, while MYPT2 expression appears to be exclusive to heart and brain (3). Related family members include MBS85, MYPT3, and TIMAP (4).Myosin phosphatase regulates the interaction of actin and myosin in response to signaling through the small GTPase Rho. Rho activity inhibits myosin phosphatase via Rho-associated kinase (ROCK). Phosphorylation of MYPT1 at Thr696 and Thr853 results in phosphatase inhibition and cytoskeletal reorganization (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Pim proteins (Pim-1, Pim-2 and Pim-3) are oncogene-encoded serine/threonine kinases (1). Pim-1, a serine/threonine kinase highly expressed in hematopoietic cells, plays a critical role in the transduction of mitogenic signals and is rapidly induced by a variety of growth factors and cytokines (1-4). Pim-1 cooperates with c-Myc in lymphoid cell transformation and protects cells from growth factor withdrawal and genotoxic stress-induced apoptosis (5,6). Pim-1 also enhances the transcriptional activity of c-Myb through direct phosphorylation within the c-Myb DNA binding domain as well as phosphorylation of the transcriptional coactivator p100 (7,8). Hypermutations of the Pim-1 gene are found in B-cell diffuse large cell lymphomas (9). Phosphorylation of Pim-1 at Tyr218 by Etk occurs following IL-6 stimulation and correlates with an increase in Pim-1 activity (10). Various Pim substrates have been identified; Bad is phosphorylated by both Pim-1 and Pim-2 at Ser112 and this phosphorylation reverses Bad-induced cell apoptosis (11,12).

$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, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Splicing factor 3b subunit 1 (SF3B1) is an integral component of the U2 small nuclear ribonucleoprotein (U2 snRNP) and plays an important role in the splicing of pre-mRNA that involves the removal of introns and the joining of exons to form mature mRNA (1-3). The assembly and proper recognition of splice sites are driven by sequences at the pre-mRNA intron-exon splice sites. The 5’ splice donor site is recognized by the U1 snRNP complex, while U2 snRNP binds to the 3’ splice site (branch point), ensuring the anchoring of the spliceosome machinery at the splice sites (3,4). Recent whole exome sequencing studies have demonstrated a high incidence of somatic mutations of SF3B1 in patients with various hematological malignancies such as chronic lymphocytic leukemia and myelodysplastic syndromes (2,3,5,6). Misregulation of pre-mRNA splicing arising from mutations of the spliceosome components such as SF3B1 is thought to contribute to changes in the expression patterns of key proteins that are involved in pathways such as cell cycle progression, cell death, and cancer metabolism (2,3).

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

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

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z (2). Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability (2). Several homologous protein complexes, such as SWR-C (S. cerevisiae), TIP60 (D. melanogaster) and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome (3,4,5). This exchange of histone H2A variants changes histone-histone interactions in the nucleosome core and alters an acidic patch on the surface of the nucleosome, resulting in changes in nucleosome stability and binding of non-histone proteins such as HP1α (6,7).

The SHP-2 Antibody Sampler Kit provides an economical means to evaluate levels of SHP-2 protein phosphorylated at the specified sites, as well as total SHP-2 levels. The kit contains enough primary and secondary antibody to perform two western blot experiments per antibody.

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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).

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

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

Background: CDC37 is an important component of the HSP90 chaperone complex (1,2). It was initially identified for its involvement in cell-cycle progression and was later found to have a much broader role as a chaperone for a wide variety of kinases and other proteins (1-3). CDC37 protein has an amino-terminal kinase binding domain followed by a central HSP90 binding domain. It recruits and stabilizes kinases in the HSP90 complex by protecting the newly synthesized kinase peptide chain from degradation and promoting the next step of protein maturation (4,5). CDC37 also suppresses the ATPase activity of HSP90, thereby leading to conformational changes in the complex that preclude target kinase loading (6). CDC37 has been proposed as a therapeutic target because of its important role in multiple kinase pathways involved in proliferation and cancer cell survival, including Raf, Akt, Src, and ErbB2 pathways (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

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

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

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

Application Methods: Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) (1,2). DUBs are categorized into 5 subfamilies: USP, UCH, OTU, MJD, and JAMM (1,2). The OTU subfamily comprises a group of approximately 100 putative cysteine proteases that are homologous to the ovarian tumor gene product of Drosophila (3). OTUB1 and OTUB2 (OTU domain-containing Ubal-binding proteins) display no significant similarity to any known DUB, but are close homologs and possess an OTU domain that contains conserved cysteine, histidine, and aspartate residues that define the putative catalytic triad of cysteine proteases. Furthermore, sequence analysis of OTUB1 and OTUB2 reveals the presence of putative Ub-interaction motifs (UIMs) and Ub-associated domains (UBAs), which are characteristic of proteins that regulate protein ubiquitination. OTUB1 and OTUB2 also possess a putative nuclear localization signal (NLS) and a consensus LxxLL motif, which mediates the interaction between transcriptional co-activators and nuclear hormone receptors (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The Large tumor suppressor (LATS) proteins (LATS1, LATS2) are serine/threonine kinases that belong to the NDR family (1). The Drosophila homolog (warts) was first identified as a tumor suppressor protein that plays a role in the maintenance of ploidy. Human LATS1 was shown to localize to the centrosome and the mitotic spindle and control G2/M transition by negatively regulating cdc2 kinase activity (2,3). LATS1 is also reported to play a role in the G1 tetraploidy checkpoint, via control of p53 expression (4). LATS1 affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1 (5). LATS1 also binds the phosphorylated form of zyxin, a regulator of actin filament assembly. This interaction promotes localization of zyxin to the mitotic spindle, suggesting a role for actin regulatory proteins during mitosis (6). Decreased expression of LATS1 is associated with breast tumor aggressiveness (7), and mutations perturbing LATS1 have been associated with human sarcomas and ovarian sarcomas (8,9). LATS1 knockout mice develop soft-tissue sarcomas, ovarian stromal cell tumor, and display a high sensitivity to carcinogenic treatments (10). LATS1 and LATS2 have also been identified as key members of the Hippo signaling pathway, a conserved kinase cascade that functions to regulate cell growth and apoptosis (11). Phosphorylation of LATS by Mammalian Sterile-20-like proteins (e.g., MST1) results in LATS-mediated phosphorylation of the transcriptional co-activators YAP and TAZ (12, 13). LATS-mediated phosphorylation of YAP and TAZ promotes their cytoplasmic sequestration and association with 14-3-3 proteins, and subsequent proteasomal degradation, leading to downregulation of YAP/TAZ target genes that promote cell growth (11, 14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Western Blotting

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

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

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

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

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

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

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

Background: Salvador homolog (SAV1), originally named WW45, was first identified as a 45 kDa protein containing a pair of WW domains and a coiled-coil region (1). SAV1 was subsequently shown to function as a scaffold protein, in a protein complex that includes the kinases MST2 and LATS1, and the transcriptional co-activator YAP (2). This protein complex comprises the core components of the Hippo signaling pathway, which regulates important cellular functions, including contact inhibition and apoptosis, that function to regulate tissue growth and organ size (3,4). A genetic screen in Drosophila identified a role for SAV1 in cell cycle regulation and apoptosis (5), while embryonic mice lacking Sav1 displayed hyperplastic growth and epithelial differentiation effects (6). These findings, together with the observation that SAV1 is mutated a number of human cancer cell lines, suggest that SAV1 functions as a tumor suppressor in the Hippo signaling pathway (5, 7).

$84
100 µl
Ghost Dye™ Violet 510 Viability Dye is used to discriminate viable from non-viable mammalian cells in flow cytometry applications. Ghost Dye™ Violet 510 Viability Dye irreversibly binds free amines available on the cell surface as well as intracellular free amines exposed in cells with compromised cell membranes. Non-viable cells with loss of membrane integrity will react with significantly more Ghost Dye™ Violet 510 Viability Dye than healthy cells in the same sample. Cells that exhibit increased fluorescence intensity can be excluded from analysis.
APPLICATIONS

Application Methods: Flow Cytometry

$489
96 assays
1 Kit
The PathScan® Phospho-HER4/ErbB4 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of phospho-HER4/ErbB4 (panTyr) protein. A HER4/ErbB4 rabbit mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-HER4/ErbB4 proteins are captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse antibody is added to detect captured tyrosine-phosphorylated HER4/ErbB4 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 optical density for this developed color is proportional to the quantity of HER4/ErbB4 phosphorylated on tyrosine residues.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Research studies have implicated the HER/ErbB receptor tyrosine kinase family in normal development, cardiac function and cancer (1,2). HER4/ErbB4, like other family members, has four ectodomains, a single transmembrane domain and a cytoplasmic tail containing the active tyrosine kinase domain (3). By binding to neuregulins and/or EGF family ligands, ErbB4 forms either a homodimer or heterodimer with other ErbB family members, which results in receptor activation and signaling (3). ErbB4 is ubiquitously expressed with the highest expression occurring in brain and heart. The expression of ErbB4 in breast cancer, pediatric brain cancer and other types of carcinomas has been reported in research studies suggesting that ErbB4 expression is involved in both normal tissue development and carcinogenesis (3).

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: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

$489
96 assays
1 Kit
The PathScan® Phospho-Stat6 (Tyr641) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Stat6 protein phosphorylated at Tyr641. A Stat6 Mouse mAb has been coated onto the microwells. After incubation with cell lysates, Stat6 (phospho or nonphospho) protein is captured by the coated antibody. Following extensive washing, Phospho-Stat6 (Tyr641) Rabbit Detection Antibody is added to detect the captured phospho-Stat6 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 the absorbance for this developed color is proportional to the quantity of Stat6 phosphorylated at Tyr641.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

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

$489
96 assays
1 Kit
The PathScan® Phospho-mTOR (Ser2448) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of mTOR protein phosphorylated at Ser2448. A mTOR mouse antibody has been coated onto the microwells. After incubation with cell lysates, mTOR (phospho and nonphospho) protein is captured by the coated antibody. Following extensive washing, a phospho-mTOR (Ser2448) rabbit antibody is added to detect the captured phospho-mTOR 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 the absorbance for this developed color is proportional to the quantity of mTOR phosphorylated at Ser2448.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse, Rat

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

The CDK Antbody Sampler Kit provides and economical means of evaluating Cdk proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments.
$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated IDO (D5J4E™) Rabbit mAb #86630.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: INDO/IDO1/indoleamine 2,3-dioxygenase (IDO) is an IFN-γ-inducible enzyme that catalyzes the rate-limiting step of tryptophan degradation (1). IDO is upregulated in many tumors and in dendritic cells in tumor-draining lymph nodes. Elevated tryptophan catabolism in these cells leads to tryptophan starvation of T cells, limiting T cell proliferation and activation (2). Therefore, IDO is considered an immunosuppresive molecule, and research studies have shown that upregulation of IDO is a mechanism of cancer immune evasion (3). The gastrointestinal stromal tumor drug, imatinib, was found to act, in part, by reducing IDO expression, resulting in increased CD8+ T cell activation and induction of apoptosis in regulatory T cells (4). In addition to its enzymatic activity, IDO was recently shown to have signaling capability through an immunoreceptor tyrosine-based inhibitory motif (ITIM) that is phosphorylated by Fyn in response to TGF-β. This leads to recruitment of SHP-1 and activation of the noncanonical NF-κB pathway (5).