Microsize antibodies for $99 | Learn More >>

Product listing: TSLP (D7U1X) Rabbit mAb, UniProt ID Q969D9 #97630 to EAAT1 (D20D5) Rabbit mAb, UniProt ID P43003 #5685

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: TSLP (thymic stromal lymphopoietin) is a cytokine produced by epithelial cells at barrier surfaces and granulocytes (1). TSLP acts on dendritic cells, lymphocytes, and granulocytes by binding to a heterodimer composed of TSLPR (TSLP receptor) and IL-7Rα (2-5). Constitutive expression of TSLP at barrier surfaces contributes to homeostasis by promoting generation of noninflammatory dendritic cells (6). TSLP promotes the differentiation of Th2 cells and type 2 immune responses both in response to helminth infection and in the context of atopic diseases including asthma and atopic dermatitis (7-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Vitamin A gives rise to multiple species of biologically active lipophilic metabolites, known as retinoids, which play a critical role in numerous physiological processes such as vision and embryonic development. Intracellularly, all-trans retinoic acid is bound with high affinity to either cellular retinoic acid-binding protein 1 (CRABP1) or cellular retinoic acid-binding protein 2 (CRABP2), which aids in its solubilization within the aqueous cytosolic compartment. Belonging to the intracellular lipid-binding protein family (iLBP), the human CRABPs are 74% identical at the protein level and each CRABP is highly conserved across multiple species. Research studies have shown that knockout of Crabp1 is not lethal but results in defects in limb development (1), suggesting that CRABP1 plays a role in establishing retinoic acid concentration gradients in the developing limb bud. Although it remains unclear how CRABP1 may regulate the formation of retinoic acid gradients in vivo, research studies have suggested that CRABP1 can enhance the activities of intracellular retinoic acid-metabolizing enzymes, thus blunting cellular responses to retinoic acid (2-4).

$327
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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-p90RSK (Ser380) (D5D8) Rabbit mAb #12032.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr kinases characterized by two nonidentical, functional kinase domains (1) and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs) (2). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation (3). RSK1-3 are activated via coordinated phosphorylation by MAPKs, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: DSS-AHC critical region on the X chromosome protein 1 (DAX1) is an orphan nuclear receptor encoded by the nuclear receptor subfamily 0 group B member 1 (NR0B1) gene. DAX1 possesses an atypical DNA binding domain that allows it to form heterodimeric complexes with DNA binding partners and repress transcriptional activity (1,2). During development, DAX1 is important for establishment of the hypothalamic-pituitary-adrenal gonadal axis. The receptor is essential for development of several important hormone-producing organs that determine this axis, including the adrenal glands, pituitary, hypothalamus, and the male and female reproductive organs (3,4). Research studies suggest that DAX1 plays a role in maintenance of pluripotency in embryonic stem cells (5,6). Loss of DAX1 function through deletion or mutation results in adrenal insufficiency and hypogonadotropic hypogonadism (7), while duplication of the NR0B1 gene on the X-chromosome causes dosage-sensitive sex reversal (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interleukin-2 (IL-2) is a T cell stimulatory cytokine best known for inducing T cell proliferation and NK cell proliferation and activation (1,2). IL-2 also promotes peripheral development of regulatory T cells (Tregs) (3,4). Conversely, IL-2 is involved in the activation-induced cell death (AICD) that is observed post T cell expansion by increasing levels of Fas on CD4+ T cells (5). The effects of IL-2 are mediated through a trimeric receptor complex consisting of IL-2Rα, IL-2Rβ, and the common gamma chain, γc (1,2). IL-2Rα binds exclusively to IL-2 with low affinity and increases the binding affinity of the whole receptor complex including IL-2Rβ and γc subunits. IL-15 also binds to IL-2Rβ (1,2). γc is used by other cytokines including IL-4, IL-7, IL-9, IL-15, and IL-21 (1,2). Binding of IL-2 initiates signaling cascades involving Jak1, Jak3, Stat5, and the PI3K/Akt pathways (1,2).

$303
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 Phospho-Tyrosine (P-Tyr-1000) MultiMab™ Rabbit mAb mix #8954.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

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

$348
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 HSP60 (D6F1) XP® Rabbit mAb #12165.
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Xenopus, Zebrafish

Application Methods: Western Blotting

Background: In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8).

$364
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-S6 Ribosomal Protein (Ser235/236) (D57.2.2E) XP® Rabbit mAb #4858.
APPLICATIONS
REACTIVITY
Human, Mink, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

The Phospho-(Ser) Kinase Substrate Antibody Sampler Kit provides a fast and economical means of evaluating several phospho-Ser kinase substrates. The kit contains enough primary and secondary antibody to perform two Western blot experiments.
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: The actin-associated scaffold protein, palladin, is associated with multiple actin-rich structures, and plays a role in cellular migration and invasion (1). Palladin regulates the formation of invasive structures called podosomes and invadopodia (1-3). Alternative splicing results in at least three palladin isoforms, including the widely expressed 140 kDa and 90 kDa isoforms (2). Palladin has been shown to promote invasion in basal-like breast carcinoma models (4). Palladin is also upregulated in injured kidneys, and promotes migration of kidney cells to facilitate repair (5). In differentiating muscle cells, palladin regulates migration and myogenesis (6). Several research studies have focused on palladin expression and function in cancer-associated fibroblasts (CAFs). Researchers have shown that expression of palladin in stromal fibroblasts of pancreatic ductal adenocarcinoma is an indication of the effectiveness of chemotherapy (7). The cancer associated transcription factor Twist1 may require palladin and collagen alpha1 for its metastatic effect in fibroblasts (8).

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Phospho-Akt1 (Ser473) Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan® Phospho-Akt1 (Ser473) Sandwich ELISA Kit #7160. Capture and Detection antibodies (100X stocks) and HRP-Conjugated Secondary Antibody (1000X stock) are supplied. Sufficient reagents are supplied for 4 x 96 well ELISAs. The Phospho-Akt (Ser473) Rabbit Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added followed by Akt1 Mouse Detection Antibody and HRP-conjugated Anti-Mouse IgG. HRP substrate (TMB) is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-Akt1 (Ser473) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse, Rat

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression including with HDACs, Rb and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also play a role as a tumor suppressors and Brg1 is mutated in several tumor cell lines (6-8).

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

Application Methods: Western Blotting

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

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

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

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis and disease pathogenesis (1-3). Upon stimulation by TGF-β, activated receptors phosphorylate Smad2 and Smad3, resulting in their translocation to the nucleus, association with Smad4 and transcriptional regulation of target genes (4). Ski and SnoN are related oncoproteins originally discovered based on homology to v-Ski, the transforming protein of the Sloan-Kettering virus (5). They regulate TGF-β signaling by binding to Smad2 and Smad4 and repressing their ability to activate transcription (6). Following TGF-β stimulation, SnoN is rapidly degraded by the ubiquitin proteasome pathway providing negative feedback regulation (6-9). Overexpression of SnoN and Ski can transform avian fibroblasts and induce muscle differentiation (10). Mice heterozygous for SnoN and Ski display increased susceptibility to tumorigenesis (11,12). Interestingly, elevated expression of Ski and SnoN has been observed in many tumors and may serve as important prognostic markers (13,14). Taken together, these studies suggest possible dual functions of these proteins at different stages of tumorigenesis (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 cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated COX IV (3E11) Rabbit mAb #4850.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig, Rat, Zebrafish

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Cytochrome c oxidase (COX) is a hetero-oligomeric enzyme consisting of 13 subunits localized to the inner mitochondrial membrane (1-3). It is the terminal enzyme complex in the respiratory chain, catalyzing the reduction of molecular oxygen to water coupled to the translocation of protons across the mitochondrial inner membrane to drive ATP synthesis. The 3 largest subunits forming the catalytic core are encoded by mitochondrial DNA, while the other smaller subunits, including COX IV, are nuclear-encoded. Research studies have shown that deficiency in COX activity correlates with a number of human diseases (4). The COX IV antibody can be used effectively as a mitochondrial loading control in cell-based research assays.

$489
96 assays
1 Kit
The PathScan® Phospho-Acetyl-CoA Carboxylase (Ser79) Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of acetyl-CoA carboxylase (ACC) protein phosphorylated at Ser79 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 samples. A Phospho-ACC (Ser79) Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, phospho-ACC protein is captured by the coated antibody. Following extensive washing, an ACC Mouse Detection mAb is added to detect the captured ACC 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-ACC (Ser79) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$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

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: T cell Ig- and mucin-domain-containing molecules (TIMs) are a family of transmembrane proteins expressed by various immune cells. TIM-4 is expressed by dendritic cells and macrophages (1). Like TIM-1, TIM-4 is a receptor for phosphatidylserine (2). Interaction of TIM-4 with phosphatidylserine exposed by cells undergoing apoptosis leads to uptake of apoptotic cells (2,3). In this way, TIM-4 regulates adaptive immunity by removing apoptotic antigen-specific T cells following clearance of infection. Peritoneal macrophages from mice deficient in TIM-4 fail to effectively clear apoptotic cells leading to hyperactive T and B cells and autoimmunity (4). In addition, TIM-4 expressed by tumor-associated macrophages and dendritic cells leads to autophagy-mediated degradation of dying tumor cells, resulting in reduced antigen presentation and T cell responses (5). TIM-4 was also identified as a ligand for TIM-1, and interaction between these proteins regulates T cell proliferation (1). Finally, TIM-4 is expressed by a subset of proinflammatory B cells that produce IFN-γ and promote Th1 cell differentiation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Interleukin-4 (IL-4) is a cytokine secreted by activated T cells, basophils, and mast cells (1,2). While it contributes to many immunomodulatory responses, it is mainly recognized as the cytokine responsible for eliciting differentiation of naive T cells into Th2 lineage cells that are defined by their secretion of IL-4, IL-5, and IL-10 (3). In addition, IL-4 contributes to immunoglobulin class switching by inducing the production of IgE from B cells (4,5). IL-4 acts through the IL-4 receptor, leading to tyrosine phosphorylation and activation of the Stat6 transcription factor (6).

$303
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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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 is also 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 is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, which are cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vps34, including p105/Vps15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14 and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14 localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response to hypoxia (1). The HIF1 complex consists of two subunits, HIF-1α and HIF-1β, which are basic helix-loop-helix proteins of the PAS (Per, ARNT, Sim) family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism, and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VHL) E3 ligase complex; ubiquitination and proteasomal degradation follows (3,4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).HIF-1β is also known as AhR nuclear translocator (ARNT) due to its ability to partner with the aryl hydrocarbon receptor (AhR) to form a heterodimeric transcription factor complex (8). Together with AhR, HIF-1β plays an important role in xenobiotics metabolism (8). In addition, a chromosomal translocation leading to a TEL-ARNT fusion protein is associated with acute myeloblastic leukemia (9). Studies also found that ARNT/HIF-1β expression levels decrease significantly in pancreatic islets from patients with type 2 diabetes, suggesting that HIF-1β plays an important role in pancreatic β-cell function (10).

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

Application Methods: 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). p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro (2,3). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (5,6). p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage (4,7). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity (8,9). p53 is phosphorylated at Ser392 in vivo (10,11) and by CAK in vitro (11). Phosphorylation of p53 at Ser392 is increased in human tumors (12) and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 (10,13,14). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (13,15). Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis (16). Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response (17). Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding (18). Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response (19).

$489
96 assays
1 Kit
CST's PathScan® Total Met Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Met protein. A Met Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-Met proteins are captured by the coated antibody. Following extensive washing, Met Rabbit Antibody is added to detect both the captured phospho- and nonphospho-Met 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 Met protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Met, a high affinity tyrosine kinase receptor for hepatocyte growth factor (HGF, also known as scatter factor) is a disulfide-linked heterodimer made of 45 kDa α- and 145 kDa β-subunits (1,2). The α-subunit and the amino-terminal region of the β-subunit form the extracellular domain. The remainder of the β-chain spans the plasma membrane and contains a cytoplasmic region with tyrosine kinase activity. Interaction of Met with HGF results in autophosphorylation at multiple tyrosines, which recruit several downstream signaling components, including Gab1, c-Cbl, and PI3 kinase (3). These fundamental events are important for all of the biological functions involving Met kinase activity. The addition of a phosphate at cytoplasmic Tyr1003 is essential for Met protein ubiquitination and degradation (4). Phosphorylation at Tyr1234/1235 in the Met kinase domain is critical for kinase activation. Phosphorylation at Tyr1349 in the Met cytoplasmic domain provides a direct binding site for Gab1 (5). Research studies have shown that altered Met levels and/or tyrosine kinase activities are found in several types of tumors, including renal, colon, and breast. Thus, investigators have concluded that Met is an attractive potential cancer therapeutic and diagnostic target (6,7).

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

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).