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Product listing: Mios (D12C6) Rabbit mAb, UniProt ID Q9NXC5 #13557 to ALK (31F12) Mouse mAb, UniProt ID Q9UM73 #3791

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex plays a critical role in cell growth regulation (1,2). mTORC1 activity is modulated by energy levels, growth factors, and amino acids (3,4). Four related GTPases (RagA, RagB, RagC, and RagD) interact with raptor in mTORC1, which is necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2). The GAP Activity Towards Rags (GATOR) complex interacts with Rag GTPases and is made up of a pair of protein subcomplexes (5). The GATOR1 subcomplex includes the proteins DEPDC5, Nprl2 and Nprl3, and is a RagA and RagB GTPase-activating protein (GAP) that negatively regulates mTORC1 signaling. Conversely, the GATOR2 subcomplex (including Mios, WDR24, WDR59, Seh1L and Sec13 proteins) is a positive regulator of mTORC1 signaling (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, 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.Atg13/Apg13 was originally identified in yeast as a constitutively expressed protein that was genetically linked to Atg1/Apg1, a protein kinase required for autophagy (4). Overexpression of Atg1 suppresses the defects in autophagy observed in Atg13 mutants (4). Autophagy requires a direct association between Atg1 and Atg13, and is inhibited by TOR-dependent phosphorylation of Atg13 under high-nutrient conditions (5). Similarly, mammalian Atg13 forms a complex with the Atg1 homologues ULK1/2, along with FIP200, which localizes to autophagic isolation membranes and regulates autophagosome biogenesis (6-8). mTOR phosphorylates both Atg13 and ULK1, suppressing ULK1 kinase activity and autophagy (7-9). ULK1 can directly phosphorylate Atg13 at a yet unidentified site, presumably to promote autophagy (7,8). Additional studies suggest that Atg13 and FIP200 can function independently of ULK1 and ULK2 to induce autophagy through an unknown mechanism (10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK3 and MKK6 are two closely related dual-specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site, Thr-Gly-Tyr, but do not phosphorylate or activate Erk1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates its ability to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 are both activated by different forms of cellular stress and inflammatory cytokines (4,5). Activation of MKK3 and MKK6 occurs through phosphorylation at Ser189 and Thr222 on MKK3 (2) and Ser207 and Thr211 on MKK6 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Cancer/testis antigens (CTAs) are a family of more than 100 proteins whose normal expression is largely restricted to immune privileged germ cells of the testis, ovary, and trophoblast cells of the placenta. Although most normal somatic tissues are void of CTA expression, due to epigenetic silencing of gene expression, their expression is upregulated in a wide variety of human solid and liquid tumors (1,2). As such, CTAs have garnered much attention as attractive targets for a variety of immunotherapy-based approaches to selectively attack tumors (3).

The AMPA Receptor (GluA) Antibody Sampler Kit provides an economical means of evaluating the four subunits of AMPARs. The kit contains enough primary and secondary antibodies to perform two western blot experiments with each antibody.

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

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

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

$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 S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Connexin 43 (Cx43) is a member of the large family of gap junction proteins. Connexins assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Clusters of these channels assemble to make gap junctions. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (1,2). Ser368 of Cx43 is phosphorylated by protein kinase C (PKC) after activation by phorbol esters, which decreases cell-to-cell communication (3). Src can interact with and phosphorylate Cx43 to alter gap junction communication (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Transferrin receptor 1 (CD71, TFRC) is a type II transmembrane receptor and carrier protein responsible for the uptake of cellular iron through receptor-mediated endocytosis (1). Neutral pH at the cell surface promotes binding of the iron-binding glycoprotein transferrin (Tf) to the CD71 receptor. The receptor-ligand complex enters the cell through receptor-mediated endocytosis and is internalized into an endosome. Relatively lower endosomal pH leads to a change in the local charge environment surrounding the iron-transferrin binding site and results in the release of iron (2). The receptor-ligand complex is recycled to the cell surface where transferrin dissociates from the CD71 receptor (2). Ubiquitously expressed transferrin receptor is continuously recycled and undergoes clathrin-mediated endocytosis regardless of ligand binding state. The interaction between receptor and ligand has been studied in detail. The helical domain of CD71 directly interacts with the transferrin C-lobe and induces a conformation change in Tf to facilitate the transport process (3). Interaction between the receptor CD71 and transferrin is mediated by the membrane protein hemochromatosis (HFE). HFE binds the α-helical domain of CD71, blocking formation of the CD71-transferrin complex and inhibiting iron uptake (4,5). In addition to binding transferrin, CD71 also interacts with H-ferritin at the cell surface and transports this intracellular iron storage protein to cellular endosomes and lysosomes (6). Additional studies indicate that the transferrin receptor is an evolutionarily conserved receptor for a number or arenaviruses and at least one retrovirus (7,8). Aberrant expression of CD71 is seen in a number of cancers, including thyroid carcinomas, lymphomas, and T-lineage leukemias, suggesting a possible therapeutic role for targeted inhibition of the transferrin receptor (9,10).

The p38 MAPK Isoform Activation Antibody Sampler Kit provides an economical means to evaluate the activation status of individual isoforms of p38 MAPK through immunoprecipitation of the phosphorylated p38 MAPK followed by western blot using isoform specific antibodies. The kit includes enough primary and secondary antibodies to perform two IP/western blot experiments.

Background: p38 MAP kinase (MAPK), also called RK (1) or CSBP (2), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (1-4). Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors (1-5). MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 (3) and to phosphorylate the transcription factors ATF-2 (5), Max (6), and MEF2 (5-8). SB203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-imidazole) is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27 (9). SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases (10).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The B cell antigen receptor (BCR) is composed of membrane immunoglobulin molecules non-covalently associated with the heterodimeric signaling component, CD79A and CD79B (also known as Igα and Igβ, respectively) (1,2). The presence of this receptor complex is essential for B cell development and function (3). Following antigen binding, CD79A/CD79B heterodimers are phosphorylated and initiate intracellular signaling through Src family kinases, Lyn, Blk, and Fyn, as well as Syk and Btk tyrosine kinases (4,5). The complexity of BCR signaling results in a variety of distinct cellular functions, such as proliferation, tolerance, apoptosis, and differentiation (6). BCR-antigen ligation also leads to internalization of the complex, trafficking to late endosomes, and antigen presentation in major histocompatibility molecules on the B cell surface (7,8). CD79B enhances the phosphorylation of CD79A (9). Alternatively spliced transcript variants encoding different isoforms of CD79B have been identified (10). CD79B is widely expressed on B cell malignancies and may serve as a target for therapeutic intervention (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Sprouty (Spry) family of proteins are antagonists of receptor tyrosine kinase (RTK)-induced signaling (1, 2). The Spry proteins play crucial roles in regulating growth and development of living organisms. Since originally discovered in Drosophila, four human orthologs of Spry proteins (Spry1-4) have been identified. All human Spry proteins possess a conserved carboxyl-terminal cysteine-rich SPR domain, which harbors a signal for protein translocation from cytosol to membrane ruffles (3,4). The SPR domain also enables the Spry proteins to form homo- or hetero-dimers and to interact with other proteins including kinases and phosphatases. The SPR domain is essential for the inhibitory modulation of Spry proteins on RTK signaling (1,2).

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

Application Methods: Western Blotting

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

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$489
96 assays
1 Kit
PathScan® Total B7-H4 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of B7-H4. A B7-H4 Rabbit mAb has been coated onto the microwells. After incubation with cell lysates, B7-H4 protein is captured by the coated antibody. Following extensive washing, a B7-H4 Mouse Detection mAb is added to detect the captured B7-H4 protein. A HRP-linked, anti-mouse 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 total B7-H4.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: B7 homolog 4 (B7-H4, VTCN1) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses (1-3). B7-H4 protein contains two extracellular Ig-like V-type domains, a transmembrane domain, and a short, two amino acid intracellular domain (3). The B7-H4 protein is shown to inhibit T cell activation, proliferation, and cytokine production (1,4,5). Although B7-H4 mRNA is widely expressed, B7-H4 protein is restricted to antigen presenting cells and B cells (1). The B7-H4 protein is also found in several tumor types, including ovarian cancer and breast cancer (6). Research studies indicate that B7-H4 protein is present on the surface of ovarian tumor cells, and that targeted inhibition of B7-H4 using recombinant antibodies restores T cell activation pathways. These studies suggest some potential therapeutic value in blocking B7-H4 function and restoring T cell function in cancer patients (7,8).

$195
200 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, 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.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 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 PD-L1 (Extracellular Domain Specific) (D8T4X) Rabbit mAb #86744.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

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

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

Application Methods: Western Blotting

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (5). Embryonic ectoderm development protein (EED) is a component of the PRC2 complex, which together with Ezh2 and SUZ12 is absolutely required for histone methyl-transferase activity (6). EED, SUZ12 and EZH2 are overexpressed in various types of cancer, including tumors of the colon, breast, prostate and ovary (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Heregulin (HRG), also called neuregulin (NRG1), neu differentiation factor (NDF) or glial growth factor-2 (GGF-2), is a soluble growth factor synthesized as a transmembrane precursor molecule. Metalloproteinases and other proteases catalyze the cleavage of its extracellular domain which is then released and functions as a ligand for ErbB3 and ErbB4 receptor tyrosine kinase. The signaling pathways of HRG-ErbB3/ErbB4 are involved in regulation of cell proliferation, differentiation, invasion, and survival of both normal and malignant tissues (1,2). Abnormality of HRG-ErbB signaling leads to development of a variety of human diseases.HRG family has four isoforms including HRG-1, -2, -3 and -4, which are derived from alternative exon splicing. Moreover, they showed various tissue expression and biological activities (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: DLK1 (delta-like-1), also known as fetal antigen 1 (FA1) and preadipocyte factor 1 (pref-1), is a member of the epidermal growth factor (EGF)-like family of proteins, containing six tandem EGF-like repeats (1,2). DLK1 is a paternally expressed, imprinted gene that plays an important role in normal development and in the maintenence of homeostasis of adipose tissue mass (3). DLK1 deficient mice display growth retardation, obesity, skeletal malformation, and increased serum lipid metabolites (4). It has been reported that the ectodomain of DLK1 is shredded from the cell surface and inhibits adipocyte differentiation ( 5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Scribble (Scrib) was originally identified in a genetic screen in Drosophila along with cell polarity determinants Discs Large (Dlg) and Lethal giant larvae (Lgl). Drosophila mutants homozygous for these genes share similar phenotypes, including the loss of apicobasal cell polarity and neoplastic tissue overgrowth. These phenotypic similarities suggest that these three proteins function in a common pathway important for establishing and maintaining apicobasal polarity in epithelial cells (1,2). Scribble contains many leucine-rich repeats and PDZ domains important for localizing scribble to adherens junctions and basolateral regions of mammalian epithelial cells (3). Scribble reportedly binds β-catenin, APC, E-cadherin and the E6 protein from high-risk virus type of HPV through a short motif important for E6-induced cell transformation (4-8). Overexpression of scribble inhibits transformation of rodent epithelial cells by HPV E6/7 proteins (8).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of proteins, which consists of nine members, has been divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All of the CHD proteins contain two tandem N-terminal chromodomains, a SWI/SNF-related ATPase domain, and a C-terminal DNA binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes the energy from ATP hydrolysis to modify chromatin structure. CHD1 is a euchromatic protein that associates with the promoters of active genes, and is required for the maintenance of open chromatin and pluripotency in embryonic stem cells (3-6). The two chromodomains of CHD1 facilitate its recruitment to active genes by binding to methyl-lysine 4 of histone H3, a mark associated with transcriptional activation (4-6). Yeast CHD1 is a component of the SAGA and SLIK histone acetyltransferase complexes, and is believed to link histone methylation with histone acetylation during transcriptional activation (6). The CHD2 protein is not well characterized; however, mouse knockout studies suggest important functions in development and tumor suppression. Homozygous CHD2 knockout mice exhibit delayed growth and perinatal lethality (7). Heterozygous knockout mice show increased mortality and gross organ abnormalities, in addition to increased extramedullary hematopoiesis and susceptibility to lymphomas (7,8). CHD2 mutant cells are defective in hematopoietic stem cell differentiation and exhibit aberrant DNA damage responses (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Collapsin Response Mediator Protein-2 (CRMP-2) is expressed at high levels in the developing nervous system and plays a critical role in axonal outgrowth by specifying axon/dendrite fate and establishing neuronal polarity (1,2). CRMP-2 enhances axon elongation and branching by binding to tubulin heterodimers to promote microtubule assembly (3). GSK-3β inactivates CRMP-2 by phosphorylating it at Thr514. CRMP-2 is primed following phosphorylation at Ser522 by CDK5 and at Thr518 by GSK-3β (2). Phosphorylation of CRMP-2, which decreases tubulin binding ability, can be inhibited by NT-3 and BDNF through the PI3 kinase/Akt pathway (2). CRMP-2 also mediates semaphorin-induced growth cone collapse (4). Hyperphosphorylation of CRMP-2 is found in Alzheimer disease plaques with concurrent elevated GSK-3β activity in these patients (5).

$115
100 µl
APPLICATIONS

Application Methods: Chromatin IP, Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunofluorescence (Paraffin), Immunohistochemistry (Paraffin), Immunoprecipitation

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.

$132
400 µl
This Cell Signaling Technology (CST) antibody is immobilized by the covalent reaction of hydrazinonicotinamide-modifed antibody with formylbenzamide-modified magnetic bead. Rabbit (DA1E) mAb IgG XP® Isotype Control (Magnetic Bead Conjugate) is useful to determine non-specific immunoprecipitation complexes.
APPLICATIONS

Application Methods: Immunoprecipitation

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.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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).