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Product listing: Ret (C31B4) Rabbit mAb, UniProt ID P07949 #3223 to ARK5 Antibody, UniProt ID O60285 #4458

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: The Ret proto-oncogene (c-Ret) is a receptor tyrosine kinase that functions as a multicomponent receptor complex in conjunction with other membrane-bound, ligand-binding GDNF family receptors (1). Ligands that bind the Ret receptor include the glial cell line-derived neurotrophic factor (GDNF) and its congeners neurturin, persephin, and artemin (2-4). Research studies have shown that alterations in the corresponding RET gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma, and a congenital developmental disorder known as Hirschsprung’s disease (1,3). The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr at position 905 dramatically inhibits Ret autophosphorylation activity (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: Brn2/POU3F2 is a POU domain-containing transcription factor involved in neuronal differentiation and activation of the corticotrophin-releasing hormone gene (1,2). In mice, disruption of the Brn2 gene results in loss of specific neuronal lineages in the hypothalamus (3). In addition to its role in mammalian neurogenesis, Brn2 has also been implicated in melanoma tumorigenesis and has been shown in the literature to be overexpressed in human melanoma cells compared to normal melanocytes (4,5). Recent studies also identify Brn2 as a transcription factor playing an important role in keratinocyte differentiation (6). Recent reports demonstrate that overexpression of three transcription factors (Brn2, Ascl1, and Myt1L) can directly convert human fibroblasts into functional neurons under precisely defined conditions (7,8).

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

Application Methods: Western Blotting

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

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

Application Methods: Flow Cytometry, Western Blotting

Background: SAPK/Erk kinase (SEK1), also known as MKK4 or Jun kinase kinase (JNKK), activates the MAP kinase homologues SAPK and JNK in response to various cellular stresses and inflammatory cytokines (1-3). Activation of SEK1 occurs through MEKK phosphorylation of serine and threonine residues at positions 257 and 261, respectively. Like MEK, SEK is a dual-specificity protein kinase that phosphorylates SAPK/JNK at a conserved T*PY* site in its activation loop (4). Phosphorylation by Akt at Ser80 inhibits SEK1 and suppresses stress-activated signal transduction (5).

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

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

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, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNF-α, the prototypical member of the TNF protein superfamily, is a homotrimeric type-II membrane protein (1,2). Membrane-bound TNF-α is cleaved by the metalloprotease TACE/ADAM17 to generate a soluble homotrimer (2). Both membrane and soluble forms of TNF-α are biologically active. TNF-α is produced by a variety of immune cells including T cells, B cells, NK cells, and macrophages (1). Cellular response to TNF-α is mediated through interaction with receptors TNF-R1 and TNF-R2 and results in activation of pathways that favor both cell survival and apoptosis depending on the cell type and biological context. Activation of kinase pathways (including JNK, Erk1/2, p38 MAPK, and NF-κB) promotes the survival of cells, while TNF-α-mediated activation of caspase-8 leads to programmed cell death (1,2). TNF-α plays a key regulatory role in inflammation and host defense against bacterial infection, notably Mycobacterium tuberculosis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: LIN28A and LIN28B are conserved, developmentally regulated RNA binding proteins that inhibit the processing and maturation of the let-7 family of miRNAs (1,2). The let-7 miRNAs have been implicated in repression of oncogenes such as Ras, Myc, and HMGA2 (3). It has recently been shown that upregulation of LIN28A and LIN28B in primary human tumors and human cancer cell lines is correlated with downregulation of let-7 miRNAs (4). LIN28 genes are reported to be involved in primordial germ cell development and germ cell malignancy (5). In addition, allelic variation in LIN28B is associated with regulating the timing of puberty in humans (6). Overexpression of LIN28A, in conjunction with Oct-4, Sox2, and Nanog, can reprogram human fibroblasts to pluripotent, ES-like cells (7).

$327
50 tests
100 µl
Cell Signaling Technology Antibody conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct Flow Cytometric analysis of human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-NF-κB p65 (Ser536) (93H1) Rabbit mAb #3033.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry

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).

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

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

Background: Calcitonin gene-related peptide (CGRP) is a peptide of 37 amino acids that belongs to the calcitonin (CT) family of peptide hormones. The calcitonin gene (CALCA) encodes a number of tissue-specific peptides through alternative splicing of mRNA transcripts and precursor protein cleavage (1). Both calcitonin and α-CGRP are produced from the CALCA gene, while a second gene (CALCB) encodes the related β-CGRP protein (2). α-CGRP and β-CGRP share similar activities and differ by three or fewer residues depending on the species (3). The CGRP peptide activates a heterotrimeric receptor complex that consists of the seven transmembrane-spanning calcitonin receptor-like receptor, the single transmembrane-spanning RAMP1 protein, and an intracellular receptor component protein (4,5). CGRP is expressed in the central and peripheral nervous system in mammals, where it exhibits several important physiologic roles. Research studies demonstrate that CGRP is a potent vasodilatator (6) and a modulator of acetylcholine receptor function at neuromuscular junctions (7). Additional studies indicate that CGRP peptide is involved in feeding (8) and inflammatory pain (9). CGRP peptide also plays a key role in the physiology of migraine attacks. Specifically, CGRP peptide levels increase during acute migraine attacks, which can be ameliorated through treatment with CGRP antagonists (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The endocannabinoid system consists of the cannabinoid receptors, CB1 and CB2 receptors, the enzymes that produce and degrade the endogenous cannabinoid ligands (such as FAAH, DAG lipases, and MAG lipase), and the endocannabinoid ligands derived from the metabolism of arachidonic acid, 2-arachidonoylglycerol (2-AG) and anandamide (1-3). CB1 receptor belongs to the superfamily of G protein-coupled receptors (GPCRs) and harbors a large N-terminal extracellular domain, seven transmembrane domains, and a C-terminal intracellular tail. CB1 receptor is coupled to the Gai/o subunit of the G protein which inhibits adenylyl cyclases and regulates calcium and potassium ion channels (4). CB1 receptor is one of the most abundant GPCRs in the central nervous system. It has been show to play critical roles in the wiring of the brain during development (5), in neuronal plasticity (6), analgesia, drug abuse and metabolic homeostasis (7). In addition, CB1 receptor has been shown to interact with other GPCRs, to give rise to novel pharmacological and signaling heteromers with implication in diseases (8,9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry analysis in monkey cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated DYKDDDDK Tag (D6W5B) Rabbit mAb (Binds to same epitope as Sigma's Anti-FLAG® M2 Antibody) #14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

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

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

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, 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

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

Background: Ku is a heterodimeric protein composed of two subunits (Ku70 and Ku80) originally identified by researchers as autoantigens associated with several autoimmune diseases including scleroderma, polymyositis, and systemic lupus erythematosus (1). Ku is an abundant, ubiquitously expressed nuclear protein that binds to and stabilizes the ends of DNA at telomeres or double-stranded DNA breaks (2-5). The Ku70/Ku80 heterodimer has ATP-dependent DNA helicase activity and functions as the DNA-binding regulatory component of DNA-dependent protein kinase (DNA-PK) (6-8). The assembly of the DNA-PK complex at DNA ends is required for nonhomologous end-joining (NHEJ), one mechanism involved in double-stranded DNA break repair and V(D)J recombination (8). DNA-PK has been shown to phosphorylate many proteins, including p53, serum response factor, c-Jun, c-Fos, c-Myc, Oct-1, Sp-1, and RNA polymerase II (1,8). The combined activities of Ku70/Ku80 and DNA-PK implicate Ku in many cellular functions, including cell cycle regulation, DNA replication and repair, telomere maintenance, recombination, and transcriptional activation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Bax is a key component for cellular induced apoptosis through mitochondrial stress (1). Upon apoptotic stimulation, Bax forms oligomers and translocates from the cytosol to the mitochondrial membrane (2). Through interactions with pore proteins on the mitochondrial membrane, Bax increases the membrane's permeability, which leads to the release of cytochrome c from mitochondria, activation of caspase-9 and initiation of the caspase activation pathway for apoptosis (3,4).

The Tight Junction Antibody Sampler Kit provides an economical means to evaluate the presence of a number of proteins involved in tight junctions. The kit contains enough primary antibodies to perform two western blot experiments per primary antibody.
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: ROS1, an orphan receptor tyrosine kinase of the insulin receptor family, was initially identified as a homolog of v-ros from the UR2 sarcoma virus (1). ROS1 consists of a large extracellular domain that is composed of six fibronectin repeats, a transmembrane domain, and an intracellular kinase domain. While the function of ROS1 is undefined, it has been shown to play an important role in differentiation of epididymal epithelium (2). The first oncogenic fusion of ROS1, FIG-ROS1, was initially identified by research studies in glioblastoma (3), and subsequent studies have found this fusion in cholangiocarcinoma (4), ovarian cancer (5) and non-small cell lung cancer (NSCLC) (6). Investigators have found additional oncogenic ROS1 fusion proteins in NSCLC (at a frequency of ~1.6%), where the ROS1 kinase domain is fused to the amino-terminal region of a number of different proteins, including CD74 and SLC34A2 (6-8). ROS1 fusion proteins activate the SHP-2 phosphatase, PI3K/Akt/mTOR, Erk, and Stat3 pathways (3,4,9).

$269
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: S100A8 and S100A9 are calcium-binding proteins that form a noncovalent heterodimer present in monocytes, neutrophils, macrophages, and some epithelial cells (1, 2). S100A8 and S100A9 are secreted by a tubulin-dependent mechanism during inflammatory conditions and have antimicrobial and chemotactic functions (3-5). Extracellular S100A8/S100A9 also induces an inflammatory response in endothelial cells, including induction of proinflammatory chemokines and adhesion molecules and increased vascular permeability (6). S100A8/S100A9 induces and recruits myeloid-derived suppressor cells (MDSC) in tumor-bearing mice (7). MDSC produce additional S100A8/S100A9 themselves, resulting in a positive feedback mechanism that sustains MDSC accumulation (7). S100A8/S100A9 is also highly expressed in psoriatic skin, where it directly upregulates transcription of complement protein C3, which contributes to disease (8). In addition, tumor-infiltrating myeloid cells induce expression of S100A8 and S100A9 in cancer cells, which increases invasiveness and metastasis (9).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Olfactomedin-4 (OLFM4, hGC-1) is a member of the Olfactomedin family, a small group of extracellular proteins defined by the presence of a conserved "Olfactomedin domain" that is thought to facilitate protein-protein interactions (1). OLFM4 is a secreted glycoprotein, which forms disulfide bond-mediated oligomers, and is thought to mediate cell adhesion through its interactions with extracellular matrix proteins such as lectins (2). Human OLFM4 was first cloned from myeloid cells (3) and is expressed in a distinct subset of neutrophils, though the functional significance of this differential expression pattern remains unclear (4). Among normal tissues, the expression of OLFM4 protein is most abundant in intestinal crypts (5), where it has garnered attention as a possible marker of intestinal stem cells (6). Notably, OLFM4 expression is markedly increased in several tumor types, including colorectal, gastric, pancreas, lung, and breast (reviewed in [1]). Furthermore, research studies show that the expression levels of OLFM4 vary in relation to the severity and/or differentiation status of multiple tumor types (1, 6-8), leading to the suggestion that OLFM4 may have utility as a prognostic marker in some cancer patients (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Janus family of tyrosine kinases (Jak1, Jak2, Jak3, and Tyk2) are activated by ligands binding to a number of associated cytokine receptors (1). Upon cytokine receptor activation, Jak proteins become autophosphorylated and phosphorylate their associated receptors to provide multiple binding sites for signaling proteins. These associated signaling proteins, such as Stats (2), Shc (3), insulin receptor substrates (4), and focal adhesion kinase (FAK) (5), typically contain SH2 or other phosphotyrosine-binding domains.Activation of Jak kinases upon cytokine receptor binding is associated with tyrosine phosphorylation within their activation loops, including Tyr1034/1035 of Jak1, Tyr1007/1008 of Jak2, Tyr980/981 of Jak3, and Tyr1054/1055 of Tyk2. Many studies have indicated that various cytokine receptors have clear preferences that utilize distinct Jak family members. Aberrant regulation of Jak signaling is associated with a number of diseases, including myeloproliferative neoplasms, leukemia, and inflammatory disease (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated c-Myc (D84C12) Rabbit mAb #5605.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$122
20 µl
$307
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Cdc25 is a protein phosphatase responsible for dephosphorylating and activating cdc2, a crucial step in regulating the entry of all eukaryotic cells into mitosis (1). cdc25C is constitutively phosphorylated at Ser216 throughout interphase by c-TAK1, while phosphorylation at this site is DNA damage-dependent at the G2/M checkpoint (2). When phosphorylated at Ser216, cdc25C binds to members of the 14-3-3 family of proteins, sequestering cdc25C in the cytoplasm and thereby preventing premature mitosis (3). The checkpoint kinases Chk1 and Chk2 phosphorylate cdc25C at Ser216 in response to DNA damage (4,5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Mitogen-activated protein kinases (MAPKs) are activated by various extracellular signals and play crucial roles in regulating cell proliferation, differentiation, survival, and apoptosis (1). MAPK-interacting kinases (Mnks or MKNKs) are direct downstream substrates of MAPK and were first discovered independently by the work of Fukunaga and Hunter (2) and Waskiewicz and Cooper (3). There are 2 Mnks in human, termed Mnk1 and Mnk2. Both Mnks possess a MAPK-binding domain that allows them to bind to and then to be phosphorylated by Erk and p38. The phosphorylation in the T-loop of Mnks stimulates their in vitro kinase activity toward a substrate, eukaryotic initiation factor-4E (eIF4E) (2,3). eIF4E is a key component of the translational machinery mediating the initiation of translation, but how phosphorylation of eIF4E regulates translation initiation is still under investigation (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Forkhead box M1 (FoxM1) is a forkhead box family transcription factor that regulates a number of genes throughout the cell cycle to help control DNA replication, mitosis, and cell proliferation. FoxM1 expression increases during G1 and S and reaches maximum levels in G2/M (1-3). Nuclear translocation occurs just before entry into G2/M and is associated with FoxM1 phosphorylation (4). Phosphorylation of FoxM1 by MAPK (Ser331, Ser704), Cyclin/Cdk (Ser4, Ser35, Thr600, Thr611, Thr620, Thr627, Ser638), Plk1 (Ser715, Ser724), and Chk2 (Ser376) stabilizes and activates FoxM1 (4-8). Forkhead box M1 is expressed in all embryonic tissues but is restricted to proliferating tissues in adults (9). Research studies show that FoxM1 expression is negatively regulated by p53 (10,11). Upregulation of FoxM1 is associated with many human cancers, including prostate, breast, lung, ovary, colon, pancreas, stomach, bladder, liver, and kidney, and may be associated with p53 mutations in some tumors (11,12). As a result, FoxM1 inhibitors have become a topic of interest for potential cancer therapy (13).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

Background: Cyclin-dependent kinases (CDKs) are a family of Ser/Thr kinases that regulate cell-cycle transitions through their association and subsequent phosphorylation of targets in a strictly ordered fashion (1). The substrates for CDKs are proline-directed. The consensus amino acid sequence for CDK substrate is (K/R)(S*)PX(K/R), where X denotes any one of the 20 amino acids (2-4) and S* is the phosphorylation site. Phospho-CDK Substrate Motif [(K/H)pSP] MultiMab™ Rabbit mAb mix recognizes phosphorylated CDK substrates at their consensus motif, providing a powerful tool for CDK target discovery and characterization, as well as HTS drug screening for potential kinase regulators.

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

Application Methods: Western Blotting

Background: AMP-activated protein kinases (AMPKs) constitute a serine/threonine protein kinase family, which is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPKα1, AMPKα2, MELK and SNARK are the catalytic subunits in the family (2). Recently, AMPK-related protein kinase ARK5 was identified, which shares 84% similarity with the sequence of the catalytic domain of SNARK (2). In vitro, Akt phosphorylates ARK5 at Ser600. This phosphorylation activates ARK5, which in turn results in the increased phosphorylation of the SAMS peptide, an AMPK consensus substrate (2). In vivo experiments showed that Akt-activated ARK5 is critical for the survival of cells under glucose starvation (2). Furthermore, studies also linked ARK5 to tumor invasion (3, 4). Overexpressed ARK5 leads to higher tumor growth rate (3). For example, the overexpression of ARK5 in pancreatic tumor cell line PANC-1 significantly elevates its metastasis in the liver (4).