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Product listing: β-Actin (13E5) Rabbit mAb (Alexa Fluor® 594 Conjugate), UniProt ID P60709 #9470 to ERp44 Antibody, UniProt ID Q9BS26 #2886

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for immunofluorescent analysis in monkey cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Actin (13E5) Rabbit mAb #4970.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

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

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Panthothenate kinase (PANK) is an enzyme that is responsible for catalyzing the first step in coenzyme A (CoA) synthesis (1-4). There are four human PANK genes (PANK1-4) (1-4). PANK4 is ubiquitously expressed, but higher expression levels are observed in muscle (1,2). PANK4 expression is elevated in rat skeletal muscle under high glucose conditions (2). There is evidence that rat PANK4 colocalizes with pyruvate kinase M2 (PKM2) in vitro (2). PANK4 may also play a protective role in beta-cell apoptosis by lowering the levels of pro-caspase-9 (3). Research studies have shown that mutations in the PANK2 gene are associated with Neurodegeneration with Brain Iron Accumulation (NBIA), formerly known as Hallervorden-Spatz syndrome (1,4). Expression of hPANK4 in a Drosophila model of NBIA rescues the phenotype with the exception of infertility (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The PAF (RNA polymerase II (RNAPII) associated factor) complex was initially identified in yeast and is comprised of subunits PAF1, Leo1, Ctr9, Cdc73, RTF1 and Ski8 (1,2). The PAF complex plays an important role in transcription initiation and elongation by RNAPII by regulating the establishment of proper histone modifications such as histone H2B ubiquitination and the recruitment of the histone chaperone FACT (facilitates chromatin transcription) (3-5). The PAF complex also plays a role in mRNA processing and maturation by interacting with and recruiting the cleavage and polyadenylation specificity factor and cleavage stimulation factor complexes via the Cdc73 subunit (6,7). In addition, the Ski8 subunit of the PAF complex is part of the hSKi complex that regulates RNA surveillance, suggesting an important function of the complex in coordinating events associated with proper RNA maturation during transcription (1,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PNK (polynucleotide kinase) is a DNA repair enzyme that participates in single strand break repair and non-homologous end rejoining (NHEJ) for double strand breaks. PNK possesses a 5'-DNA kinase activity and a 3'-DNA phosphatase activity (1,2). It has three domains, a C-terminal kinase domain, a central phosphatase domain, and an N-terminal forkhead associated (FHA) domain that is responsible for protein-protein interactions. Reduction in expression of PNK by RNAi sensitizes cells to ionizing radiation and topoisomerase I inhibitors (3)

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated E-Cadherin (24E10) Rabbit mAb #3195.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

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

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

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

Background: Echinoderm microtubule-associated protein-like 4 (EML4) is a 120 kDa microtubule-associated WD-repeat protein of the echinoderm microtubule-associated protein family (1). The expression of EML4 is necessary for correct intracellular microtubule network formation (2). EML4 protein expression is upregulated during mitosis and downregulated during the remaining cell cycle (1). During mitosis, EML4 is heavily phosphorylated and is associated with the mitotic spindle (2). The amino-terminal segment of EML4 is essential for microtubule association and function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: RanBP9 (RanBPM) is a Ran binding protein ubiquitously expressed and highly conserved in different organisms. It is a scaffolding protein that was identified as an interacting protein of MET inducing Ras- Erk activation (1). Several domains and motifs regulate the nuclear and cytoplasmic localization of RanBP9 (2). Research studies indicate that RanBP9 might contribute to the pathogenesis of Alzheimer’s Disease (AD). In addition to elevated expression levels in AD samples, this may involve interaction of RanBP9 with APP and BACE1 promoting endocytosis of APP and increased BACE1 mediated cleavage of APP to generate β-amyloid peptides (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CHD5 (chromodomain-helicase-DNA-binding-5) is one of the 9 known CHD proteins and is homologous to its family members, CHD3 and CHD4 (1-3). CHD5 interacts with the nucleosome remodeling and deacetylation (NuRD) complex (1,4). CHD5 is characterized by two PHD domains, two chromo domains, a SNF2-like helicase/ATPase domain, as well as a conserved coiled-coil motif in the C-terminal region (1). CHD5 binds to the N-terminus of Histone H3 via its PHD domains (1). CHD5 was first characterized as a tumor suppressor gene found to be frequently lost in neuroblastomas (1). Since its initial discovery, CHD5 has been studied extensively and has been implicated in numerous other cancers including gliomas, breast, lung, ovarian, and prostate cancers as well as in laryngeal squamous cell carcinomas and gallbladder carcinoma (1). CHD5 is thought to be a prognostic marker in neuroblastoma patients. High CHD5 levels are strongly correlated with favorable clinical outcomes, whereas low or absent expression is associated with MYCN amplification and poor outcomes (1). In addition, CHD5 has a dual function in neurogenesis, playing a transcription activating role in neurogenesis, while interacting with the Polycomb group proteins to repress genes encoding regulators of other lineages. Deletion of CHD5 also inhibits neuronal differentiation leading to the accumulation of undifferentiated progenitors (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The voltage gated potassium channel Kv7.2 (KCNQ2) associates with its family member Kv7.3 (KCNQ3) to form an M-channel that is involved in synaptic input response and sub-threshold excitability of neurons (1). This heteromeric channel generates the M-current, a slowly activating and deactivating potassium conductance that determines the neuronal excitability (2,3). Expression of these two M-channel proteins is mainly seen within the central nervous system, with both Kv7.2 and Kv7.3 expressed post-synaptically in the human cortex and hippocampus (4). The calcium-binding protein calmodulin binds two separate sites in Kv7.2 to influence exit of the channel protein from the endoplasmic reticulum and translocation to the plasma membrane (5). Mutations in the corresponding KCNQ2 gene cause benign familial neonatal seizures-1 (BFNS1), an autosomal dominant form of epilepsy characterized by seizure clusters closely following birth (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

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

$293
100 µl
REACTIVITY
Human

Background: Nanog is a homeodomain-containing transcription factor that is essential for the maintenance of pluripotency and self renewal in embryonic stem cells (1). Nanog expression is controlled by a network of factors including Sox2 and the key pluripotency regulator Oct-4 (1). Recent advances in somatic cell reprogramming have utilized viral expression of combinations of transcription factors including nanog, Oct-4, Sox2, KLF4, c-Myc, and LIN28 (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The high affinity copper uptake protein 1 (CTR1, SLC31A1) helps maintain copper homeostasis by mediating dietary copper intake chiefly in the small intestine (1). A series of methionine-rich repeats and other residues are conserved among CTR1 genes across taxa, and are thought to be important for copper transport (2,3). In mammalian cells, CTR1 is localized to the plasma membrane and intracellular vesicles (3). Upon copper uptake via plasma membrane into cells, CTR1 is down regulated by clathrin-dependent endocytosis and degradation of CTR1 protein (4). Research studies suggest that the CTR1 copper transporter also mediates uptake of the anticancer drug cisplatin in yeast and mammals and that decreased CTR1 can result in the development of cisplatin resistance (5,6). Treatment of cancer cells with cisplatin can result in reduced CTR1 expression, which reduces cisplatin accumulation within cells and leads to cisplatin resistance in some human cancer cells (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Voltage gated sodium channels are composed of a large alpha subunit and auxiliary beta subunits. The alpha subunit has 4 homologous domains, with each domain containing 6 transmembrane segments. These segments function as the voltage sensor and sodium permeable pore. Upon change of membrane potential, the sodium channel is activated, which allows sodium ions to flow through (1,2). When associated with beta subunits or other accessory proteins, the alpha subunit is regulated at the level of cell surface expression, kinetics, and voltage dependence (3,4).There are 9 mammalian alpha subunits, named Nav1.1-Nav1.9 (5). These alpha subunits differ in tissue specificity and biophysical functions (6,7). Seven of these subunits are essential for the initiation and propagation of action potentials in the central and peripheral nervous system while Nav1.4 and Nav1.5 are mainly expressed in skeletal muscle and cardiac muscle (8,9). Mutations in these alpha channel subunits have been identified in patients with epilepsy, seizure, ataxia, sensitivity to pain, and cardiomyopathy (reviewed in 10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). The PLD2 isoform is highly expressed in many cancers, such as colorectal and breast cancers (2,3). PLD2 also acts as a guanine nucleotide exchange factor for the small GTPase Rac2 independent of its phospholipase activity (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: Peptide tyrosine-tyrosine (PYY; also known as Peptide YY) is a short amino acid peptide that is a member of the gastrointestinal (GI) family of hormones (1). Other GI hormone family members include glucagon-like peptide-1 (GLP-1), ghrelin, cholecytokinin (CCK), leptin, glucose, and insulin. GI hormones have diverse physiological and behavioral functions, but some are part of the brain-gut axis that combines neural functions with the gut to regulate appetite and satiety. This subset of hormones is expressed in enteroendocrine cells, specialized cells of the GI tract and pancreas that are part of the enteric endocrine system. PYY, as well as GLP-1, is secreted by a specific group of enteroendocrine cells, L cells, which line parts of the ileum and colon. At least two endogenous forms of PYY exist: full length PYY (1-36) and cleavage-generated PYY (3-36). Ectopic peripheral injection of PYY (3-36) suppresses food intake and reduces weight gain (2). Systemic PYY (3-36) is likely to regulate food intake, in part, by regulation of hypothalamus-mediated homeostasis via arcuate nucleus (Arc)-expressed neuropeptide Y2 receptor (Y2R) (2, 3). Thus, Peptide YY is an important GI hormone that regulates Arc-expressed neuropeptide Y2R to inhibit feeding in the gut-hypothalamic pathway.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Phosphatidylcholine-specific phospholipase D (PLD) hydrolyzes phosphatidylcholine (PC) to produce choline and phosphatidic acid (PA). PA is the precursor of the second messenger, diacylglycerol (DAG). Two isoforms of PLD (PLD1 and PLD2) have been identified so far. Both are regulated by protein kinases, small GTPases and Ca2+ (1). PLD1 is phosphorylated at Ser2, Ser561, and Thr147 by PKC (2,3). Phosphorylation at Thr147 and Ser561 regulates PLD1 activity (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: The neurotransmitters GABA and glycine activate ligand-gated chloride channels and thus mediate fast synaptic inhibition. Gephyrin is a postsynaptic, scaffolding protein anchoring type A GABA and glycine receptors to the cytoskeleton. In addition to gephyrin’s function clustering synaptic neurotransmitter receptors, it plays an essential role in the biosynthesis of the molybdenum cofactor (MoCo). Molybdenum cofactor chelates and activates sulfite oxidase, an enzyme crucial for survival (1). GSK-3β and Erk1/2 phosphorylate gephyrin at residue Ser270 and Ser268, respectively. These post-translational modifications alter the clustering of gephyrin, effecting the amplitude and frequency of GABAergic inhibitory currents (2,3). Researchers are analyzing the role of abnormal gephyrin clustering and function in major neurological, neuro-developmental and psychiatric disorders (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Hypoxia up-regulated protein 1 (HYOU1, ORP150) is an endoplasmic reticulum (ER)-resident stress protein whose expression is upregulated in response to a variety of environmental conditions that promote ER stress (1,2). The amino-terminal region of HYOU1 displays extensive similarity to the ATPase domain of HSP70 family proteins, suggesting that HYOU1 contributes to maintaining proper protein folding and secretion under conditions that promote ER stress (2). Research studies have demonstrated that HYOU1 is cytoprotective and is involved in the inhibition of hypoxia-induced cell death (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).

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

Application Methods: Western Blotting

Background: Focal adhesions connect the cytoskeleton with the extracellular matrix (ECM), a complex structure of secreted macromolecules that surrounds mammalian organs and tissues. Integrins clustered on the extracellular side of focal adhesions signal from the ECM to intracellular protein complexes, which in turn signal to the actin cytoskeleton to regulate the tension needed for cell motility. Internal signals also converge on focal adhesions to regulate integrin affinity and avidity. Signaling through focal adhesions regulates cell adhesion, migration, proliferation, apoptosis, and gene expression, and impacts cellular processes such as development, wound healing, immune response, invasion, metastasis, and angiogenesis (reviewed in 1-3). Talin is a large, multidomain focal adhesion protein that interacts with the intracellular domains of integrins and other focal adhesion proteins. Talin is involved in the formation of focal adhesions and in linking focal adhesions to the actin cytoskeleton (4). The interaction between talin and integrins increases the affinity between integrin and both insoluble and soluble ECM proteins (5,6).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: OX40 (TNFRSF4, CD134) is a member of the tumor necrosis factor (TNF) receptor superfamily that regulates T cell activity and immune responses. The OX40 protein contains four cysteine rich domains, a transmembrane domain, and a cytoplasmic tail containing a QEE motif (1,2). OX40 is primarily expressed on activated CD4+ and CD8+ T-cells, while the OX40 ligand (OX40L, TNFSF4, CD252) is predominantly expressed on activated antigen presenting cells (3-7). The engagement of OX40 with OX40L leads to the recruitment of TNF receptor-associated factors (TRAFs) and results in the formation of a TCR-independent signaling complex. One component of this complex, PKCθ, activates the NF-κB pathway (2,8). OX40 signaling through Akt can also enhance TCR signaling directly (9). Research studies indicate that the OX40L-OX40 pathway is associated with inflammation and autoimmune diseases (10). Additional research studies show that OX40 agonists augment anti-tumor immunity in several cancer types (11,12).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: MEF2A is a member of the MEF2 (myocyte enhancer factor 2) family of transcription factors. In mammals, four MEF2A-related genes (MEF2A, MEF2B, MEF2C and MEF2D) encode proteins which exhibit significant amino acid sequence similarity within their DNA binding domains and to a lesser extent throughout the remaining proteins (1). The MEF2 family members were originally described as muscle-specific DNA binding proteins that recognize MEF2 motifs found within the promoters of many muscle-specific genes (2,3). Phosphorylation of MEF2A at Thr312 and Thr319 within the transcription activation domain by p38 MAP kinase enhances MEF2A-MEF2D heterodimer-dependent gene expression (4). On the other hand, apoptotic stimuli (e.g. neurotoxic insult) result in CDK5-dependent phosphorylation of MEF2A at Ser408 within the activation domain, inhibiting MEF2A pro-survival function (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CDC73 (HPRT2) is a putative tumor suppressor protein thought to bind RNA polymerase II to help inhibit cell cycle progression (1,2). Commonly referred to as parafibromin, CDC73 is expressed in endocrine tissues, kidney, heart, and skeletal muscle and is localized to both nuclear and cytoplasmic compartments (3). CDC73 acts as a Wnt signaling regulator as it binds the carboxy-terminal region of β-catenin (4). Mutations in the corresponding gene cause an endocrine disorder known as hyperparathyroidism 2, which is characterized by hypercalcemia, bone resorption, and the development of jaw tumors (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Neuronal Cell Adhesion Molecule, or NRCAM, belongs to the immunoglobulins Cell Adhesion Molecules (CAM's) superfamily (1). NRCAM, an ankyrin-binding protein, contributes to the neurite outgrowth by providing directional signaling during axonal cone growth (2, 3, 4). Additionally, it plays a role in mediating the interaction between axons and Schwann cells and contributes to the formation and maintenance of Nodes of Ranvier (5, 6, 7, 8). NRCAM also plays an important role in the establishment of dendritic spines in developing cortical neurons (9). NRCAM is expressed in non-neuronal cells, mostly in endothelial cells (10).

$262
3 nmol
300 µl
SignalSilence® DDX5 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit DDX5 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interferons (IFNs) appear both locally and systematically early after viral infection and participate in limiting the spread of infection. They also affect cell differentiation, growth, surface antigen expression and immunoregulation (1). There are three naturally occurring interferons: α, β and γ. IFN-α is derived from lymphoblastic tissue and has a number of therapeutic applications in the treatment of various human cancers and diseases of viral origin. Recombinant IFN-α from both natural and synthetic genes binds to a common cell surface receptor and induces antiviral activity in a variety of cell lines. When binding to discrete cell surface receptors on target cells, IFN-α induces rapid changes in Jak/Stat phosphorylation, which initiates the Jak/Stat signaling pathway (2). IFN-α signaling also involves production of DAG without an increased intracellular free calcium concentration and the subsequent activation of calcium-independent isoforms of PKC (β and ε) (3). All IFN-α signaling pathways lead to final alterations of gene expression, which mediate their pleiotropic biologic activities.

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated β-Tubulin (D2N5G) Rabbit mAb #15115.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: The synthetic compound dinitrophenol (DNP) is a small hapten molecule that can be conjugated to proteins for use in immunoassays (1). Antibodies that recognize dinitrophenol will display strong binding affinity to DNP conjugated molecules, including nucleic acids and proteins. These DNP-conjugated compounds can be used in in situ hybridization, western, northern, and Southern blotting (1,2). Dinitrophenol is a commonly used insecticide and has been used as a treatment for weight loss (3).

$262
3 nmol
300 µl
SignalSilence® BRCA1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit BRCA1 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).

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

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum resident protein 44 (ERp44), constitute the PDI family (2). ERp44 is induced upon ER stress and is linked to Ero1-Lα and Ero1-Lβ through mixed disulfide bonds (3). ERp44 was shown to mediate the ER localization of Ero1-Lα (4).