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Product listing: MetAP2 (D3I1H) Rabbit mAb, UniProt ID P50579 #12547 to Enolase-2 Antibody, UniProt ID P09104 #9536

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

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 2 (eIF2)-associated glycoprotein, p67/methionine aminopeptidase 2 (MetAP2) is one of the three known MetAPs responsible for the co-translational processing of the N-terminal initiator methionine from nascent proteins in cells. MetAP2 regulates the rates of global protein synthesis by controlling the levels of eIF2α phosphorylation (1). MetAP2 has also been shown to bind Erk1/2 to inhibit their activation and activity, thus connecting the protein synthesis machinery with the cell signaling pathway mediated by Erk1/2 MAP kinases (2-4). Although MetAP2 is characterized as having aminopeptidase activity that removes the N-terminal methionine from nascent peptides in vitro, mounting evidence suggests that MetAP2 has no methionine aminopeptidase activity. Rather, MetAP2 possesses auto-proteolytic activity that can be inhibited by several small molecule inhibitors including anti-angiogenic drugs, fumagillin and its derivatives (5). It has also been demonstrated that O-GlcNAcylation of MetAP2 plays a major role in its stability, eIF2α binding, and maintenance of eIF2α phosphorylation (6).MetAP2 knockout mice show embryonic lethality, suggesting its role in embryonic development and survival at the initiation of gastrulation (7). It is likely that lowering the levels of MetAP2 in mammalian cells causes cell growth inhibition and leads to apoptosis due to the high levels of eIF2α phosphorylation that inhibits global protein synthesis (8). During pathological or various stress conditions, MetAP2 dissociates from eIF2 subunits possibly due to its deglycosylation-induced autoproteolytic cleavage. As a result, eIF2α becomes hyperphosphorylated and global protein synthesis is inhibited. eIF2 complex-dissociated MetAP2 also displays a higher affinity toward Erk1/2, which results in the blockade of Erk1/2 activity. Thus, MetAP2 mediates cooperation between cell signaling and protein synthesis machinery to regulate cell growth and proliferation during physiological and pathological conditions (9). Research studies have shown higher expression of MetAP2 in human cancers, supporting the contention that MetAP2 plays a role in oncogenesis. For example, investigators have reported high MetAP2 expression in follicular lymphomas, large B-cell lymphomas, and Burkitt's lymphomas (10). Elevated expression of MetAP2 has also been reported in human colorectal adenocarcinomas (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: BACH1, also known as BRIP1 and FANCJ, is a DNA helicase involved in repair of DNA cross-links and double strand breaks (1-3). Interaction between phosphorylated BACH1 and BRCA1 is required for DNA damage-induced checkpoint signaling (3,4). Originally identified as a breast cancer susceptibility gene (1), the BACH1 gene is mutated in Fanconi anemia (5), a recessive disorder characterized by multiple congenital abnormalities, progressive bone marrow failure, and high cancer risk/predisposition. Research investigators have concluded that BACH1 interactions with BRCA1 and the presence of BACH1 mutations in patients with early onset breast cancer indicate that BACH1 may act as a tumor suppressor (6).Phosphorylation of BACH1 at Thr1133 is thought to be involved in regulation of the replication checkpoint and is required for the interaction of BACH1 with TopBP1 (7).

$260
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).

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

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

Background: JNK-Interacting Proteins (JIPs), as their name implies, coordinate c-Jun N-terminal Kinase (JNK) signaling by acting as scaffolds for components of the JNK signaling cascade (1). JIPs localize and promote JNK activation in response to stress by amalgamating and co-localizing upstream kinases and downstream effectors in the stress-kinase pathway analogous to the mechanism by which AKAPs orchestrate PKA signaling. JIPs bind to an array of MAPKs and other signaling proteins, including the mixed-lineage kinases, MKK7, p38α MAPK, JNK1-3, Max, Myc, NF-κB, LRRK2, and others (1-4).There are four known JIPs, JIP1-4, of which JIP1 and JIP2 share extensive sequence homology and domain structure. JIP1 and JIP2 are mainly expressed in neurons, testis and in β pancreatic cells, where they have been implicated in cellular responses to metabolic stress, the development of diabetes, and post-traumatic brain damage (5-7). Although architecturally distinct from JIP1 and JIP2, JIP3 and JIP4 share some overlapping functions and are more broadly expressed. JIP4, encoded by the SPAG9 (sperm-associated antigen-9) gene, is a homooligomer that binds to and coordinates the activation of numerous components of the stress-activated kinase cascade including MEK4, MEKK3, p38α MAPK, and JNK1-3 (3,8). However, unlike the other JIP members, JIP4 does not appear to activate JNK directly, instead favoring stimulation of p38 MAPK signaling events in response to cellular stress (3,9).In addition to mediating stress responses, JIP4 (or its splice variant, JLP) has also been shown to interact with ARF6 and PIKfyve, thus regulating microtubule-based endosomal trafficking (10,11). There are extensive reports indicating that JIP4 is phosphorylated in response to stress (UV damage etc.) but it is unclear what effect, if any, this has on its function, localization, or binding properties (12-15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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

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

Application Methods: Western Blotting

Background: Phosphatidylinositol-5-phosphate 4-kinases (PIP4K) synthesize phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), a key precursor in phosphoinositide signaling that directly modulates the activity of signaling proteins and cellular processes. There are two subfamilies of PIP kinases, type I and II, that generate PtdIns(4,5)P2 from distinct substrate pools. PIP4 type I kinases use PtdIns5P as a substrate, whereas PIP5 type II kinases use PtdIns4P (1,2). In mammalian cells, three isoforms of each PIP4K and PIP5K subfamily, encoded by distinct genes, have been characterized (3-7). All PIP kinases are stimulated by phosphatidic acid, extensively regulated by ARF and Rho GTPases, and inhibited by protein kinase A and PI-stimulated autophosphorylation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: P2X purinergic receptors are ATP-gated ion channels involved in physiological processes that include inflammation, afferent sensory signaling, and sympathetic motor nerve activity. Seven different vertebrate genes (P2RX1-P2RX7) encode for individual receptor protein subunits (1). All P2X subunit proteins share similar protein domain structure, but can differ in overall protein length from 384 to 595 amino acids. Each P2X subunit is composed of amino- and carboxy-terminal intracellular domains, two transmembrane domains, and a large extracellular loop that contains ten evenly spaced cysteines and multiple glycosylation sites (2). P2X receptors are found in a variety of cell types and tissues, including central and peripheral nervous system neurons and glial cells, autonomic and sensory neurons, bone, muscle, and hematopoietic tissues (1).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Cortactin is a cortical actin binding protein. Its amino-terminal acidic domain (NTA) associates with the Arp2/3 and WASP complex at F-actin branches. The central region of the protein contains six repeats of 37 amino acids that are important in F-actin binding and cross-linking. The carboxy-terminus contains a proline-rich region and an SH3 domain that can interact with numerous scaffolding proteins, such as CortBP1 and Shank3 (1,2). Cortactin is involved in signaling events that coordinate actin reorganization during cell movement. The human cortactin homologue EMS1 is overexpressed in numerous cancers with poor patient prognosis (3). Cortactin may also play an important role in the organization of transmembrane receptors at postsynaptic densities (PSD) and tight junctions by linking scaffolding proteins to the actin network (4).Cortactin is phosphorylated at tyrosine residues 421, 466, and 482. Tyrosine phosphorylation of cortactin regulates cell motility (5), rac1-mediated actin dynamics (6), cadherin-dependent adhesion (7), chemokine trafficking and chemokine-dependent chemotaxis (8).

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

Application Methods: Western Blotting

Background: Phosphoglycerate mutase (PGAM1) catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis (1-5). Research studies have shown increased PGAM1 expression in cancer (1-4) and mental disease (5). Specifically, PGAM1 was shown to be phosphorylated at His11 by phosphoenolpyruvate (PEP) in PKM2-expressing cells, suggesting a possible regulatory role for PGAM1 in actively proliferating cells via an alternative glycolytic pathway (1).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

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

Background: Protein phosphatase type 2A (PP2A) is an essential protein serine/threonine phosphatase that is conserved in all eukaryotes. PP2A is a key enzyme within various signal transduction pathways as it regulates fundamental cellular activities such as DNA replication, transcription, translation, metabolism, cell cycle progression, cell division, apoptosis and development (1-3). The core enzyme consists of catalytic C and regulatory A (or PR65) subunits, with each subunit represented by α and β isoforms (1). Additional regulatory subunits belong to four different families of unrelated proteins. Both the B (or PR55) and B' regulatory protein families contain α, β, γ and δ isoforms, with the B' family also including an ε protein. B'' family proteins include PR72, PR130, PR59 and PR48 isoforms, while striatin (PR110) and SG2NA (PR93) are both members of the B''' regulatory protein family. These B subunits competitively bind to a shared binding site on the core A subunit (1). This variable array of holoenzyme components, particularly regulatory B subunits, allows PP2A to act in a diverse set of functions. PP2A function is regulated by expression, localization, holoenzyme composition and post-translational modification. Phosphorylation of PP2A at Tyr307 by Src occurs in response to EGF or insulin and results in a substantial reduction of PP2A activity (4). Reversible methylation on the carboxyl group of Leu309 of PP2A has been observed (5,6). Methylation alters the conformation of PP2A, as well as its localization and association with B regulatory subunits (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Hexamethylene bis-acetamide-inducible protein 1 (HEXIM1) was originally identified in vascular smooth muscle cells as a protein that is upregulated upon treatment with the differentiating agent hexamethylene bisacetamide (1). HEXIM1 binds 7SK RNA, a highly abundant non-coding RNA, and together they act as a potent inhibitor of positive transcription elongation factor b (P-TEFb) (2,3). P-TEFb phosphorylates the C-terminal domain of the largest subunit of RNA polymerase II and is an important regulator of transcription elongation (4-8). 7SK RNA-bound HEXIM1 interacts with the cyclin T1 subunit of P-TEFb, sequestering P-TEFb in an inactive form leading to transcription inhibition (2,3). The regulation of the relative ratio of inactive to active P-TEFb in the cell by HEXIM1/7SK RNA is thought to play a critical role in regulation of a wide range of cellular gene expression programs such as estrogen and glucocorticoid receptor regulated genes (9-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Notch proteins (Notch1-4) are a family of transmembrane receptors that play important roles in development and the determination of cell fate (1). Mature Notch receptors are processed and assembled as heterodimeric proteins, with each dimer comprised of a large extracellular ligand-binding domain, a single-pass transmembrane domain, and a smaller cytoplasmic subunit (Notch intracellular domain, NICD) (2). Binding of Notch receptors to ligands of the Delta-Serrate-Lag2 (DSL) family triggers heterodimer dissociation, exposing the receptors to proteolytic cleavages; these result in release of the NICD, which translocates to the nucleus and activates transcription of downstream target genes (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Interferon regulatory factors (IRFs) comprise a family of transcription factors that function within the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in pathogen defense, autoimmunity, lymphocyte development, cell growth, and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, IRF-9/ISGF3γ, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7, and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA-binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA-binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS), and IFN regulatory elements (IRF-E) (2).

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

Application Methods: Western Blotting

Background: The DEAD box family of RNA helicases is characterized in part by a common D-E-A-D amino acid motif. The family is composed of a growing number of proteins found in a wide range of organisms from bacteria to mammals. DEAD helicases have distinct biological functions in RNA metabolism and ribonucleoprotein (RNP) processing (reviewed in 1,2).DDX3 is a DEAD box family RNA helicase with diverse cellular functions. DDX3 is required for nuclear export of HIV-1 viral transcripts, possibly in a complex with the viral Rev protein and host cofactor CRM1 (3). DDX3 is required for hepatitis C virus (HCV) RNA replication (4) and its expression is downregulated in hepatitis B virus (HBV) associated hepatocellular carcinoma (HCC) (5).Recent evidence suggests that DDX3 functions as a tumor suppressor protein. Its expression inhibits tumor cell colony formation and increases expression of the cdk inhibitor p21 Waf1/Cip1. Low DDX3 expression has been shown in HCC (5,6), and aberrant subcellular localization occurs in many squamous cell carcinomas (6). Reduced DDX3 expression in cultured cells causes a diminished dependence on serum for cell proliferation and changes in cyclin D1 and p21 Waf1/Cip1 expression (5).DDX3 is phosphorylated at Thr204 and Thr323 by the mitotic cyclin dependent kinase, cyclin B/cdc2. This phosphorylation is thought to cause a loss of DDX3 function and a concomitant repression of ribosome biogenesis and translation in mitosis (7).

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

Application Methods: Western Blotting

Background: The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways (1,2). 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms, β, γ, ε, σ, ζ, τ, and η that have been identified in mammals. The initially described α and δ isoforms are confirmed to be phosphorylated forms of β and ζ, respectively (3). Through their amino-terminal α helical region, 14-3-3 proteins form homo- or heterodimers that interact with a wide variety of proteins: transcription factors, metabolic enzymes, cytoskeletal proteins, kinases, phosphatases, and other signaling molecules (3,4). The interaction of 14-3-3 proteins with their targets is primarily through a phospho-Ser/Thr motif. However, binding to divergent phospho-Ser/Thr motifs, as well as phosphorylation independent interactions has been observed (4). 14-3-3 binding masks specific sequences of the target protein, and therefore, modulates target protein localization, phosphorylation state, stability, and molecular interactions (1-4). 14-3-3 proteins may also induce target protein conformational changes that modify target protein function (4,5). Distinct temporal and spatial expression patterns of 14-3-3 isoforms have been observed in development and in acute response to extracellular signals and drugs, suggesting that 14-3-3 isoforms may perform different functions despite their sequence similarities (4). Several studies suggest that 14-3-3 isoforms are differentially regulated in cancer and neurological syndromes (2,3).

The Loading Control Antibody Sampler Kit provides an economical means to detect a variety of housekeeping proteins. The kit contains enough primary and secondary antibodies to perform two western blot experiments.
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Phosphoinositide-3,4,5-triphosphate (PtdIns(3,4,5)P3)-dependent Rac exchanger 1 (PREX1) is a Rac-specific GTP-exchange factor (GEF) regulated by heterotrimeric G-protein β/γ subunits and the lipid second messenger PtdIns(3,4,5)P3 (1-4). PREX1 contains two DEP (Dishevelled, Egl-10, and Pleckstrin homology) domains that coordinate heterotrimeric G-protein signaling. It also contains a Dbl-homology domain, which exhibits Rac-GEF activity, and PH and PDZ domains for interacting with upstream and downstream signaling components (1). Originally shown to modulate cellular migration of neutrophils by Rac2 activation (5-8), it is clear that PREX1 plays a broader role in modulating cell migration. PREX1 promotes metastasis of prostate cancer and melanoma cells, affects endothelial junction integrity, and is required for platelet generation and function (9-14). Research studies suggest that PREX1 plays an essential role in mediating ErbB-dependent signaling events in breast cancer by coordinating Rac activation in response to paracrine signals within the tumor microenvironment. Activation of PREX1 downstream of ErbB3 and EGFR chemokine receptors (CXCR4) promotes Rac activation, increased migration, proliferation, tumorigenesis, and metastasis in breast cancer cells (15,16). Consistent with this observation, deletion of PREX1 expression in mice results in resistance to melanoma metastasis (11). Expression of PREX1 in human tumors transplanted into mice inversely correlates with increased tumor progression and poor survival (15). Additional research studies suggest that PREX Rac-GEF activity is enhanced by phosphorylation in response to growth factors or hormones, and may require coincident dephosphorylation of two PH domain serine residues. The upstream kinases and precise regulatory mechanism remains elusive (15,17).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Silent Information Regulator (Sir2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of this family is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT6, a mammalian homolog of Sir2, is a nuclear, chromatin-associated protein that promotes the normal maintenance of genome integrity mediated by the base excision repair (BER) pathway (2-4). The BER pathway repairs single-stranded DNA lesions that arise spontaneously from endogenous alkylation, oxidation, and deamination events. SirT6 deficient mice show increased sensitivity to DNA-damaging agents, including the alkylating agents MMS and H2O2 (2). In addition, these mice show genome instability with increased frequency of fragmented chromosomes, detached centromeres, and gaps (2). SirT6 may regulate the BER pathway by deacetylating DNA Polβ or other core components of the pathway (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: A20, also referred to as TNF-α-induced protein 3 (TNFAIP3), is cytokine-inducible protein that functions to inhibit apoptosis and activate NF-κB (1,2). It was first identified as a TNF-α inducible primary response gene in human umbilical vein endothelial cells, and encodes a 790-amino acid protein containing seven Cys2/Cys2-zinc finger motifs (3). Constitutive expression of A20 is observed in lymphoid tissues (4), but it is transiently expressed in a variety of cell types in response to inflammatory signals such as TNF-α (3,5), IL-1 (3,5), phorbol esters (6), and LPS (7). Expression of A20 can confer resistance to apoptosis and NF-κB activation triggered by these signals, probably through interference with TRAF (TNF receptor associated factor) family members (8,9), and interaction with the NF-κB inhibiting protein ABIN (10). Studies also show that A20 contains site-specific ubiquitin modifying activity that can contribute to its biological functions (11,12). The amino-terminus of A20 contains de-ubiquitinating (DUB) activity for Lys63 branches, such as those found in TRAF6 and RIP, while the carboxyl-terminus contains ubiquitin ligase (E3) activity for Lys48 branches of the same substrates and leads to their degradation (12).

SignalSilence® Akt siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Akt 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.

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Sigma non-opioid intracellular receptor 1 (SIGMAR1) is an endoplasmic reticulum (ER) membrane chaperone that forms raft-like microdomains on the ER, where it interacts with mitochondria at the mitochondria-associated ER membrane domain (MAM). At MAM, SIGMAR1 maintains proper ER-mitochondrion Ca2+ signaling, regulates mitochondria function, and enhances cellular survival upon ER stress (1-4). When activated, SIGMAR1 translocates to ER and plasma membrane, where it interacts with a plethora of membrane proteins, including ion channels, neurotransmitter receptors, and kinases. SIGMAR1 also modulates a variety of neuronal functions, such as neuronal excitability, neuroplasticity, neuroprotection, and neurorestoration (5-7). SIGMAR1 binds to many anti-psychotic drugs and it is implicated in addiction, pain, neurodegenerative diseases, and depression (8-11). Recently, mutations in the SIGMAR1 gene have been reported to be associated with amyotrophic lateral sclerosis (12,13). Besides its important roles in central nervous system and peripheral nervous system, SIGMAR1 also enhances cancer cell migration and invasion (14,15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors defined by the presence of a winged helix DNA binding domain called a Forkhead box (1). In humans, there are over 40 known Fox protein family members, divided into 19 subfamilies, which have evolved to regulate gene transcription in diverse and highly specialized biological contexts throughout development (2). Mutations that disrupt the expression of Fox gene family members have consequently been implicated in a broad array of human disorders, including immunological dysfunction, infertility, speech/language disorders, and cancer (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The mediator complex consists of about 25-30 proteins and is thought to facilitate transcription activation by acting as a molecular bridge between the RNA polymerase II (RNAPII) machinery and transcription factors (1). Mediator is recruited to target genes by transcription factors and plays an essential role in the recruitment and stabilization of the RNAPII transcription complex at promoters, as well as the activation of transcription post RNAPII recruitment (1-5). The mediator complex also plays an important role in creating ‘chromatin loops’ that occur as a result of interactions between the transcription factor bound at distal enhancers and RNAPII bound at the proximal promoter, and works to sustain proper chromatin architecture during active transcription (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Phosphoinositide-dependent protein kinase 1 (PDK1) plays a central role in many signal transduction pathways (1,2) including the activation of Akt and the PKC isoenzymes p70 S6 kinase and RSK (3). Through its effects on these kinases, PDK1 is involved in the regulation of a wide variety of processes, including cell proliferation, differentiation and apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The nuclear factor-like 2 (NRF2) transcriptional activator binds antioxidant response elements (ARE) of target gene promoter regions to regulate expression of oxidative stress response genes. Under basal conditions, the NRF2 inhibitor INrf2 (also called KEAP1) binds and retains NRF2 in the cytoplasm where it can be targeted for ubiquitin-mediated degradation (1). Small amounts of constitutive nuclear NRF2 maintain cellular homeostasis through regulation of basal expression of antioxidant response genes. Following oxidative or electrophilic stress, KEAP1 releases NRF2, thereby allowing the activator to translocate to the nucleus and bind to ARE-containing genes (2). The coordinated action of NRF2 and other transcription factors mediates the response to oxidative stress (3). Altered expression of NRF2 is associated with chronic obstructive pulmonary disease (COPD) (4). NRF2 activity in lung cancer cell lines directly correlates with cell proliferation rates, and inhibition of NRF2 expression by siRNA enhances anti-cancer drug-induced apoptosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Vasoactive intestinal polypeptide (VIP) is a neuropeptide synthesized as a precursor that is processed to an active mature peptide of 28 residues (1). VIP is produced by neurons, endocrine, and immune cells and is expressed in many tissues, in agreement with its various biological functions (2). VIP acts through activation of two receptors belonging to the G protein-coupled receptor family, VPAC1 and VPAC2 (2) and elicits several effects such as vasodilation, regulation of smooth muscle cell contractility, and blood flow in the gastrointestinal track (3,4). In addition, VIP is involved in the regulation of T cell differentiation (6), and in immunosuppression (7,8).

$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, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: BRCA1-Associated Protein 1 (BAP1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its amino-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its carboxy-terminal segment (1). Frequent gene locus rearrangement, deletion, and null mutation of BAP1 have been found in lung and breast cancers (1,2). In vivo mutation analysis of cancer cell line survival and animal tumorigenesis indicates that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinated BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the complex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinate HCF-1, thereby controlling its stability (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Enolase is a glycolytic enzyme that is involved in the conversion of 2-phosphoglycerate to phosphoenolpyruvate (1). Mammalian enolase has three subunits: α, β, and γ, that can form homo and heterodimers. Homodimers of γ enolase are neuronal-specific (2). Research studies have shown elevated levels of neuro-specific enolase-2 in neuroblastoma (2) and small-cell lung cancer (3,4).