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Product listing: DYKDDDDK Tag (D6W5B) Rabbit mAb (HRP Conjugate) #86861 to Mios (D12C6) Rabbit mAb, UniProt ID Q9NXC5 #13557

$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 DYKDDDDK Tag (D6W5B) Rabbit mAb #14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

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.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin is a major hormone controlling critical energy functions, such as glucose and lipid metabolism. Insulin binds to and activates the insulin receptor (IR) tyrosine kinase, which phosphorylates and recruits adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of the Glut4 glucose transporter from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt Ser/Thr kinase (AS160, TBC1D4) is a Rab GTPase-activating protein that regulates insulin-stimulated Glut4 trafficking. AS160 is expressed in many tissues including brain, kidney, liver, and brown and white fat (2). Multiple Akt phosphorylation sites have been identified on AS160 in vivo, with five sites (Ser318, Ser570, Ser588, Thr642, and Thr751) showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrate that insulin-stimulated phosphorylation of AS160 is a crucial step in Glut4 translocation (3) and is reduced in some patients with type 2 diabetes (4). The interaction of 14-3-3 regulatory proteins with AS160 phosphorylated at Thr642 is a necessary step for Glut4 translocation (5). Phosphorylation of AS160 by AMPK is involved in the regulation of contraction-stimulated Glut4 translocation (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, 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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Son of sevenless (SOS) was first identified in Drosophila as a guanine nucleotide exchange factor (GEF) for Ras acting downstream of the Sevenless receptor (1). Two closely related homologs of Drosophila SOS are found in mammalian cells: SOS1 and SOS2 (2). SOS1 consists of histone folds, Dbl (DH) and pleckstrin (PH) homology domains, a Ras exchange motif (REM), and Cdc25 homology and polyproline domains (3). SOS1 binds to GRB2, NCK, and other adaptor proteins, and plays an important role in ERK activation downstream of protein tyrosine kinase receptor (RTK). Research studies have identified mutations in the corresponding SOS1 gene of patients with Noonan syndrome, a developmental disorder characterized by short stature, facial dysmorphia, and congenital heart defects (4,5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Stathmin is a ubiquitously expressed microtubule destabilizing phosphoprotein that is upregulated in a number of cancers. The amino terminus of the protein contains multiple phosphorylation sites and is involved in the promotion of tubulin filament depolymerization. Phosphorylation at these sites inactivates the protein and stabilizes microtubules. Ser16 phosphorylation by CaM kinases II and IV (1,2) increases during G2/M-phase and is involved in mitotic spindle regulation (3,4). Ser38 is a target for cdc2 kinase (5) and TNF-induced cell death gives rise to reactive oxygen intermediates leading to hyperphosphorylation of stathmin (6). EGF receptor activation of Rac and cdc42 also increases phosphorylation of stathmin on Ser16 and Ser38 (7). Other closely related family members are neuronally expressed and include SCG10, SCLIP, RB3 and its splice variants RB3' and RB3''. Stathmin and SCG10 have been shown to play roles in neuronal-like development in PC-12 cells (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Bid is a pro-apoptotic “BH3 domain-only” member of the Bcl-2 family originally discovered to interact with both the anti-apoptotic family member Bcl-2 and the pro-apoptotic protein Bax (1). Bid is normally localized in the cytosolic fraction of cells as an inactive precursor and is cleaved at Asp60 by caspase-8 during Fas signaling, leading to translocation of the carboxyl terminal p15 fragment (tBid) to the mitochondrial outer membrane (2-4). Translocation of Bid is associated with release of cytochrome c from the mitochondria, leading to complex formation with Apaf-1 and caspase-9 and resulting in caspase-9 activation (5-7). Thus, Bid relays an apoptotic signal from the cell surface to the mitochondria triggering caspase activation (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Members of the SALL gene family encode putative zinc finger transcription factors highly expressed during development (1). Sall4 is expressed very early in development with other pluripotency regulators, such as Oct-4 and Nanog (2). Recent studies suggest Sall4 works as a master regulator that controls its own expression and the expression of Oct-4 in a transcriptional regulation feedback loop governing stem cell pluripotency and stem cell fate (2,3). Immunohistochemical studies indicate that Sall4 is a sensitive and specific diagnostic marker for primary germ cell tumors and yolk sac tumors (4,5). Research studies have shown that Sall4 is constitutively expressed in acute myeloid leukemia (AML) and is a probable effector of the Wnt/β-catenin signaling pathway in this disease (6). In addition, mutations in Sall4 have been implicated in human malformation syndromes including Duane-radial ray syndrome (Okihiro syndrome) and Acro-renal-ocular syndrome (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: TAK1 is a mitogen-activated protein kinase kinase kinase activated by TGF-β and various pro-inflammatory signals (1,2). In vivo, TAK1 activation requires its association with TAK1 binding protein 1 (TAB1), which triggers TAK1 autophosphorylation at Thr184 and Thr187 (3,4). The TAB2 adaptor protein links TAK1 with TRAF6 to mediate TAK1 activation following IL-1 stimulation (5). Once activated, TAK1 phosphorylates the MAPK kinases MKK4 and MKK3/6, which activate JNK and p38 MAPK, respectively. TAK1 and TRAF6 also activate the NF-κB pathway by phosphorylating the NF-κB inducing kinase (NIK) to trigger subsequent activation of IKK (2,6). In addition to TAK1, TAB1 interacts with and activates p38α MAPK (7). Targeted disruption of the TAB1 gene in mice causes a drastic reduction in TAK1 activity and leads to embryonic lethality (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Forkhead box protein A2 (FoxA2, also known as hepatocyte nuclear factor 3β or HNF3β) is a transcription factor that plays an important role in hepatocyte function (1). FoxA2/HNF3β is required for the activation of hepatic gluconeogenic gene expression during fasting (1). Together with the PGC-1β coactivator, FoxA2/HNF3β stimulates the expression of genes involved in fatty acid β-oxidation and therefore increases fatty acid metabolism (2). FoxA2/HNF3β, along with PGC-1β, also activates the expression of microsomal triacylglycerol transfer protein (MTP) and promotes VLDL secretion (2). In addition to its roles in metabolic syndromes, FoxA2/HNF3β is essential for development of the endoderm and midline structures in mouse embryos (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The protein folliculin (FLCN) is encoded by the BHD (Birt-Hogg-Dube) gene that is altered in BHD Syndrome, a disorder characterized by the presence of benign connective tissue tumors known as fibrofolliculomas, renal tumors and lung cysts (1). Clinical similarities between BHD and hamartoma-producing disorders caused by Tsc2, PTEN and LKB1 gene mutations indicate that FLCN might also be important in nutrient and energy sensing through the mTOR pathway (2). This model is supported by studies demonstrating a direct correlation between the down regulation of BHD and a reduction in mTOR associated phosphorylation of S6 ribosomal protein (3). Mutation of either the TSC1 or TSC2 gene results in elevated mTOR activity (4) while deletion of the Tsc2 and BHD homologs in yeast have opposing effects on both mTOR signaling and amino acid homeostasis (5). BHD knock-out mice develop cysts and renal cell tumors similar to those found in BHD patients along with low levels of phosphorylated S6 ribosomal protein (3). Based on these finding, it appears that either abnormally high or abnormally low levels of mTOR signaling might contribute to renal cell carcinogenesis.

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The c-Cbl proto-oncogene is a ubiquitously expressed cytoplasmic adaptor protein that is especially predominant in hematopoietic cells (1,2). c-Cbl is rapidly tyrosine-phosphorylated in response to stimulation of a variety of cell-surface receptors and becomes associated with a number of intracellular signaling molecules such as protein tyrosine kinases, phosphatidylinositol-3 kinase, Crk, and 14-3-3 proteins (3,4). c-Cbl possesses a highly conserved amino-terminal phosphotyrosine binding domain (TKB) and a C3HC4 RING finger motif. The TKB recognizes phosphorylated tyrosines on activated receptor tyrosine kinases (RTKs) as well as other nonreceptor tyrosine kinases. The RING finger motif recruits ubiquitin-conjugating enzymes. These two domains are primarily responsible for the ubiquitin ligase activity of c-Cbl and downregulation of RTKs (3). Research studies have indicated that in human cancer tissues, c-Cbl is frequently tyrosine-phosphorylated in a tumor-specific manner (5). Phosphorylation of Tyr731 of c-Cbl provides a docking site for downstream signaling components such as p85 and Fyn (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Serine hydroxymethyltransferases 1 and 2 (SHMT1, SHMT2) are cytoplasmic and mitochondrial serine hydroxylmethyltransferases, respectively (1,2). They catalyze the conversion of serine to glycine with the transfer of β-carbon from serine to tetrahydrofolate (THF) to form 5, 10-methylene-THF (1, 2). Research studies indicate that SHMT1 hemizygosity is associated with higher risk of intestinal cancer in mice of a certain genetic background (3). Suppression of SHMT2 was shown to block cell proliferation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromatosis 2 (NF2) is an autosomal dominant, inherited disorder characterized by the occurrence of vestibular schwannomas, meningiomas, and other nervous system tumors. Both the familial tumors of NF2 and equivalent sporadic tumors found in the general population are caused by inactivation of the NF2 tumor suppressor gene. Merlin (moesin, ezrin, and radixin-like protein) is the NF2 gene product, displaying striking similarity to ezrin, radixin, and moesin (ERM) proteins. Regulation of merlin (also called schwannomin) and ERM proteins involves intramolecular and intermolecular head-to-tail associations between family members (1). Merlin and ERM proteins act as linkers between the plasma membrane and the cytoskeleton, affecting cell morphology, polarity, and signal transduction (2). Merlin is phosphorylated by the Rac/Cdc42 effector p21-activated kinase (PAK) at Ser518, negatively regulating Rac (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The hematopoietic cell kinase (Hck) is a Src family protein tyrosine kinase that is prominently expressed in lymphoid and myeloid lineages of hematopoiesis (1). The Hck kinase participates in transduction of a variety of extracellular signals that affect cellular processes, including cell proliferation, differentiation, and migration. Hck protein structure includes a relatively divergent amino-terminal "unique" domain that is subject to post-translational lipid modifications and targets Hck to the plasma membrane. Src homology 3 (SH3) and 2 (SH2) domains, and a tyrosine kinase catalytic domain are adjacent to the "unique" domain. Research studies indicate that phosphorylation of conserved tyrosine residues positively and negatively regulate Hck catalytic activity. Phosphorylation of Hck at the conserved, carboxy-terminal Tyr499 by protein kinase Csk promotes an interaction between the phosphorylated tyrosine and the SH2 domain, rendering Hck inactive. Disruption of this interaction through dephosphorylation, the replacement of the Tyr522 with phenylalanine, or carboxy-terminal truncation mutations, results in constitutive activation of Hck. Autophosphorylation of Tyr411 within the kinase domain positively regulates Hck catalytic activity. Thus, the activation of Hck requires both disruption of the regulatory tyrosine-SH2 domain interaction and autophosphorylation of the regulatory tyrosine residue within the kinase domain (2,3). The dysfunction or dysregulation of Hck may contribute to the pathogenesis of some human forms of leukemia (4).

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

Application Methods: Western Blotting

Background: Ribosomal protein L5 (RPL5) is one of several proteins that comprise the 60S ribosomal subunit. RPL5 binds 5S rRNA and the nucleolar RPL11 protein to form the 5S ribonucleoprotein particle (RNP) that is incorporated into the large 60S ribosomal subunit (1). An RP-MDM2-p53 protein complex that contains ribosomal proteins RPL5, RPL11, and RPL23 acts as a nucleolar stress sensor that binds and inhibits MDM2 ubiquitin ligase activity and enhances p53-mediated transcriptional activity (2,3). RPL5 cooperates with RPL11 to influence ribosome biogenesis through regulating expression of the transcription factor c-Myc, which acts as the master regulator of ribosome biogenesis (4). Mutations in the corresponding RPL5 gene are associated with Diamond-Blackfan anemia, which is a form of red blood cell aplasia, and some cases of pediatric T-cell acute lymphoblastic leukemia (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Poly (ADP-ribose) glycohydrolase (PARG) is an enzyme that hydrolyzes poly (ADP-ribose) (PAR) formed by members of the PAR polymerase (PARP) enzyme family. Poly (ADP)-ribosylation is a post-translational modification that is catalyzed by PARP proteins. This modification involves polymerization of ADP-ribose from NAD+ to target proteins, such as histones and transcription factors, and plays a wide range of biological roles, including the response to DNA damage and transcriptional regulation (1,2). The mammalian PARG enzyme that catalyzes the removal of this modification exists as multiple isoforms. Longer PARG isoforms (100-110 kDa) shuttle between the nucleus and cytoplasm and are responsible for most of the PARG activity. The smaller (65 kDa) isoform resides in the cytoplasm (3-5). Research studies link altered PAR metabolism to inflammatory and autoimmune diseases, as well as neuronal degeneration (6-8). PARG inhibitors that increase PAR levels may sensitize cells to cancer treatments (e.g., cisplatin) and may help in the development of cancer therapies (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Helios (Ikaros family zinc finger 2, IZKF2) is an Ikaros family transcription factor composed of several zinc fingers that mediate DNA binding and homodimerization or heterodimerization with other Ikaros family proteins (1,2). In the hematopoietic system, Helios expression is restricted to T cells and early hematopoietic progenitors (1,2). In regulatory T cells, expression of Helios contributes to an anergic phenotype by binding to the IL-2 promoter and suppressing IL-2 transcription (3). In addition, alteration of the corresponding Helios gene IZKF2 is one hallmark of low-hypodiploid acute lymphoblastic leukemia (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: hnRNP E1 is a member of the hnRNP family of proteins that are involved in pre-mRNA processing and mRNA export, localization, stability, and translation (1-6). hnRNP E1 exerts a wide range of biological functions, such as transcriptional activation of mouse MOR gene expression (7), attenuation of alternative splicing of GHR pseudoexon expression (8), stabilization of collagen I and II (9), beta-globin (10), and androgen receptor (11) mRNAs, and regulation of translation of various genes including Dab2, ILEI, and Bag-1 (12,13). hnRNP E1 is ubiquitously expressed. Phosphorylation of hnRNP E1 affects its RNA binding affinity (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), 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

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), 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
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The stress-activated protein kinase/Jun-amino-terminal kinase SAPK/JNK is potently and preferentially activated by a variety of environmental stresses including UV and gamma radiation, ceramides, inflammatory cytokines, and in some instances, growth factors and GPCR agonists (1-6). As with the other MAPKs, the core signaling unit is composed of a MAPKKK, typically MEKK1-MEKK4, or by one of the mixed lineage kinases (MLKs), which phosphorylate and activate MKK4/7. Upon activation, MKKs phosphorylate and activate the SAPK/JNK kinase (2). Stress signals are delivered to this cascade by small GTPases of the Rho family (Rac, Rho, cdc42) (3). Both Rac1 and cdc42 mediate the stimulation of MEKKs and MLKs (3). Alternatively, MKK4/7 can be activated in a GTPase-independent mechanism via stimulation of a germinal center kinase (GCK) family member (4). There are three SAPK/JNK genes each of which undergoes alternative splicing, resulting in numerous isoforms (3). SAPK/JNK, when active as a dimer, can translocate to the nucleus and regulate transcription through its effects on c-Jun, ATF-2, and other transcription factors (3,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutamate-ammonia ligase (GLUL), also known as glutamine synthetase (GS), catalyzes the de novo synthesis of glutamine from glutamate and ammonia. GLUL is ubiquitously expressed with particularly high expression in the muscle, liver, and brain (1). GLUL expression is elevated in various cancers. Its expression is upregulated by oncogenic c-Myc (2). High expression of GLUL in breast cancer patients is associated with larger tumor size and high level of HER2 expression. It is a predictor of poor survival in patients with glioma and liver cancers (3-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Nicotinamide phosphoribosyltransferase (NAMPT; also known as Pre-B cell-enhancing factor PBEF) catalyzes the synthesis of nicotinamide mononucleotide (NMN) from nicotinamide and 5-phosphoribosylpyrophosphate (PRPP), the rate-limiting step in the NAD biosynthesis pathway starting from nicotinamide (1,2). NAD biosynthesis mediated by NAMPT plays a critical role in glucose-stimulated insulin secretion in pancreatic beta cells (3). Both NAMPT inhibitors and activators have been sought for clinical applications (4,5). NAMPT has intra- and extracellular forms (iNAMPT and eNAMPT), and deacetylation of iNAMPT by SIRT1 promotes eNAMPT secretion through a nonclassical secretory pathway (3,6). eNAMPT, independent of its enzymatic activity, can induce epithelial-to-mesenchymal transition in mammary epithelial cells and promote monocyte differentiation into a tumor-supporting M2 macrophage (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Syk family protein tyrosine kinase Zap-70 is expressed in T and NK cells and plays a critical role in mediating T cell activation in response to T cell receptor (TCR) engagement (1). Following TCR engagement, Zap-70 is rapidly phosphorylated on several tyrosine residues through autophosphorylation and transphosphorylation by the Src family tyrosine kinase Lck (2-6). Tyrosine phosphorylation correlates with increased Zap-70 kinase activity and downstream signaling events. Expression of Zap-70 is correlated with disease progression and survival in patients with chronic lymphocytic leukemia (7,8).

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

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

Background: The ezrin, radixin, and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling, and microvilli formation (1). ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers (2). Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin) disrupts the amino- and carboxy-terminal association and may play a key role in regulating ERM protein conformation and function (3,4). Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogene-induced transformation (5). Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Western Blotting

Background: Vav proteins belong to the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho/Rac small GTPases. The three identified mammalian Vav proteins (Vav1, Vav2 and Vav3) differ in their expression. Vav1 is expressed only in hematopoietic cells and is involved in the formation of the immune synapse. Vav2 and Vav3 are more ubiquitously expressed. Vav proteins contain the Dbl homology domain, which confers GEF activity, as well as protein interaction domains that allow them to function in pathways regulating actin cytoskeleton organization (reviewed in 1). Phosphorylation stimulates the GEF activity of Vav protein towards Rho/Rac (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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