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Product listing: Nischarin (D6T4X) Rabbit mAb, UniProt ID Q9Y2I1 #85124 to Rab3A (D7B10) Rabbit mAb, UniProt ID P20336 #12214

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Nischarin (also known as imidazoline receptor antisera-selected protein, IRAS) was first identified through its association with the cytoplasmic domain of integrin α5, and shown to regulate cell migration and cystoskeletal organization (1).Nischarin regulates Rac-1 signaling (2), as well as the p21-activated kinase (PAK) (3) and cofilin/LIMK pathways (4). Nischarin also interacts with LKB1, regulating the migration and metastatic behavior of breast epithelial cells (5). In addition, nischarin regulates neuronal migration in rat brain (6).Research studies have implicated nischarin in the regulation of invasion and metastasis of breast cancer (7,8). Researchers have shown that nischarin is frequently downregulated in ovarian cancer, and regulates invasion through focal adhesion kinase (FAK) signaling (9).

PTMScan® Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include phosphorylation (PhosphoScan®), ubiquitination (UbiScan®), acetylation (AcetylScan®), and methylation (MethylScan®), among others. PTMScan® Technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur. For more information on PTMScan® Proteomics Services, please visit www.cellsignal.com/services/index.html.

Background: Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 1 (SATB1) functions as both a global chromatin organizer and a gene-specific transcription factor (1). SATB1 cooperates with promyelocytic leukemia protein (PML) to regulate global chromatin architecture by organizing chromatin into distinct loops via periodic anchoring of matrix attachment regions (MARs) in DNA to the nuclear matrix (1-3). In addition, SATB1 recruits multiple chromatin-remodeling proteins that contribute to specific gene activation and repression, including the chromatin remodeling enzymes ACF and ISWI, the histone deacetylase HDAC1, and the histone acetyltransferases PCAF and p300/CBP (4-6). Phosphorylation of SATB1 on Ser185 by protein kinase C regulates its interaction with HDAC1 and PCAF. While unphosphorylated SATB1 binds to PCAF, phosphorylated SATB1 preferentially binds to HDAC1 (6). Acetylation of SATB1 on Lys136 by PCAF impairs its DNA binding activity, thereby removing SATB1 from gene promoters (6). SATB1 is expressed predominantly in thymocytes and is involved in gene regulation during T cell activation (1). SATB1 is also expressed in metastatic breast cancer cells and is a potential prognostic marker and therapeutic target for metastatic breast cancer (7). In a mouse model system, RNAi-mediated knockdown of SATB1 reversed tumorigenesis by inhibiting tumor growth and metastasis, while ectopic expression of SATB1 in non-metastatic breast cancer cells produced invasive tumors.

$489
96 assays
1 Kit
The PathScan® Phospho-mTOR (Ser2481) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of mTOR protein phosphorylated at Ser2481. A mTOR Mouse mAb has been coated onto the microwells. After incubation with cell lysates, mTOR (phospho and nonphospho) protein is captured by the coated antibody. Following extensive washing, Phospho-mTOR (Ser2481) Rabbit mAb is added to detect the captured phospho-mTOR protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of mTOR phosphorylated at Ser2481.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Tec kinase belongs to a structurally related subfamily of protein tyrosine kinases (PTKs) that includes Btk, Itk (also known as Emt or Tsk), Bmx, and Txk (or Rlk) (1). With the exception of Txk, the members of this subfamily possess a long amino-terminal region consisting of a pleckstrin homology (PH) domain and a Tec homology (TH) domain . Because PH domains bind phosphoinositides with high affinity, the Tec family kinases have been proposed to act downstream of phosphatidylinositol 3-kinase (PI3-kinase) in signaling pathways. Binding of the PH domain with phosphoinositides is probably required for targeting of Tec family kinases to the cell membrane (2). Tec kinase is activated in response to many upstream signaling events including antigen receptor, RTK, GPCR, and integrin stimulation (3,4). Activated Tec kinase directly phosphorylates substrates such as PLC-gamma 2 and BRDG1 docking protein (5) and mediates downstream signaling.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: DNA repair systems operate in all living cells to manage a variety of DNA lesions. Nucleotide excision repair (NER) is implemented in cases where bulky helix-distorting lesions occur, such as those brought about by UV and certain chemicals (1). Excision Repair Cross Complementing 4 (ERCC4, XPF) forms a complex with the ERCC1 excision repair protein to create an essential 5’ endonuclease responsible for lesion excision (2). ERCC1-XPF is also required for repair of DNA interstrand crosslinks (ICLs) (3) and involved in repair of double strand breaks (4). Mutations in the corresponding XPF gene cause specific forms of xeroderma pigmentosum, Cockayne syndrome, and Fanconi anemia, while altered XPF protein levels may be associated with disease progression and response to treatment in specific human cancers (5,6).

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

Application Methods: Western Blotting

Background: Transformation/transcription domain-associated protein (TRRAP) is a highly conserved 434 kDa protein found in various multiprotein complexes, such as SAGA, PCAF, NuA4 and TIP60, which contain histone acetyltransferase (HAT) activity (1-4). TRRAP functions as an adaptor protein by binding directly to the transactivation domains of transcriptional activator proteins and facilitating the recruitment of HAT complexes to acetylate histone proteins and activate transcription (1-5). TRRAP is required for the transcriptional activation and cell transformation activities of c-Myc, E2F1, E2F4, p53 and the adenovirus E1A proteins (1,6,7). TRRAP is also essential in early development and is required at the mitotic checkpoint and for normal cell cycle progression (8,9). In addition, TRRAP has been shown to function in DNA repair. As part of the TIP60 complex, TRRAP is required for the acetylation of histone H4 at double-stranded DNA breaks and subsequent DNA repair by homologous recombination (10). In addition, TRRAP associates with the MRN (MRE11, RAD50, NBS1) complex, which lacks intrinsic HAT activity yet functions in the sensing and subsequent repair of double-stranded breaks by non-homologous DNA end-joining (11). TRRAP shows significant homology to the PI-3 kinase domain of the ATM family of kinases; however, amino acids that map to the catalytic site of the kinase domain are not conserved in TRRAP (1).

$118
10 western blots
150 µl
Nonphosphorylated EGF Receptor Control Cell Extracts: Total extracts from A431 cells, serum starved overnight to serve as a negative control. Supplied in SDS Sample Buffer.Phosphorylated EGF Receptor Control Cell Extracts: Total extracts from A431 cells, serum starved overnight and treated with 100 ng/ml hEGF #8916 for five minutes to serve as a positive control. Supplied in SDS Sample Buffer.
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Nanog (D73G4) XP® Rabbit mAb #4903.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated p21 Waf1/Cip1 (12D1) Rabbit mAb #2947.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: The tumor suppressor protein p21 Waf1/Cip1 acts as an inhibitor of cell cycle progression. It functions in stoichiometric relationships forming heterotrimeric complexes with cyclins and cyclin-dependent kinases. In association with CDK2 complexes, it serves to inhibit kinase activity and block progression through G1/S (1). However, p21 may also enhance assembly and activity in complexes of CDK4 or CDK6 and cyclin D (2). The carboxy-terminal region of p21 is sufficient to bind and inhibit PCNA, a subunit of DNA polymerase, and may coordinate DNA replication with cell cycle progression (3). Upon UV damage or during cell cycle stages when cdc2/cyclin B or CDK2/cyclin A are active, p53 is phosphorylated and upregulates p21 transcription via a p53-responsive element (4). Protein levels of p21 are downregulated through ubiquitination and proteasomal degradation (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Reelin signaling pathway plays a critical role in neuronal development. Reelin is a secreted glycoprotein that binds to the lipoprotein receptors VLDLR and ApoER2 or alpha3beta1 integrin on the surface of neurons (1,2). Activation of these receptors induces tyrosine phosphorylation of Disabled 1 (Dab1), an intracellular adaptor. It is generally believed that tyrosine phosphorylation of Dab1 by Src family tyrosine kinases is the most critical downstream event in Reelin signaling. The phosphotyrosine-binding (PTB) domain within its amino terminus enables Dab1 to recognize and bind to a conserved sequence motif within the cytoplasmic tail of the receptors. In addition, the PTB contains a Pleckstrin Homology-like subdomain that binds to phosphoinositides. The phosphoinositide-binding region within the Dab1 PTB domain is required for membrane localization and basal tyrosine phosphorylation of Dab1 independent of VLDLR and ApoER2 (3). It has been demonstrated that Src, CrkII, CrkL and Dock1 associate with tyrosine-phosphorylated Dab. The CrkII-Dab1 interaction requires tyrosine phosphorylation of Dab1 at residues 220 or 232 (4).

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

Application Methods: Western Blotting

Background: Transducin-like enhancer of split proteins (TLE1, TLE2, TLE3, TLE4, and TLE6) are mammalian homologs of Drosophila Groucho (1). TLEs contain several WD-repeats implicated in protein-protein interaction (2,3). TLEs are transcriptional co-repressors that bind to many transcription factors such as LEF1, Runx1, Oct-1, hepatocyte nuclear factor 3-β as well as histone H3 (4-7). TLEs are differentially expressed during animal development and may have overlapping as well as distinct functions (8).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Myosin phosphatase-rho interacting protein (M-RIP), also known as p116RIP, RIP3, and MPRIP, localizes to actin-myosin filaments regulating cytoskeletal dynamics (1-3). M-RIP contains amino-terminal pleckstrin homology domains, carboxyl-terminal coiled-coil domains, and was originally identified to associate with the myosin phosphatase complex. M-RIP binds to MBS/MYRT, the myosin binding subunit of myosin phosphatase, as well as RhoA (1-3). Phosphorylation of MYRT by Rho-associated kinase (ROCK) inhibits myosin phosphatase activity, resulting in increased levels of phosphorylation on myosin light chain, and enhanced contractility (4,5). M-RIP may function as a scaffolding protein for the complex between the myosin phosphatase complex, Rho/ROCK, and actin (2,6). Silencing of M-RIP results in disassembly of the complex, increased phosphorylation of myosin light chain, and changes to cytoskeletal dynamics (7,8).

$489
96 assays
1 Kit
The PathScan® Total α-Tubulin Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of α-tubulin. An α-tubulin rabbit antibody has been coated onto the microwells. After incubation with cell lysates, α-tubulin is captured by the coated antibody. Following extensive washing, an α-tubulin mouse detection antibody is added to detect the captured α-tubulin. An anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate (TMB) is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of α-tubulin.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey, Mouse

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
Human

Application Methods: Western Blotting

Background: The transcriptional intermediary factor 1 (TIF1) family represents a group of proteins with multiple histone-binding domains. In humans, this family comprises four proteins, TIF1α/TRIM24, TIF1β/TRIM28/KAP1, TIF1γ/TRIM33/Ectodermin, and TIF1δ/TRIM66, which are characterized by an amino-terminal tripartite motif (TRIM) domain consisting of a RING domain, two B boxes, a coiled-coil domain, and a carboxy-terminal PHD finger and bromodomain (1). Despite their similar overall structure, these proteins have diverse roles in transcriptional regulation. TIF1α functions as a ligand-dependent nuclear receptor coregulator and more recently has been implicated in regulating p53 stability (2). TIF1β is an intrinsic component of the N-CoR1 corepressor complex and the NuRD nucleosome-remodeling complex (3) and functions as a corepressor for Kruppel-associated box (KRAB) zinc-finger transcription factors (4). Furthermore, TIF1β promotes heterochromatin-mediated gene silencing formation by serving as a cofactor for heterochromatin protein HP1 (5). TIF1δ expression is restricted to the testis and has been shown to interact with HP1γ (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzymes (DUB) action (1,2). There are five DUB subfamilies including the USP, UCH, OTU, MJD and JAMM enzymes. USP28 is an important member of the USP subfamily (3). USP28 can bind to and deubiquinate several target proteins in DNA-damage pathway, resulting in their stability, including p53BP1 and Chk2 (4). USP28 also plays an important role in Myc related signaling by binding through FBW7α to Myc . It catalyzes the deubiquitinylation of Myc, thereby promoting its stabilization and contributing to tumor-cell growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor (InsR) is a heterodimeric membrane receptor tyrosine kinase. It is comprised of an extracellular α-subunit, containing the ligand binding domain, and a β-subunit containing an extracellular domain, a transmembrane domain and a cytoplasmic tyrosine kinase domain (1). Binding of insulin to InsR results in receptor autophosphorylation, and subsequent tyrosine kinase activation (2). This provides a docking site for various adaptor molecules, including insulin-receptor substrate (IRS), Gab and Shc, phosphorylation of which promotes subsequent activation of multiple downstream signaling pathways including MAPK, PI3K and TC10 (3,4). These events lead to increased glucose uptake and metabolism, and can promote cell growth. Loss of function mutation or desensitization of the InsR are two major contributors to insulin resistance and Type 2 diabetes (5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Langerin (CD207) is a C-type lectin receptor whose expression is restricted mainly to dendritic cells in the skin including Langerhans cells in the epidermis and langerin+/CD103+ dermal dendritic cells (1-4). Langerin is found on the cell surface and within rod-shaped organelles called Birbeck granules, and its expression is required for the formation of Birbeck granules (1,5). Langerin recognizes carbohydrate motifs on the surface of pathogens, resulting in endocytosis of the pathogen into Birbeck granules, degradation of the pathogen, and antigen presentation to T cells (6-8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: α-methylacyl-CoA racemase (AMACR), an enzyme localized in peroxisomes and mitochondria, is involved in the β-oxidation of branched-chain fatty acids and fatty acid derivatives (1). AMACR has been reported to be a biomarker for prostate cancer (2-4). The expression of AMACR is also related to other types of cancers such as hepatocellular carcinoma (1), noninvasive bladder cancer (5), colorectal cancer (6) and gastric adenocarcinoma (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Maspin (SERPINB5) was discovered as a mammary tumor suppressor that is expressed in normal mammary epithelium but lost in most breast cancer cell lines (1). While maspin is related to the serpin family of serine protease inhibitors, it may not function as a protease inhibitor (2). It plays an essential role in embryonic development through critical roles in cell adhesion (3). While the precise mechanism of maspin signaling is unclear (4), the tumor suppressing activity of maspin has been attributed to its ability to inhibit cell invasion/metastasis (5,6) and angiogenesis (7), while promoting apoptosis (8). Nuclear translocation of active IKKα has been shown to repress maspin transcription and promote prostate cancer metastasis (9).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-p53 (Ser15) (16G8) Mouse mAb #9286.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The p53 tumor suppressor protein plays a major role in cellular response to DNA damage and other genomic aberrations. Activation of p53 can lead to either cell cycle arrest and DNA repair or apoptosis (1). p53 is phosphorylated at multiple sites in vivo and by several different protein kinases in vitro (2,3). DNA damage induces phosphorylation of p53 at Ser15 and Ser20 and leads to a reduced interaction between p53 and its negative regulator, the oncoprotein MDM2 (4). MDM2 inhibits p53 accumulation by targeting it for ubiquitination and proteasomal degradation (5,6). p53 can be phosphorylated by ATM, ATR, and DNA-PK at Ser15 and Ser37. Phosphorylation impairs the ability of MDM2 to bind p53, promoting both the accumulation and activation of p53 in response to DNA damage (4,7). Chk2 and Chk1 can phosphorylate p53 at Ser20, enhancing its tetramerization, stability, and activity (8,9). p53 is phosphorylated at Ser392 in vivo (10,11) and by CAK in vitro (11). Phosphorylation of p53 at Ser392 is increased in human tumors (12) and has been reported to influence the growth suppressor function, DNA binding, and transcriptional activation of p53 (10,13,14). p53 is phosphorylated at Ser6 and Ser9 by CK1δ and CK1ε both in vitro and in vivo (13,15). Phosphorylation of p53 at Ser46 regulates the ability of p53 to induce apoptosis (16). Acetylation of p53 is mediated by p300 and CBP acetyltransferases. Inhibition of deacetylation suppressing MDM2 from recruiting HDAC1 complex by p19 (ARF) stabilizes p53. Acetylation appears to play a positive role in the accumulation of p53 protein in stress response (17). Following DNA damage, human p53 becomes acetylated at Lys382 (Lys379 in mouse) in vivo to enhance p53-DNA binding (18). Deacetylation of p53 occurs through interaction with the SIRT1 protein, a deacetylase that may be involved in cellular aging and the DNA damage response (19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA double-strand breaks (DSBs) are potentially hazardous lesions that can be induced by ionizing radiation (IR), radiomimetic chemicals, or DNA replication inhibitors. Cells sense and repair DSBs via two distinct but partly overlapping signaling pathways, nonhomologous end joining (NHEJ) and homologous recombination (HR). Defects in both pathways have been associated with human disease, including cancer (1). The DNA repair and recombination protein RAD54-like (Rad54, RAD54L) is a Swi2/Snf2 family DNA helicase that is involved in homologous recombination DNA repair. Rad54 is a double-stranded DNA-dependent ATPase that translocates in a processive manner along double-stranded DNA. The Rad54 helicase interacts with the Rad51 recombinase to regulate its DNA binding and strand exchange activities during homologous recombination (2-4). Mutations in the corresponding RAD54L gene are associated with multiple forms of human cancer, including non-Hodgkin's lymphoma, breast cancer, and parathyroid adenoma (5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: TPP1 is encoded by the the ACD gene, and is one of six core proteins of the shelterin complex (TRF1, TRF2, Rap1, TIN2, POT1 and TPP1) that regulates telomere length and integrity. This nuclear protein complex localizes to telomeres, and protects the natural ends of chromosomes from inappropriate processing by DNA repair pathways (1). TPP1 was identified in screens for proteins that bind TIN2, which is considered to be the central component of the shelterin complex (1). TPP1 contains two protein-protein interaction domains that facilitate shelterin complex function: a carboxy-terminal TIN2-binding domain and a more central POT1-binding domain. Heterodimerization of TPP1 with POT1 promotes binding to single-stranded telomeric DNA, which facilitates telomere elongation and protection by the shelterin complex. The TPP1 protein also contains a TEL patch, a collection of surface amino acids that recruits telomerase and modulates its processivity (2). In addition to playing an important role in normal development (3), TPP1 is implicated in the etiology of selected diseases. For example, mutations in ACD that alter the composition of the TEL patch have been linked to Hoyeraal-Hreidarsson syndrome, a clinically severe form of dyskeratosis congenita characterized by hematopoietic stem cell dysfunction, bone marrow failure, and a predisposition to cancer (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Interferon-induced transmembrane protein (IFITM) family members are composed of short amino- and carboxy-termini, two transmembrane domains, and a cytoplasmic domain (1). There are four family members in humans: IFITM1, IFITM2, IFITM3, and IFITM5 (2,3). Mice have two additional family members, IFITM6 and IFITM7 (2,3). Basal expression of IFITM proteins is observed in some cells and expression can also be induced by type I and type II interferons (4-6). The primary function of IFITM family proteins appears to be viral restriction, as IFITM proteins inhibit cytosolic entry of viruses by preventing fusion of viral and host membranes (7,8). The mechanism by which IFITM proteins inhibit fusion is unclear. Although IFITM proteins are present on both the plasma membrane and intracellular membranes, they most effectively restrict viral fusion in late endosomes and lysosomes (8,9). In addition, different family members exhibit specific viral preferences (9). For example, IFITM3 is most effective at restricting influenza A infection, while IFITM1 is more successful in controlling filoviruses and SARS (9,10).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody c-Myc (D84C12) Rabbit mAb #5605.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

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

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

Application Methods: Western Blotting

Background: MEK1 and MEK2, also called MAPK or Erk kinases, are dual-specificity protein kinases that function in a mitogen activated protein kinase cascade controlling cell growth and differentiation (1-3). Activation of MEK1 and MEK2 occurs through phosphorylation of two serine residues at positions 217 and 221, located in the activation loop of subdomain VIII, by Raf-like molecules. MEK1/2 is activated by a wide variety of growth factors and cytokines and also by membrane depolarization and calcium influx (1-4). Constitutively active forms of MEK1/2 are sufficient for the transformation of NIH/3T3 cells or the differentiation of PC-12 cells (4). MEK activates p44 and p42 MAP kinase by phosphorylating both threonine and tyrosine residues at sites located within the activation loop of kinase subdomain VIII.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The Rab family of proteins includes small, monomeric GTPases essential for regulating intracellular vesicle trafficking. Members of the Rab3 subfamily, including Rab3A-3D, are involved in the exocytosis of neurotransmitters and hormones (1). Rab3A is primarily expressed in neurons (2), neuroendocrine cells (such as rat PC-12 cells), and in human pancreatic β cells (3,4). By acting as a molecular switch between active GTP-bound Rab3A and the inactive GDP-bound form, Rab3A inhibits synaptic vesicle and chromaffin granule secretion during late membrane release (5,6). Loss-of-function studies suggest Rab3A is involved in controlling synaptic vesicle targeting and docking at the active zone (7). Through binding to its direct effector Rabphillin, Rab3A also orchestrates the coupling between synaptic vesicle exocytosis and endocytosis (8).