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Product listing: PathScan® Total p53 Sandwich ELISA Antibody Pair, UniProt ID P04637 #7844 to Phospho-Catenin δ-1 (Tyr904) Antibody, UniProt ID O60716 #2910

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Total p53 Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan® Total p53 Sandwich ELISA Kit #7370. Capture and Detection antibodies (100X stocks) and HRP-conjugated secondary antibody (1000X stock) are supplied. Sufficient reagents are supplied for 4 x 96 well ELISAs. The p53 Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added followed by a p53 Detection Antibody and anti-Mouse IgG, HRP conjugated antibody. HRP substrate, TMB, is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of total p53 protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

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, Monkey, Mouse, Rat

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

Background: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism, and transport of nuclear pre-mRNA transcripts (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nucleomethylin (NML), also known as ribosomal RNA-processing protein 8 (RRP8) and human cerebral protein 1 (Hucep-1), is a nucleolar protein (1,2). NML interacts with the histone de-acetylase protein SirT1 and histone methyl-transferase protein SUV39H1 to form the energy-dependent nucleolar silencing complex (eNoSC) that regulates ribosomal RNA (rRNA) transcription in response to changes in the energy state of the cell (2). As energy levels in the cell decrease due to caloric restriction, eNoSC binds to rRNA genes and represses transcription by SirT1-mediated de-acetylation of histones and SUV39H1-mediated methylation of histone H3 on Lys9. NML binds to di-methylated Lys9 of histone H3 and likely functions in the recruitment and spreading of eNoSC along the rRNA genes (2). NML also contains a methyltransferases-like domain, which binds to S-adenosyl-methionine (SAM) and is required for eNoSC function (2). By limiting the transcription of rRNA genes during caloric restriction, eNoSC promotes the restoration of energy balance and protects cells from energy-dependent apoptosis.

$262
3 nmol
300 µl
SignalSilence® HDAC4 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit HDAC4 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Special AT-rich binding protein 2 (SATB2) is a close homolog to SATB1 that functions as a transcription factor. It binds to nuclear matrix attachment regions (MARS); regulatory DNA sequences important for chromatin structure. SATB2 was initially identified when bound to the MARS of the immunoglobulin μ gene in pre-B cells, enhancing its expression (1). SATB2 plays a role in osteoblast differentiation by repressing the HoxA2 gene and enhancing the activity of Runx2 and ATF4 (2). SATB2 also plays a role in the developing cerebral cortex by changing chromatin structure surrounding the Ctip2 regulatory regions (3). In erythroid cells, SATB2 activates the γ-globin locus by recruiting PCAF and reordering the chromatin structure (4). Downregulation of SATB2 is linked to colorectal cancer and head and neck squamous carcinomas (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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.

$260
100 µl
APPLICATIONS

Application Methods: Western Blotting

Background: Sleeping Beauty Transposase is part of a transposon system designed to allow viral free genetic insertion into vertebrate DNA. The system is composed of two components: a transposable element (transposon) that can carry DNA of interest, and a transposase that cuts and pastes the transposon into the genome. The transposase was identified from a consensus sequence of inactive Tc1/mariner-like transposase DNA sequences from salmonid fish. It was constructed by fusing and modifying two sequences from Atlantic salmon (Salmo salar) and one sequence from rainbow trout (Oncorhynchus mykiss). The transposon,T, was identified from a consensus sequence of extinct Tc-1 like transposons in salmonid fish (Tanichthys albonubes) (1). Further modifications of the system have been made since its initial construction: sequence changes to the transposase to fit better to an improved consensus sequence has increased its efficiency by 100 fold (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: 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).

Jurkat cells are treated with 100 nM calyculin A and 1 mM pervanadate to inhibit multiple serine/threonine and tyrosine phosphatases, respectively and upregulate protein phosphorylation. Treated Jurkat cells were lysed in 1X cell lysis buffer and lysates were lyophilized.
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD151 (PETA-3, SFA-1) is a member of the evolutionarily conserved tetraspanin family of multipass glycoproteins (TM4SF), highlighted by four transmembrane domains, two extracellular loops, and N/C-termini that reside within the cytoplasm. Identified as the first member of the tetraspanin family to be implicated in tumorigenesis, research studies have demonstrated that CD151 participates in tumor neovascularization (1), tumor cell cell invasion (2), and cell adhesion (3). Furthermore, a positive correlation exists between CD151 expression levels and poor prognosis for tumors of the lung (4), kidney (5), and prostate (6). CD151 is localized predominantly to the plasma membrane and research studies have demonstrated that CD151 exerts its pro-tumorigenic effects, in part, through the modulation of laminin-binding integrins (7-9) and oncogenic receptor tyrosine kinases, such as c-Met (10,11) and EGFR (12).

Molecular Weight:560.64 g/mol

Background: Geldanamycin (GA) is a naturally existing HSP90 inhibitor that belongs to the benzoquinone ansamycin family. GA binds to the amino terminal ATP-binding pocket of HSP90 and inhibits ATP binding and hydrolysis. HSP90 is a chaperone interacting with a wide variety of important target proteins for cell signaling and regulation during tumorgenesis (1,2). The binding of GA to HSP90 interferes with HSP-mediated target protein folding, leading to target aggregation and degradation (1-3). GA and its synthetic derivatives show higher affinity to HSP90 in tumor cells as compared to normal tissues and constitute a class of protential antitumor drugs (2-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI) (1). RhoA, RhoB and RhoC are highly homologous, but appear to have divergent biological functions. Carboxy-terminal modifications and differences in subcellular localization allow these three proteins to respond to and act on distinct signaling molecules (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Macrophage inhibitory cytokine-1 (Mic-1), also termed GDF15 (1), PTGF-β (2), PLAB (3), PDF (4), and NAG-1 (5), is a divergent member of the transforming growth factor-β (TGF-β) superfamily (6). Like other family members, Mic-1 is synthesized as an inactive precursor that undergoes proteolytic processing involving removal of an N-terminal hydrophobic signal sequence followed by cleavage at a conserved RXXR site generating an active C-terminal domain that is secreted as a dimeric protein. Mic-1 is highly expressed in the placenta and is also dramatically increased by cellular stress, acute injury, inflammation, and cancer. In the brain, Mic-1 is found in the choroid plexus and is secreted into the cerebrospinal fluid (7). It is also a transcriptional target of the p53 tumor suppressor protein and may serve as a biomarker for p53 activity (8,9). During tumor progression, Mic-1 has various effects on apoptosis, differentiation, angiogenisis, and metastasis, and may also contribute to weight loss during cancer (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Transthyretin (TTR) is a highly conserved homotetremric protein that is synthesized in the liver and choroid plexus of the brain. TTR was originally discovered as a protein found in human plasma and cerebrospinal fluid (CSF) (1). TTR transports thyroid hormones (TH) and retinol by binding to retinol-binding protein (2). Although TTR is synthesized in the liver and choroid plexus, TTR is detected in blood plasma and cerebrospinal fluid migrating as monomers, dimers, and tetramers. Beyond its function as a carrier protein of TH and retinol in plasma and CSF, several additional TTR functions have been described, including proteolytic cleavage of specific substrates like apolipoprotein, neuropeptide Y (NPY), and APP (3, 4, 5). These neuronal substrates suggest a functional role for TTR in the central nervous system. Consistent with a CNS function, TTR null mice exhibit memory impairments and altered sensorimotor behavior (6, 7). TTR may also be linked to neurodegenerative disease: TTR levels in Alzheimer’s disease (AD) patients are negatively correlated with disease progression, and a protective role for TTR, at least in AD mouse models, has been described (8, 9). TTR itself may play a more direct role in disease as gain-of-function mutations in TTR cause the protein to misfold and aggregate into amyloid fibrils, contributing to autosomal dominant hereditary amyloidosis in diseases such as familial amyloid polyneuropathy, familial amyloid cardiomyopathy, and familial leptomeningeal amyloidosis (10). 

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Intercellular cell adhesion molecule-1 (CD54 or ICAM-1) is a cell surface glycoprotein that belongs to the immunoglobulin superfamily (IgSF) of adhesion molecules. CD54 is expressed at low levels in diverse cell types, and is induced by cytokines (TNF-α, interleukin-1) and bacterial lipopolysaccharide (1). Apical localization of CD54 on endothelial cells (or basolateral localization on epithelial cells) is a prerequisite for leukocyte trafficking through the endothelial (or epithelial) barrier (1). Apical expression of CD54 on epithelial cells mediates pathogen invasion as well as host defense, a pattern also observed in tumors (1). CD54 also functions as a co-stimulator on antigen presenting cells, binding to its receptor LFA-1 (leukocyte function-associated antigen-1) on the surface of T cells during antigen presentation (2). Cross-linking of CD54 or binding to its ligand triggers activation of Src family kinases and the Rho/ROCK pathway (3-7). Phosphorylation on Tyr485 of CD54 is required for its association with SHP-2 (5). SHP-2 seems essential for CD54-induced Src activation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The KiSS-1 receptor (KISS1R, GPR54) is a G protein-coupled receptor that inhibits cancer cell metastasis and plays a major role in gonadotropic axis physiology (1). The GPR54 protein was originally described as an orphan receptor homologous to the galanin receptor, and later identified as a receptor for amidated peptide products of the metastasis suppressor gene KiSS-1 (2,3). In humans, amidated kisspeptin ligands are produced predominantly in cells of the arcuate nucleus and preoptic area, with expression controlled by gonadal hormones (4). Research studies show that deletion of either the KiSS-1 receptor or KiSS-1 genes leads to hypogonadotropic hypogonadism, a disorder characterized by reduced levels of circulating testosterone and gonadotropins, as well as abnormal sexual maturation (5,6) The administration of kisspeptins potently stimulates gonadotropin secretion, indicating that KISS1R and kisspeptins play a major role in the physiology of the gonadotropic axis (7). Additional research demonstrates that KISS1R and kisspeptins inhibit metastasis in cancer cells by inhibiting cell motility (8). However, other studies indicate that increased expression of KISS1R and its ligands in human breast tumors correlates with higher tumor grade and metastatic potential, likely by engaging MMP-9 activation via transactivation of EGFR (9).

$489
96 assays
1 Kit
PathScan® Phospho-FGF Receptor 4 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated FGR receptor 4 protein. An FGF receptor 4 rabbit mAb has been coated onto the microwells. After incubation with cell lysates, FGF receptor 4 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse detection mAb is added to detect captured phospho-FGF receptor 4 protein. 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 optical density for this developed color is proportional to the quantity of FGF Receptor 4 protein phosphorylated on tyrosine residues.Antibodies in the kit are custom formulations specific to kit.
REACTIVITY
Human

Background: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain, and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).

$262
3 nmol
300 µl
REACTIVITY
Human

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

$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 SUMO-2/3 (18H8) Rabbit mAb #4971.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Small ubiquitin-related modifier 1, 2 and 3 (SUMO-1, -2 and -3) are members of the ubiquitin-like protein family (1). The covalent attachment of the SUMO-1, -2 or -3 (SUMOylation) to target proteins is analogous to ubiquitination. This post-translational modification is a reversible, multi-step process that is initiated by cleaving a precursor protein to a mature protein. Mature SUMO-1, -2 or -3 is then linked to the activating enzyme E1, conjugated to E2 and in conjunction with E3, SUMO-1, -2 or -3 is ligated to the target protein (2). Ubiquitin and the individual SUMO family members are all targeted to different proteins with diverse biological functions. Ubiquitin predominantly regulates degradation of its target (1). In contrast, SUMO-1 is conjugated to RanGAP, PML, p53 and IκB-α to regulate nuclear trafficking, formation of subnuclear structures, regulation of transcriptional activity and protein stability (3-7). SUMO-2/-3 forms poly-(SUMO) chains, is conjugated to topoisomerase II and APP, regulates chromosomal segregation and cellular responses to environmental stress, and plays a role in the progression of Alzheimer disease (8-11).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: REPS1 is a RalBP1-associated EH-homology domain containing protein. The sequence of REPS1 has an EH domain, followed by two proline-rich segments, and a C-terminal coiled-coil domain for binding to RalBP1 (1). The EH domain of REPS1 interacts with the NPF motif of Rab11-FIP2, mediates their colocalization to endosome vesicles, and influences EGFR endocytosis (2). The two proline-rich regions of REPS1 are important for binding to the SH3 domain of GRK/GRB2 and further regulate EGFR downstream signaling. The proline-rich regions of REPS1 have also been shown to interact with the SH3 domain of intersectin1 (ITSN1) and contribute to ITSN1/SGIP1/REPS1 complex formation on clathrin-coated pits (3). Three alternatively spliced isoforms of REPS1 have been identified.

$305
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Akt (pan) (C67E7) Rabbit mAb (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of Akt. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Akt (pan) (C67E7) Rabbit mAb #4691.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Na+/H+ exchanger regulatory factor (NHERF1 or EBP-50) is one of several related PDZ domain-containing proteins (1). NHERF1 was first identified as a necessary cofactor for cyclic AMP-associated inhibition of Na+/ H+ exchanger isoform 3 (NHE3) (2). NHERF1 is a multifunctional adaptor protein that interacts with receptors and ion transporters via its PDZ domains, and with the ERM family of proteins, including merlin, via its carboxy-terminus (2,3). NHERF1 may play an important role in breast cancer. Estrogen has been found to induce NHERF1 in estrogen receptor-positive breast cancer cells (2,3). Furthermore, NHERF1 has been shown to bind to PDGFR, which is activated in breast carcinomas. NHERF1 has been found to promote the formation of a ternary complex containing PTEN, NHERF1, and PDGFR. Therefore, NHERF1 may function to recruit PTEN to PDGFR to inhibit the activation of PI3K/Akt signaling in normal cells; this mechanism may be disrupted in cancer (4). NHERF1 also binds to the cystic fibrosis transmembrane conductance regulator (CFTR), which functions as an ion channel and has disease-causing mutations in cystic fibrosis (5). Other proposed functions of NHERF1 include testicular differentiation, endosomal recycling, membrane targeting, protein sorting, and trafficking (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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.

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

Application Methods: Chromatin IP, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Rho family GTPases are key regulators of diverse processes such as cytoskeletal organization, cell growth and differentiation, transcriptional regulation, and cell adhesion/motility. The activities of these proteins are controlled primarily through guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, promoting the active (GTP-bound) state, and GTPase activating proteins (GAPs) that promote GTP hydrolysis and the inactive (GDP-bound) state (1,2).The p190 RhoGAP proteins are widely expressed Rho family GAPs. p190-A has been characterized as a tumor suppressor, and research studies have shown that loss or rearrangement of the chromosomal region containing the gene for p190-A is linked to tumor development (3,4). p190-A binds the mitogen-inducible transcription factor TFII-I, sequestering it in the cytoplasm and inhibiting its activity. Phosphorylation of p190-A at Tyr308 reduces its affinity for TFII-I, relieving the inhibition (5). p190-A can also inhibit growth factor-induced gliomas in mice (6) and affect cleavage furrow formation and cytokinesis in cultured cells (7).Mice lacking p190-B RhoGAP show excessive Rho activation and a reduction in activation of the transcription factor CREB (8). Cells deficient in p190-B display defective adipogenesis (9). There is increasing evidence that p190 undergoes tyrosine phosphorylation, which activates its GAP domain (9-11). Levels of tyrosine phosphorylation are enhanced by Src overexpression (10,11). IGF-I treatment downregulates Rho through phosphorylation and activation of p190-B RhoGAP, thereby enhancing IGF signaling implicated in adipogenesis (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The matrix metalloproteinase (MMP) family of proteases is a group of zinc-dependent enzymes that target extracellular proteins, including growth factors, cell surface receptors, adhesion molecules, matrix structural proteins, and other proteases (1, 2). Within this family, MMP1, MMP8, and MMP13 have been characterized as a collagenase sub-family of MMPs targeting fibrillar collagen (collagen type I, II, and III) for degradation. In addition to collagen, MMP1 also has activity toward a broad array of other ECM proteins such as fibronectin, gelatin, aggrecan (etc.), as well as growth factors, chemokines, and cytokines (3). MMP1 is widely involved in tissue remodeling during wound healing, tumor growth, invasion and metastasis, and arthritis (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Serine racemase, also called SRR, is an enzyme that is highly expressed in the brain and converts L-serine to D-serine (1,2). D-serine is a co-agonist of the NMDA receptor. NMDA receptor activation requires the binding of glutamate to its GluN2 subunit and the concomitant binding of either glycine or D-serine to its glycine binding site on the GluN1 subunit (3). Decreased activation of NMDA receptors is a typical feature of impaired synaptic plasticity in age-related memory deficits. Therefore, D-serine availability makes serine racemase an important therapeutic target for memory deficit associated with nonpathological aging (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Na+/H+ exchanger regulatory factor (NHERF1 or EBP-50) is one of several related PDZ domain-containing proteins (1). NHERF1 was first identified as a necessary cofactor for cyclic AMP-associated inhibition of Na+/ H+ exchanger isoform 3 (NHE3) (2). NHERF1 is a multifunctional adaptor protein that interacts with receptors and ion transporters via its PDZ domains, and with the ERM family of proteins, including merlin, via its carboxy-terminus (2,3). NHERF1 may play an important role in breast cancer. Estrogen has been found to induce NHERF1 in estrogen receptor-positive breast cancer cells (2,3). Furthermore, NHERF1 has been shown to bind to PDGFR, which is activated in breast carcinomas. NHERF1 has been found to promote the formation of a ternary complex containing PTEN, NHERF1, and PDGFR. Therefore, NHERF1 may function to recruit PTEN to PDGFR to inhibit the activation of PI3K/Akt signaling in normal cells; this mechanism may be disrupted in cancer (4). NHERF1 also binds to the cystic fibrosis transmembrane conductance regulator (CFTR), which functions as an ion channel and has disease-causing mutations in cystic fibrosis (5). Other proposed functions of NHERF1 include testicular differentiation, endosomal recycling, membrane targeting, protein sorting, and trafficking (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).