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Product listing: HMGCS1 (D5W8F) Rabbit mAb, UniProt ID Q01581 #36877 to SMARCE1/BAF57 (E6H5J) Rabbit mAb, UniProt ID Q969G3 #33360

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytoplasmic 3-hydroxy-3-methylglutaryl-CoA synthase (HMGCS1) catalyzes the first committed step of mevalonate pathway essential for cholesterol biosynthesis (1). HMGCS1 transcription is regulated by sterol levels (2). Studies showed that miR-223 reduces cholesterol biosynthesis by inhibiting HMGCS1 and methylsterol monooxygenase 1 (3). In addition, activation of the EGFR family member ERBB4 induces the expression of SREBP-regulated genes (including HMGCS1) involved in cholesterol biosynthesis, suggesting a role of this enzyme in the metabolic re-programming in ERBB4-driven cancers (4).

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

Application Methods: Flow Cytometry, Western Blotting

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The methylation state of lysine residues in histone proteins is a major determinant for formation of active and inactive regions of the genome and is crucial for proper programming of the genome during development (1,2). Jumonji C (JmjC) domain-containing proteins represent the largest class of potential histone demethylase proteins (3). The JmjC domain can catalyze the demethylation of mono-, di-, and tri-methyl lysine residues via an oxidative reaction that requires iron and α-ketoglutarate (3). Based on homology, both humans and mice contain at least 30 such proteins, which can be divided into 7 separate families (3). The JARID (Jumonji/AT-rich interactive domain-containing protein) family contains four members: JARID1A (also RBP2 and RBBP2), JARID1B (also PLU-1), JARID1C (also SMCX) and JARID1D (also SMCY) (4). In addition to the JmJC domain, these proteins contain JmJN, BRIGHT, C5HC2 zinc-finger, and PHD domains, the latter of which binds to methylated histone H3 (Lys9) (4). All four JARID proteins demethylate di- and tri-methyl histone H3 Lys4; JARID1B also demethylates mono-methyl histone H3 Lys4 (5-7). JARID1A is a critical RB-interacting protein and is required for Polycomb-Repressive Complex 2 (PRC2)-mediated transcriptional repression during ES cell differentiation (8). A JARID1A-NUP98 gene fusion is associated with myeloid leukemia (9). JARID1B, which interacts with many proteins including c-Myc and HDAC4, may play a role in cell fate decisions by blocking terminal differentiation (10-12). JARID1B is over-expressed in many breast cancers and may act by repressing multiple tumor suppressor genes including BRCA1 and HOXA5 (13,14). JARID1C has been found in a complex with HDAC1, HDAC2, G9a and REST, which binds to and represses REST target genes in non-neuronal cells (7). JARID1C mutations are associated with X-linked mental retardation and epilepsy (15,16). JARID1D is largely uncharacterized.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to produce ceramide and phosphocholine (1). Ceramide is an important bioactive lipid triggering signal transduction involved in cell proliferation, apoptosis and differentiation (1,2). A number of SMases have been described and categorized based on their optimum pH activity, cation dependence, tissue distribution, and subcellular localization (1). These include a lysosomal acid SMase, a Zn++-dependent secreted acid SMase, a membrane-bound Mg++-dependent neutral SMase, a Mg++-independent neutral SMase, and an alkaline SMase.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by Erk, GSK-3, and CDK5 (1,2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease; these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: RNase L is an antiviral protein that is expressed in most mammalian cells (1). Latent RNase L in the cytoplasm is activated by the second messenger 2’,5’-linked oligoadenylate (2-5A), which is produced by oligoadenylate synthase (OAS) after it binds viral double-stranded RNA (dsRNA) (2, 3). RNase L forms a crossed homodimer that is stabilized by kinase homology and ankyrin domains, which position two kinase extension nuclease domains for RNA recognition (4). RNase L then degrades both viral and cellular RNA (5). In mouse models, RNase L has been shown to produce small self-RNAs that act to amplify innate antiviral immunity through IFN-β induction (6). Research has also shown that RNase L forms a complex with Filamin A that acts as a barrier to restrict virus entry, and that RNase L can induce autophagy in response to viral infection (7, 8). Finally, research suggests RNase L may contribute to type I diabetes onset through immune response regulation (9).

$262
3 nmol
300 µl
SignalSilence® Atg7 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Atg7 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: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Aconitase 2 (ACO2) catalyzes the conversion of citrate to isocitrate via cis-aconitate in the second step of the tricarboxylic acid (TCA) cycle (1,2). ACO2 is also an important regulator of iron homeostasis within cells (1-4). In addition, research studies have shown that this enzyme is deficient in the mitochondrial disease Friedreich's Ataxia (4,5).

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Ikaros (D6N9Y) Rabbit mAb #14859.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: The Ikaros family of zinc-finger DNA-binding proteins belongs to the Kruppel transcription factor superfamily. Ikaros proteins are characterized by the presence of an amino-terminal zinc finger DNA-binding domain and a carboxy-terminal dimerization domain. Members of the Ikaros family include Ikaros, Aiolos, Helios, EOS, and Pegasus (1). All family members can form homodimers and heterodimers with other members of the Ikaros family. Most also contain multiple isoforms that are generated as a result of differential splicing, with some isoforms behaving in a dominant negative manner upon dimerization (2).Ikaros (IKZF1, LYF1) is the prototypical Ikaros family zinc-finger transcription factor and is expressed abundantly in lymphoid cells. Genetic studies in mice demonstrate that Ikaros is a tumor suppressor that is important for the normal development of B, T, natural killer, and dendritic cells (3,4). Additional studies show that imbalanced expression of different Ikaros isoforms, as well as mutations in the corresponding IKAROS gene, can be associated with a number of hematologic malignancies in humans (2,5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Integrins are transmembrane glycoproteins that form heterodimers consisting of one α and one β subunit. Integrin dimers act as receptors for extracellular matrix proteins and cell-surface ligands. Integrin signaling to (inside-out) and from (outside-in) extracellular molecules regulates multiple cellular processes, such as development, wound healing, immune response, invasion, metastasis, and angiogenesis (1,2). Integrin β2 (CD18) is the β subunit of the leukocyte-specific integrin family. Leukocyte integrins include Integrin β2 (CD18)/αL (CD11a) (LFA-1, lymphocyte function associated antigen 1), Integrin β2 (CD18)/αM (CD11b) (Mac-1), Integrin β2(CD18)/αX (CD11c), and Integrin β2 (CD18)/αD (CD11d). These integrins bind to immunoglobulin superfamily members, such as ICAM-1 and VCAM-1 on endothelial cells, to mediate firm adhesion and transendothelial migration of leukocytes (3). Integrin β2 (CD18) deficiency results in LAD (leukocyte adhesion deficiency), a disease characterized by impairment of leukocyte recruitment resulting in inability to fight infection (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Presenilin 1 and presenilin 2 are transmembrane proteins belonging to the presenilin family. Mutation of presenilin genes has been linked to early onset of Alzheimer disease, probably due to presenilin's associated γ-secretase activity for amyloid-β protein processing (1,2). Endogenous presenilin mainly exists in a heterodimeric complex formed from the endoproteolytically processed amino-terminal (34 kDa) and carboxy-terminal (~20, 22, 23 kDa) fragments (CTF) (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: PCK2 (PEPCK2 or PEPCK-M) encodes an isoform of phosphoenolpyruvate carboxykinase (PEPCK) that is found in the mitochondria of renal and hepatic tissues (1). PEPCK is involved in gluconeogenesis, the process of generating glucose from non-carbohydrate substrates such as lactate and glycerol (2). PEPCK catalyzes the reaction whereby oxaloacetate becomes phosphoenolpyruvate, a rate limiting step in the metabolic process (2). The predominant function of PCK2 is to process the lactate that is continually produced by red blood cells in the liver and kidney (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). CBX4 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7,8). CBX4 itself is a SUMO E3 ligase, and its function influences EMT, DNA damage response, tumor angiogenesis, and self-renewal (9-13).

$260
100 µg
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions, such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamins have been subdivided into types A and B. Type-A lamins consist of lamin A and C, which arise from alternative splicing of the lamin A gene LMNA. Lamin A and C are cleaved by caspases into large (41-50 kDa) and small (28 kDa) fragments, which can be used as markers for apoptosis (4,5). Type-B lamins consist of lamin B1 and B2, encoded by separate genes (6-8). Lamin B1 is also cleaved by caspases during apoptosis (9). Research studies have shown that duplication of the lamin B1 gene LMNB1 is correlated with pathogenesis of the neurological disorder adult-onset leukodystrophy (10).

$469
Reagents for 4 x 96 well plates
1 Kit
CST's PathScan® Phospho-c-Kit (Tyr719) Sandwich ELISA Antibody Pair is offered as an economical alternative to our PathScan® Phospho-c-Kit (Tyr719) Sandwich ELISA Kit #7298. 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 c-Kit Mouse Capture Antibody is coated in PBS overnight in a 96 well microplate. After blocking, cell lysates are added followed by Phospho-c-Kit (Tyr719) Rabbit Detection Antibody and Anti-rabbit IgG, HRP-linked Antibody. HRP substrate (TMB) is added for color development. The magnitude of the absorbance for this developed color is proportional to the quantity of phospho-c-Kit (Tyr719) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human

Background: c-Kit is a member of the subfamily of receptor tyrosine kinases that includes PDGF, CSF-1, and FLT3/flk-2 receptors (1,2). It plays a critical role in activation and growth in a number of cell types including hematopoietic stem cells, mast cells, melanocytes, and germ cells (3). Upon binding with its stem cell factor (SCF) ligand, c-Kit undergoes dimerization/oligomerization and autophosphorylation. Activation of c-Kit results in the recruitment and tyrosine phosphorylation of downstream SH2-containing signaling components including PLCγ, the p85 subunit of PI3 kinase, SHP2, and CrkL (4). Molecular lesions that impair the kinase activity of c-Kit are associated with a variety of developmental disorders (5), and mutations that constitutively activate c-Kit can lead to pathogenesis of mastocytosis and gastrointestinal stromal tumors (6). Tyr719 is located in the kinase insert region of the catalytic domain. c-Kit phosphorylated at Tyr719 binds to the p85 subunit of PI3 kinase in vitro and in vivo (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Estrogen Receptor α (D6R2W) Rabbit mAb #13258.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades poly-ubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The placenta-specific gene 8 (Plac8) encodes a chromatin-binding protein that was first identified from placenta and that is highly expressed in plasmacytoid dendritic cells (1,2). Research studies indicate that Plac8 plays a role in immune function and is essential in the differentiation of brown fat (3,4). During brown fat differentiation, Plac8 interacts with the transcription factor C/EBPβ at its promoter sequence to activate the transcription of C/EBPβ (4). Experimental deletion of Plac8 in mice leads to impaired innate immune function, abnormal brown fat function, cold intolerance, and obesity (3,4). Additional studies examining the spread of colorectal carcinoma suggest a possible role for Plac8 in cancer invasion, possibly through promoting the epithelial-to-mesenchymal transition seen during tumor progression (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SNAT1/SLC38A1 belongs to the system A transporters that mediate Na+-dependent transport of short-chain neutral amino acids such as alanine, serine, and glutamine. SNAT1/SLC38A1 mediates the uptake of glutamine in neurons and plays a crucial role in glutamate-glutamine cycle. Steep concentration gradients across the plasma membrane are achieved by coupling of the electrochemical sodium gradient to amino acid transport. This allows a unidirectional mode of transport for SNAT1/SLC38A1. Upregulation of SNAT1/SLC38A1 by neurotrophic factors is key to dendritic growth and branching of cortical neurons. High expression of SNAT1/SLC38A1 is found in cerebral cortex primarily in neurons and to a lesser extent in astrocytes (1-4). Elevated SNAT1/SLC38A1 expression is prominent in human solid tumors including gliomas, hepatocellular carcinomas and human breast cancer (5-8). Research studies show that an aberrant SNAT1/SLC38A1 expression profile correlates with solid tumor recurrence and poor prognosis in patients with cholangiocarcinoma (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Multi-drug resistance protein 2 (MRP2), also known as cMRP, cMOAT, and ABCC2, is an ATP binding cassette (ABC) transporter and part of the multi-drug resistance (MRP) family (1,2). The MRP proteins are membrane proteins that function as organic anion pumps involved in the cellular removal of cancer drugs (2). MRP2 is associated with resistance to a number of cancer drugs, such as cisplatin, etoposide, doxorubicin, and methotrexate (3-5). MRP2 is predominately expressed on the apical membranes in the liver (6-9) and kidney proximal tubules (10). It is responsible for the ATP-dependent secretion of bilirubin glucuronides and other organic anions from hepatocytes into the bile, a process important for the excretion of endogenous and xenobiotic substances. Loss of MRP2 activity is the cause of Dubin-Johnson syndrome, an autosomal recessive disorder characterized by defects in the secretion of anionic conjugates and the presence of melanin like pigments in hepatocytes (11-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nucleotide excision repair (NER) is a process by which cells identify and repair DNA lesions that result from chemical and radiation exposure (1). The DNA binding protein XPA is an essential part of a pre-incision complex that forms at sites of damage, and is necessary for the initiation of nucleotide excision repair (2). XPA is one of eight NER proteins (XPA-G, XPV) encoded by genes that are defective in cases of xeroderma pigmentosum, a disorder characterized by sensitivity to sunlight, predisposition to exposed tissue cancers, and neurological defects in some patients (3). Activation of XPA follows phosphorylation at Ser196 and results in increased NER activity. Phosphorylation of XPA at Ser196 is induced by UV exposure in an ATR-dependant fashion (4) and promotes nuclear accumulation of XPA (5). Research studies suggest that XPA may be a direct substrate of the serine/threonine kinase ATR (4) and that NER activity may be negatively regulated through dephosphorylation of Ser196 by the phosphatase WIP1 (6).

$489
96 assays
1 Kit
CST's PathScan® Total Survivin Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total survivin protein. A Survivin Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both phospho and nonphospho survivin proteins are captured by the coated antibody. Following extensive washing, Survivin Rabbit Detection Antibody is added to detect the captured survivin 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 absorbance for this developed color is proportional to the quantity of total survivin protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Monkey

Background: Survivin is a 16 kDa anti-apoptotic protein highly expressed during fetal development and cancer cell malignancy (1). Survivin binds and inhibits caspase-3, controlling the checkpoint in the G2/M-phase of the cell cycle by inhibiting apoptosis and promoting cell division (2,3). This regulatory process requires the phosphorylation of survivin at Thr34 by p34 cdc2 kinase (4). Gene targeting using a Thr34 phosphorylation-defective survivin mutant, as well as antisense survivin, have been shown to inhibit tumor growth (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Western Blotting

Background: Parkinson's disease (PD) is characterized by the presence of Lewy bodies (intracellular inclusions) and by the loss of dopaminergic neurons. Research studies have shown that mutations in α-synuclein, Parkin, and DJ-1 are linked to PD (1). α-synuclein is a major component of the aggregates found in Lewy bodies. Parkin is involved in protein degradation through the ubiquitin-proteasome pathway, and investigators have shown that mutations in Parkin cause early onset of PD (1). Loss-of-function mutations in DJ-1 cause early onset of PD, but DJ-1 is associated with multiple functions: it cooperates with Ras to increase cell transformation, it positively regulates transcription of the androgen receptor, and it may function as an indicator of oxidative stress (2-5). Dopamine D2 receptor-mediated functions are greatly impaired in DJ-1 (-/-) mice, resulting in reduced long-term depression (6).

$489
96 assays
1 Kit
CST's PathScan® Phospho-IκBα (Ser32) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-IκBα (Ser32) protein. An IκBα Mouse mAb has been coated onto the microwells. After incubation with cell lysates, both nonphospho- and phospho-IκBα proteins are captured by the coated antibody. Following extensive washing, Phospho-IκBα (Ser32) Antibody is added to detect the captured phospho-IκBα (Ser32) 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 optical density for this developed color is proportional to the quantity of phospho-IκBα (Ser32) protein.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

The Resazurin Cell Viability Kit is a fluorescent assay that detects cellular metabolic activity. The blue nonfluorescent resazurin reagent is reduced to highly fluorescent resorufin by dehydrogenase enzymes in metabolically active cells. This conversion only occurs in viable cells and thus, the amount of resorufin produced is proportional to the number of viable cells in the sample. The resorufin formed in the assay can be quantified by measuring the relative fluorescence units (RFU) using a fluorometer (Ex=530-570 nm, Em=590-620 nm).
$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Stat1 (D1K9Y) Rabbit mAb #14994.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The Stat1 transcription factor is activated in response to a large number of ligands (1) and is essential for responsiveness to IFN-α and IFN-γ (2,3). Phosphorylation of Stat1 at Tyr701 induces Stat1 dimerization, nuclear translocation, and DNA binding (4). Stat1 protein exists as a pair of isoforms, Stat1α (91 kDa) and the splice variant Stat1β (84 kDa). In most cells, both isoforms are activated by IFN-α, but only Stat1α is activated by IFN-γ. The inappropriate activation of Stat1 occurs in many tumors (5). In addition to tyrosine phosphorylation, Stat1 is also phosphorylated at Ser727 through a p38 mitogen-activated protein kinase (MAPK)-dependent pathway in response to IFN-α and other cellular stresses (6). Serine phosphorylation may be required for the maximal induction of Stat1-mediated gene activation.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Insulin-like growth factor-II mRNA-binding proteins (IMPs) belong to a family of zipcode-binding proteins (1,2). Three members of this family, IMP1, IMP2, and IMP3, have been identified (1,2). They contain two RNA recognition motifs, four K homology domains, and were found to function in mRNA localization, turnover, and translation control (1,2). Research studies have implicated these proteins in a variety of physiological and pathological processes, such as growth and development (3), testicular neoplasia (4), and melanocytic neoplasia (5).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The modulation of chromatin structure is an essential component in the regulation of transcriptional activation and repression. Modifications can be made by at least two evolutionarily conserved strategies, through the disruption of histone-DNA contacts by ATP-dependent chromatin remodelers, or by histone tail modifications including methylation and acetylation. One of the four classes of ATP-dependent histone remodelers is the SWI/SNF complex, the central catalytic subunit of which is Brg1 or the highly related protein hBRM (1). This SWI/SNF complex contains varying subunits but its association with either Brg1 or hBRM remains constant (1). SWI/SNF complexes have been shown to regulate gene activation, cell growth, the cell cycle and differentiation (1). Brg1/hBRM have been shown to regulate transcription through enhancing transcriptional activation of glucocorticoid receptors (2). Although usually associated with transcriptional activation, Brg1/hBRM have also been found in complexes associated with transcriptional repression including with HDACs, Rb and Tif1β (3-5). Brg1/hBRM plays a vital role in the regulation of gene transcription during early mammalian embryogenesis. In addition, Brg1/hBRM also play a role as a tumor suppressors and Brg1 is mutated in several tumor cell lines (6-8).