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Product listing: xCT/SLC7A11 Antibody, UniProt ID Q9WTR6 #98051 to PDAP1 Antibody, UniProt ID Q13442 #4300

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: The x(c)(-) cysteine/glutamate antiporter consists of a light chain subunit (xCT/SLC7A11) that confers substrate specificity and a glycosylated heavy chain subunit (4F2hc/SLC3A2) located on the cell surface (1,2). The heterodimeric amino acid transport system x(c)(-) provides selective import of cysteine into cells in exchange for glutamate and regulating intracellular glutathione (GSH) levels, which is essential for cellular protection from oxidative stress (3). Research studies have shown that xCT expression increases in various tumors, including gliomas, and have implicated xCT in GSH-mediated anticancer drug resistance (4,5). Researchers have found that xCT provides neuroprotection by enhancing glutathione export from non-neuronal cells (6). Moreover, investigators identified xCT as the fusion-entry receptor for Kaposi's sarcoma-associated herpesvirus (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 analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated CHOP (L63F7) Mouse mAb #2895.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: CHOP was identified as a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (1). CHOP expression is induced by certain cellular stresses including starvation and the induced CHOP suppresses cell cycle progression from G1 to S phase (2). Later it was shown that, during ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (3). Studies also found that CHOP mediates the activation of GADD34 and Ero1-Lα expression during ER stress. GADD34 in turn dephosphorylates phospho-Ser51 of eIF2α thereby stimulating protein synthesis. Ero1-Lα promotes oxidative stress inside the endoplasmic reticulum (ER) (4). The role of CHOP in the programmed cell death of ER-stressed cells is correlated with its role promoting protein synthesis and oxidative stress inside the ER (4).

$305
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated ELAVL1/HuR (D9W7E) Rabbit mAb #12582.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The ELAVL (embryonic lethal, abnormal vision and Drosophila-like) family of proteins includes ELAVL1/HuR, ELAVL2/HuB, ELAVL3/HuC and ELAVL4/HuD (1). ELAVL1/HuR is ubiquitously expressed whereas expression of the other three members is neuronal-specific (1). ELAVL/Hu proteins are highly conserved RNA-binding proteins (1). Besides three RNA recognition motifs, these proteins also contain nuclear localization signals that enable them to shuttle between nucleus and cytoplasm (2). Upon inhibition of transcription by actinomycin D, ELAVL1/HuR relocates from nucleus to cytoplasm where it binds the AU-rich elements within 3' UTRs to stabilize mRNAs (3, 4). ELAVL1/HuR is suggested to increase translation by binding to mRNAs (5,6). In addition, ELAVL1/HuR interacts with microRNAs (miRNAs) (7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated FoxO1 (C29H4) Rabbit mAb #2880.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The Forkhead family of transcription factors is involved in tumorigenesis of rhabdomyosarcoma and acute leukemias (1-3). Within the family, three members (FoxO1, FoxO4, and FoxO3a) have sequence similarity to the nematode orthologue DAF-16, which mediates signaling via a pathway involving IGFR1, PI3K, and Akt (4-6). Active forkhead members act as tumor suppressors by promoting cell cycle arrest and apoptosis. Increased expression of any FoxO member results in the activation of the cell cycle inhibitor p27 Kip1. Forkhead transcription factors also play a part in TGF-β-mediated upregulation of p21 Cip1, a process negatively regulated through PI3K (7). Increased proliferation results when forkhead transcription factors are inactivated through phosphorylation by Akt at Thr24, Ser256, and Ser319, which results in nuclear export and inhibition of transcription factor activity (8). Forkhead transcription factors can also be inhibited by the deacetylase sirtuin (SirT1) (9).

$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 NBR1 (D2E6) Rabbit mAb #9891.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Next to BRCA1 gene 1 (NBR1) protein is known for its encoding gene proximity to the BRCA1 tumor suppressor gene (1,2). N-terminal Phox and Bem1p (PB1) domains of NBR1 mediate its interaction with muscle specific titin kinase (3,4) and scaffolding protein p62 (4). NBR1 plays a role in autophagy by facilitating the autophagosomal degradation of ubiquitinated proteins independently and also in concert with p62 (5,6).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Semaphorin-4D/CD100 (Sema4D) is a disulfide-linked homodimeric type 1 transmembrane glycoprotein belonging to the class IV family of membrane bound semaphorins. The extracellular domain of Sema4D contains a cysteine-rich semaphorin-like domain, an Ig-like domain, and a PSI domain (1). Research studies have suggested that the cytoplasmic domain has a signaling function as it is phosphorylated on serine residues (2). Initial studies involving Sema4D revealed that it was implicated in axon guidance within the central nervous system through binding its high affinity receptor, plexin-B1 (3). Sema4D function has also been extensively characterized in the immune system and is the first semaphorin found to be expressed on the surface of many types of immune cells (4-6). In the immune system, CD72 serves as a low-affinity receptor for Sema4D (7) and research studies have shown that Sema4D not only regulates T-cell activation (8,9) but is also involved in the regulation of B-cell survival and differentiation (10). Many of the physiologic effects of Sema4D in the immune system are regulated by a soluble extracellular domain-containing fragment generated through proteolytic cleavage (11).Sema4D has also been implicated in oncogenesis as research studies have demonstrated overexpression in multiple types of solid tumors (12,13). The role of Sema4D in oncogenesis, in part, has been linked to its ability to promote tumor angiogenesis (14), cell invasion (15), and immunosuppression through enhancement of myeloid derived suppressor cell function (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: TNFRSF9 is a member of the tumor necrosis factor receptor superfamily (1, 2). It is also called 4-1BB or CD137 (1, 2). 4-1BB/CD137/TNFRSF9 is expressed in activated CD4+ and CD8+ T cells, natural killer cells and dendritic cells (2-5). The ligand 4-1BBL/CD137L/TNFSF9 on antigen presenting cells binds to 4-1BB/CD137/TNFRSF9 and costimulates the activation of T cells (5). The binding of agonistic antibodies to 4-1BB/CD137/TNFRSF9 also leads to costimulation for T cell activation (5). Studies have shown the effectiveness of targeting 4-1BB/CD137/TNFRSF9 by its agonistic antibodies in cancer immunotherapy (6).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) #4814.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Small regulatory Polypeptide of Amino Acid Response (SPAR) is a polypeptide, encoded by the lncRNA LINC00961 gene and is localized in late endosomal and lysosomal membranes. SPAR binds to the lysosomal v-ATPase complex in addition to ragulator, RagA and RagC. Upon amino acid stimulation, this supercomplex activates mTORC1 signaling. However, this process is inhibited by the binding of SPAR to the v-ATPase complex, as its formation prevents mTORC1 recruitment to lysosomes. SPAR downregulation and inactivation is an important focus for promoting muscle regeneration following muscle injury. This downregulation and inactivation promotes mTORC1 activation and results in myofiber maturation. In addition to muscle regeneration, SPAR downregulation and inactivation also promotes stem cell proliferation and differentiation.

$305
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads.SV40 Large T Antigen (D1E9E) Rabbit mAb (Sepharose® Bead Conjugate) is useful for immunoprecipitation assays. The antibody is expected to exhibit the same cross-species reactivity as the unconjugated SV40 Large T Antigen (D1E9E) Rabbit mAb #15729.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation

Background: Simian Virus 40 (SV40) is a small double-stranded, circular DNA tumor virus encoding three tumor antigens: large T, Small T, and 17KT. These antigens contribute to cellular transformation, an area of research where they are utilized extensively. Transformation of cells by SV40 large T antigen is mediated by its binding to the tumor suppressor proteins RB and p53 in the nucleus. Additional binding partners include p300, CBP, Cul7, IRS1, Bub1, Nbs1, and Fbw7, which also contribute to transformation (1).

$262
3 nmol
300 µl
SignalSilence® B-Raf siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit B-Raf 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: A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).

$262
3 nmol
300 µl
SignalSilence® Bim siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Bim 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 protein expression by western analysis.
REACTIVITY
Human, Mouse, Rat

Background: Bim/Bod is a pro-apoptotic protein belonging to the BH3-only group of Bcl-2 family members including Bad, Bid, Bik, Hrk, and Noxa that contain a BH3 domain but lack other conserved BH1 or BH2 domains (1,2). Bim induces apoptosis by binding to and antagonizing anti-apoptotic members of the Bcl-2 family. Interactions have been observed with Bcl-2, Bcl-xL, Mcl-1, Bcl-w, Bfl-1, and BHRF-1 (1,2). Bim functions in regulating apoptosis associated with thymocyte negative selection and following growth factor withdrawal, during which Bim expression is elevated (3-6). Three major isoforms of Bim are generated by alternative splicing: BimEL, BimL, and BimS (1). The shortest form, BimS, is the most cytotoxic and is generally only transiently expressed during apoptosis. The BimEL and BimL isoforms may be sequestered to the dynein motor complex through an interaction with the dynein light chain and released from this complex during apoptosis (7). Apoptotic activity of these longer isoforms may be regulated by phosphorylation (8,9). Environmental stress triggers Bim phosphorylation by JNK and results in its dissociation from the dynein complex and increased apoptotic activity.

$262
3 nmol
300 µl
SignalSilence® EGF Receptor siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit EGF Receptor 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 are rigorously tested in-house and have been shown to reduce protein expression in specified cell lines.
REACTIVITY
Human

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).

$262
50-100 transfections
300 µl
SignalSilence® HSP27 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit HSP27 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: Heat shock protein (HSP) 27 is one of the small HSPs that are constitutively expressed at different levels in various cell types and tissues. Like other small HSPs, HSP27 is regulated at both the transcriptional and posttranslational levels (1). In response to stress, the HSP27 expression increases several-fold to confer cellular resistance to the adverse environmental change. HSP27 is phosphorylated at Ser15, Ser78, and Ser82 by MAPKAPK-2 as a result of the activation of the p38 MAP kinase pathway (2,3). Phosphorylation of HSP27 causes a change in its tertiary structure, which shifts from large homotypic multimers to dimers and monomers (4). It has been shown that phosphorylation and increased concentration of HSP27 modulates actin polymerization and reorganization (5,6).

$262
3 nmol
300 µl
SignalSilence® MEK1 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit MEK1 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: 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.

$262
3 nmol
300 µl
SignalSilence® MEK2 siRNA from Cell Signaling Technology allows the researcher to specifically inhibit MEK2 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 are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

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.

$262
3 nmol
300 µl
SignalSilence® p42 MAPK (Erk2) siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit p42 MAP Kinase 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 are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$262
3 nmol
300 µl
SignalSilence® p44 MAPK (Erk1) siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit p44 MAPK (Erk1) 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: Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases involved in many cellular programs, such as cell proliferation, differentiation, motility, and death. The p44/42 MAPK (Erk1/2) signaling pathway can be activated in response to a diverse range of extracellular stimuli including mitogens, growth factors, and cytokines (1-3), and research investigators consider it an important target in the diagnosis and treatment of cancer (4). Upon stimulation, a sequential three-part protein kinase cascade is initiated, consisting of a MAP kinase kinase kinase (MAPKKK or MAP3K), a MAP kinase kinase (MAPKK or MAP2K), and a MAP kinase (MAPK). Multiple p44/42 MAP3Ks have been identified, including members of the Raf family, as well as Mos and Tpl2/COT. MEK1 and MEK2 are the primary MAPKKs in this pathway (5,6). MEK1 and MEK2 activate p44 and p42 through phosphorylation of activation loop residues Thr202/Tyr204 and Thr185/Tyr187, respectively. Several downstream targets of p44/42 have been identified, including p90RSK (7) and the transcription factor Elk-1 (8,9). p44/42 are negatively regulated by a family of dual-specificity (Thr/Tyr) MAPK phosphatases, known as DUSPs or MKPs (10), along with MEK inhibitors, such as U0126 and PD98059.

$262
50-100 transfections
300 µl
SignalSilence® PKA C-α siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit PKA C-α 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: The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).

$262
3 nmol
300 µl
SignalSilence® Puma siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Puma 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: Puma (p53 upregulated modulator of apoptosis) is a "BH3-only" Bcl-2 family member originally identified in differential gene expression studies as a p53-inducible gene (1,2). The "BH3-only" family members include Bad, Bid, Bik, Hrk, Bim, and Noxa, all of which contain a BH3 domain but lack other conserved domains, BH1 and BH2, and generally promote apoptosis by binding to and antagonizing anti-apoptotic Bcl-2 family members through BH3 domain interactions (3). Two BH3-containing proteins are produced from the puma gene, Puma-α and Puma-β, both of which are induced by p53, bind Bcl-2 and Bcl-xL, localize to the mitochondria, and promote cytochrome c release and apoptosis (1,2). Puma plays a critical role in the p53 tumor suppressor pathway. Targeted disruption of the puma gene impairs p53-mediated apoptosis and tumor suppression (4-7). Puma knockout mice show defects from multiple apoptotic stimuli, including ionizing irradiation, deregulated c-Myc expression, and cytokine withdrawal (4).

$262
3 nmol
300 µl
SignalSilence® Vitamin D3 Receptor siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit vitamin D3 receptor 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: Although originally identified based on their roles in calcium and bone homeostasis, the vitamin D3 receptor (VDR/NR1I1) and its ligand 1-α, 25-dihydroxycholecalciferol [1α, 25(OH)2D3] are now recognized to exert biological effects in almost every tissue of the human body. Targets for vitamin D signaling include the central nervous system, skin, immune system, endocrine glands, kidney, and colon. At the cellular level, vitamin D signaling affects proliferation, differentiation, and apoptosis of both normal and transformed cells. Within the steroid receptor gene family, VDR belongs to the NR1I subfamily that also includes NR1I2/PXR and NR1I3/CAR. The human VDR gene is composed of 11 exons that encode six domains (A-F) of the full length VDR protein, which includes an N-terminal dual zinc finger DNA binding domain, a C-terminal ligand-binding activity domain, and an extensive unstructured region that links the two functional domains together (1). Upon 1α, 25(OH)2D3 binding to the hormone ligand-binding domain, VDR is stabilized by the phosphorylation of Ser51 in the DNA-binding domain by PKC (2), and Ser208 in the hinge region by casein kinase II (3). VDR associates with the retinoic acid receptor (RXR) through dimerization domains. The 1α, 25(OH)2D3-VDR-RXR complex binds to the vitamin D response elements (VDREs) in the promoters of target genes through the DNA-binding domain. Ligand-induced conformation changes in VDR results in the dissociation of the co-repressor, silencing-mediator for retinoid and thyroid hormone receptors (SMRT), and allows interaction of the VDR activation function (AF2) transactivation domain with transcriptional coactivators (1).Studies have shown that variable VDR expression is associated with different forms or stages of cancer and likely results from tissue-type variation in 1α, 25(OH)2D3 signaling. In the case of colon cancer, research indicates that VDR expression is relatively higher in hyperplastic colon polyps and during early tumorigenesis but diminishes in later stage, poorly differentiated tumors. Multiple studies suggest that 1α, 25(OH)2D3 may be an attractive target for development as a therapeutic anticancer agent (4,5) .

This peptide is used to specifically block β-Actin (13E5) Rabbit mAb #4970 by dot blot.

Background: Actin, a ubiquitous eukaryotic protein, is the major component of the cytoskeleton. At least six isoforms are known in mammals. Nonmuscle β- and γ-actin, also known as cytoplasmic actin, are predominantly expressed in nonmuscle cells, controlling cell structure and motility (1). α-cardiac and α-skeletal actin are expressed in striated cardiac and skeletal muscles, respectively; two smooth muscle actins, α- and γ-actin, are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. These actin isoforms regulate the contractile potential of muscle cells (1). Actin exists mainly as a fibrous polymer, F-actin. In response to cytoskeletal reorganizing signals during processes such as cytokinesis, endocytosis, or stress, cofilin promotes fragmentation and depolymerization of F-actin, resulting in an increase in the monomeric globular form, G-actin (2). The ARP2/3 complex stabilizes F-actin fragments and promotes formation of new actin filaments (2). Research studies have shown that actin is hyperphosphorylated in primary breast tumors (3). Cleavage of actin under apoptotic conditions has been observed in vitro and in cardiac and skeletal muscle, as shown in research studies (4-6). Actin cleavage by caspase-3 may accelerate ubiquitin/proteasome-dependent muscle proteolysis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Aprataxin is a DNA repair protein that resolves DNA lesions (DNA adenylates) caused by abortive ligations in single-strand break repair, double-strand break repair and base excision repair (1). Aprataxin is recruited to sites of DNA damage by PARP1 (2). In the mitochondria, aprataxin and tyrosyl-DNA-phosphodiesterase 1 (TDP1) are required for repair of single strand breaks caused primarily by reactive oxygen species (ROS) (3).The gene for aprataxin, APTX, is defective in the neurodegenerative disorder oculomotor apraxia type 1 (AOA1)(4). Researchers have shown that levels of aprataxin can predict patient response to irinotecan-based treatments in colorectal cancer (5).

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

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin)

Background: The human DAZ (Deleted in Azoospermia) gene family contains at least three members that encode RNA-binding proteins with a common RNA-recognition motif (1). An autosomal homolog of DAZ, DAZL (DAZ-like), is specifically expressed in germ cells and is essential for the specification of the germ cell lineage during embryogenesis and during gametogenesis in adults of both sexes (2,3). DAZL may function by directly recruiting poly(A)-binding proteins (PABPs) in order to activate silent mRNAs during germ cell development (2). Deletions encompassing the Y chromosomal DAZ genes are the most common molecularly defined cause of infertility in humans (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin. The inherited localization of the centromere is specified by CENP-A (1). CENP-A deposition to the correct chromosomal location in early G1 phase is regulated by the Mis18 complex, which consists of Mis18-alpha, Mis18-beta, Mis18BP1, RbAp48 and RbAp46 (2).Mis18-alpha deficiency in mice results in inappropriate localization of CENP-A, as well as DNA methylation defects (3). Localization of the Mis18 complex to centromeres is regulated by the mitotic kinase Plk1 (polo-like kinase 1) (4).

$229
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: NCAM (neural cell adhesion molecule, CD56) is an adhesion glycoprotein with five extracellular immunoglobulin-like domains followed by two fibronectin type III repeats. Structural diversity is introduced by alternative splicing resulting in different cytoplasmic domains (1). NCAM mediates neuronal attachment, neurite extension and cell-cell interactions through homo and heterophilic interactions. PSA (polysialic acid) post-translationally modifies NCAM and increases the metastatic potential of small cell lung carcinoma, Wilms+ tumor, neuroblastoma and rhabdomyosarcoma (2). CD56 and CD16 are commonly used to identify NK cells although some cells with the T cell markers CD3 and CD4 also express CD56 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cellular levels of mRNAs are controlled by mRNA stability, the rate of synthesis and the rate of degradation. The presence and length of the poly(A) tail has been associated with mRNA stability (1). Exonucleolytic shortening of the poly(A) tail is the process that initiates the decay of many eukaryotic mRNAs (2). Poly(A)-specific ribonuclease (PARN) is the enzyme responsible for initiation of deadenylation and exonucleolytic shortening of mRNA transcripts. Through an evolutionarily conserved mechanism, PARN also translationally silences selective mRNAs during early embryonic development (3). PARN is constitutively expressed in most mammalian tissues and plays a critical role in the post-transcriptional control of gene expression (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Platelet derived growth factor (PDGF) proteins function as dimeric isoforms (i.e., PDGF AA, PDGF AB, PDGF BB, PDGF CC and PDGF DD) that bind receptor tyrosine kinases and activate cytoplasmic SH2 domain-containing proteins to control multiple signaling pathways that regulate angiogenesis, cell growth, actin reorganization, migration and differentiation (1). PDGFA-associated protein 1 (PDAP1) was originally identified as a novel, PDGF-associated protein found in a rat retinal tumor cell line (2). While copurified with PDGFA, PDAP1 interacts with PDGFB at a slightly higher affinity than with PDGFA (2). Although the exact function of PDAP1 is unclear, it has been shown to both increase PDGFA-induced incorporation of [3H]thymidine in Swiss 3T3 cells and decrease PDGFB growth factor activity (2). Ubiquitously expressed PDAP1 is highly conserved among species (2,3) and is phosphorylated in vitro by several kinases, including PKC, PKA, CKI and CKII. Among this group, CKII seems to be the major kinase that phosphorylates PDAP1 in intact cells (3).