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Product listing: Argonaute 4 (D10F10) Rabbit mAb, UniProt ID Q9HCK5 #6913 to Cleaved Drosophila ICE (drICE) (Asp230) Antibody, UniProt ID O01382 #9478

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Small non-coding RNAs are important regulators of gene expression in higher eukaryotes (1,2). Several classes of small RNAs, including short interfering RNAs (siRNAs) (3), microRNAs (miRNAs) (4), and Piwi-interacting RNAs (piRNAs) (5), have been identified. MicroRNAs are about 21 nucleotides in length and have been implicated in many cellular processes such as development, differentiation, and stress response (1,2). MicroRNAs regulate gene expression by modulating mRNA translation or stability (2). MicroRNAs function together with the protein components in the complexes called micro-ribonucleoproteins (miRNPs) (2). Among the most important components in these complexes are Argonaute proteins (1,2). There are four members in the mammalian Argonaute family and only Argonaute 2 (Ago2) possesses the Slicer endonuclease activity (1,2). Argonaute proteins participate in the various steps of microRNA-mediated gene silencing, such as repression of translation and mRNA turnover (1).

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

Application Methods: Western Blotting

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

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 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 cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated LEF1 (C12A5) Rabbit mAb #2230
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

$489
96 assays
1 Kit
The PathScan® Phospho-PDGF Receptor α/β (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of PDGF receptor α/β when tyrosine phosphorylated. A PDGF Receptor α/β Rabbit Antibody has been coated onto the microwells. After incubation with cell lysates, PDGF Receptor α/β (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a Biotinylated Phospho-Tyrosine Mouse Detection Antibody is added to detect tyrosine phosphorylation of the captured PDGF receptor α/β protein. HRP-linked Strepavidin is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of PDGF receptor α/β phosphorylated on tyrosine.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Myoglobin (MB) is an oxygen-binding protein that contains one polypeptide chain and one heme group. It is expressed in vertebrate skeletal and cardiac muscles where it plays an essential role in the storage and transport of oxygen to mitochondria. Reversible oxygen binding occurs by a linkage with the imidazole nitrogen of the 91st histidine residue in the myoglobin chain. Research studies indicate that the blockade of myoglobin in isolated cardiac myocytes mimics hypoxia when electrically stimulated for paced contractions (1). During fetal development, myoglobin is required to support cardiac function (2). Diving mammals are known to have high concentrations of myoglobin in their blood, which may contribute to their ability to endure long periods of oxygen deprivation during deep dives (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PEA-15 is a 15 kDa phosphoprotein expressed abundantly in astrocytes and fibroblasts as well as in tissues, including the lung and eye (1). The protein has been shown to coordinate cell growth, death, and glucose utilization (2-4). The amino-terminal DED domain of PEA-15 mediates its binding to FADD or Erk and further regulates the Erk and apoptosis signaling pathways. PEA-15 can be phosphorylated at two serine residues, Ser104 and Ser116, located within the carboxy terminus. Phosphorylation at these sites regulates binding to Erk and FADD (2,3).

$262
50-100 transfections
300 µl
SignalSilence® Survivin siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit survivin 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: 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, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Dog, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) respectively (1,2). DUBs are categorized into five subfamilies-USP, UCH, OTU, MJD, and JAMM. Ubiquitin-specific protease 9, X-linked (USP9X) possesses a well-conserved catalytic domain with cysteine peptidase activity, which allows for cleavage of ubiquitin and polyubiquitin conjugates. USP9X is the mammalian homolog of the Drosophila fat-facets (faf) gene, which is essential for normal eye development and viability of the early fly embryo (3,4). While USP9X expression is also critical for normal mammalian development (5-7), many of its substrates are only beginning to be elucidated. There is mounting evidence that USP9X functions in the formation of epithelial cell-cell contacts through deubiquitination-dependent stabilization of molecules involved in maintaining the integrity of both adherens and tight junctions. Indeed, USP9X has been found to associate with AF-6, the β-catenin-E-cadherin complex, and EFA6 (8-11). Research studies have also demonstrated that USP9X is an integral component of the TGF-β/BMP signaling cascade by opposing TRIM33-mediated monoubiquitination of SMAD4 (12). USP9X is overexpressed in a variety of human cancers and contributes to enhanced cell survival, in part, through its ability to deubiquitinate and stabilize the Mcl-1 oncoprotein (13). There is some evidence, however, that suggests the role of USP9X in tumorigenesis is context dependent. Research studies have implicated USP9X in a tumor suppressor role during the early stages of pancreatic ductal adenocarcinoma (PDAC) and in an oncogenic role during advanced stages of PDAC (14,15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dihydropyrimidine dehydrogenase (DPD, DPYD) catalyzes the initial and rate-limiting step in uracil and thymidine catabolism as well as catabolism of the chemotherapeutic drug 5-fluorouracil (5-FU) and its derivatives. DPYD deficiency, which results from mutations in the DPYD gene, causes errors in pyrimidine metabolism and potentially life-threatening side effects in cancer patients treated with 5-FU (reviewed in 1). As a result, ongoing work examines whether or how DPYD gene variation and protein expression can be used to predict 5-FU toxicity (1,2). Several genes that impart resistance to 5-FU were recently identified in human hepatocellular carcinoma (HCC). AEG-1, which is highly expressed in HCC, increases the expression of DPYD. DPYD is expressed more highly in HCC than in normal liver, and this is thought to be one mechanism of 5-FU resistance (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex plays a critical role in cell growth regulation (1, 2). mTORC1 activity is modulated by cellular environmental factors (e.g., energy levels, growth factors, amino acids) (3, 4), which are mediated through a protein complex known as GATOR (GAP Activity Towards Rags) (5). GATOR is comprised of two protein subcomplexes (GATOR1 and GATOR2), that function in opposing fashion to regulate mTORC1 activity (5). WDR59 was identified as a component of the GATOR2 subcomplex (also containing Mios, WDR24, Seh1L and Sec13), that functions to positively regulate mTORC1 activity (5). Conversely, the GATOR1 subcomplex (containing DEPDC5, Nprl2 and Nprl3), negatively regulates mTORC1 activity, through activation of RagA and RagB GTPases (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Apolipoproteins are plasma lipoproteins that function as transporters of lipids and cholesterol in the circulatory system. Chylomicrons are a fundamental class of apolipoproteins containing very low-density lipoproteins (VLDL), intermediate-density lipoproteins (IDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nerve growth factor (NGF) is a small, secreted protein and member of the neurotrophin family of growth factors that promote neuronal cell survival and differentiation (1). Producing cells release NGF that bind and activate TrkA high affinity receptors to mediate NGF-driven signaling. NGF also binds to a low affinity p75 (NTR) receptors, which belong to the death receptor family (2). Although NGF has been classically described as favoring neuron survival and differentiation, nerve growth factor can promote apoptosis in cells that contain p75 (NTR) and lack TrkA. NGF can induce neuron death in a variety of neurodegenerative conditions, including Alzheimer disease (3). Besides its neurotrophic actions, NGF has an effect on non-neuronal cells and may help mediate inflammation, angiogenesis, and stimulate breast cancer cell growth (4-6). NGF signaling is looking increasingly promising as potential drug targets for diseases.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Praja-2 (PJA2/RNF131) is a RING-H2-type E3 ubiquitin ligase. PJA2 is highly expressed in neural tissue and research studies have shown that PJA2 plays a role modulating synaptic archictecture and long-term memory by promoting the ubiquitin-dependent proteolysis of NOGO-A and PKA regulatory subunits (1,2). Research studies have also shown that PJA2 sustains gliobastoma growth by driving the ubiquitin-dependent proteasomal degradation of MOB, which inactivates the LATS tumor suppressor kinase of the Hippo pathway (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: α-Actinin belongs to the spectrin family of cytoskeletal proteins. It was first recognized as an actin cross-linking protein, forming an antiparallel homodimer with an actin binding head at the amino terminus of each monomer. The α-actinin protein interacts with a large number of proteins involved in signaling to the cytoskeleton, including those involved in cellular adhesion, migration, and immune cell targeting (1). The interaction of α-actinin with intercellular adhesion molecule-5 (ICAM-5) helps to promote neurite outgrowth (2). In osteoblasts, interaction of α-actinin with integrins stabilizes focal adhesions and may protect cells from apoptosis (3). The cytoskeletal α-actinin isoforms 1 and 4 (ACTN1, ACTN4) are non-muscle proteins that are present in stress fibers, sites of adhesion and intercellular contacts, filopodia, and lamellipodia. The muscle isoforms 2 and 3 (ACTN2, ACTN3) localize to the Z-discs of striated muscle and to dense bodies and plaques in smooth muscle (1).

$314
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: N-myc downstream-regulated gene 1 (NDRG1), also termed Cap43, Drg1, RTP/rit42, and Proxy-1, is a member of the NDRG family, which is composed of four members (NDRG1-4) that function in growth, differentiation, and cell survival (1-5). NDRG1 is ubiquitously expressed and highly responsive to a variety of stress signals including DNA damage (4), hypoxia (5), and elevated levels of nickel and calcium (2). Expression of NDRG1 is elevated in N-myc defective mice and is negatively regulated by N- and c-myc (1,6). During DNA damage, NDRG1 is induced in a p53-dependent fashion and is necessary for p53-mediated apoptosis (4,7). Research studies have shown that NDRG1 may also play a role in cancer progression by promoting differentiation, inhibiting growth, and modulating metastasis and angiogenesis (3,4,6,8,9). Nonsense mutation of the NDRG1 gene has been shown to cause hereditary motor and sensory neuropathy-Lom (HMSNL), which is supported by studies demonstrating the role of NDRG1 in maintaining myelin sheaths and axonal survival (10,11). NDRG1 is up-regulated during mast cell maturation and its deletion leads to attenuated allergic responses (12). Both NDRG1 and NDRG2 are substrates of SGK1, although the precise physiological role of SGK1-mediated phosphorylation is not known (13). NDRG1 is phosphorylated by SGK1 at Thr328, Ser330, Thr346, Thr356, and Thr366. Phosphorylation by SGK1 primes NDRG1 for phosphorylation by GSK-3.

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) 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 Histone H2A.X (D17A3) XP® Rabbit mAb #7631.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: Histone H2A.X is a variant histone that represents approximately 10% of the total H2A histone proteins in normal human fibroblasts (1). H2A.X is required for checkpoint-mediated cell cycle arrest and DNA repair following double-stranded DNA breaks (1). DNA damage, caused by ionizing radiation, UV-light, or radiomimetic agents, results in rapid phosphorylation of H2A.X at Ser139 by PI3K-like kinases, including ATM, ATR, and DNA-PK (2,3). Within minutes following DNA damage, H2A.X is phosphorylated at Ser139 at sites of DNA damage (4). This very early event in the DNA-damage response is required for recruitment of a multitude of DNA-damage response proteins, including MDC1, NBS1, RAD50, MRE11, 53BP1, and BRCA1 (1). In addition to its role in DNA-damage repair, H2A.X is required for DNA fragmentation during apoptosis and is phosphorylated by various kinases in response to apoptotic signals. H2A.X is phosphorylated at Ser139 by DNA-PK in response to cell death receptor activation, c-Jun N-terminal Kinase (JNK1) in response to UV-A irradiation, and p38 MAPK in response to serum starvation (5-8). H2A.X is constitutively phosphorylated on Tyr142 in undamaged cells by WSTF (Williams-Beuren syndrome transcription factor) (9,10). Upon DNA damage, and concurrent with phosphorylation of Ser139, Tyr142 is dephosphorylated at sites of DNA damage by recruited EYA1 and EYA3 phosphatases (9). While phosphorylation at Ser139 facilitates the recruitment of DNA repair proteins and apoptotic proteins to sites of DNA damage, phosphorylation at Tyr142 appears to determine which set of proteins are recruited. Phosphorylation of H2A.X at Tyr142 inhibits the recruitment of DNA repair proteins and promotes binding of pro-apoptotic factors such as JNK1 (9). Mouse embryonic fibroblasts expressing only mutant H2A.X Y142F, which favors recruitment of DNA repair proteins over apoptotic proteins, show a reduced apoptotic response to ionizing radiation (9). Thus, it appears that the balance of H2A.X Tyr142 phosphorylation and dephosphorylation provides a switch mechanism to determine cell fate after DNA damage.

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Prostatic Acid Phosphatase (ACPP or PAP) is a member of the histidine acid phosphatase family. It is a non-specific phosphatase that is capable of dephosphorylating tyrosine residues as well as phospholipids under mildly acidic conditions. ACPP has ecto-5'-nucleotidase activity in pain-sensing neurons where it converts AMP to adenosine, suppressing the pain response (1,2). ACPP occurs as two isoforms that are both heavily glycosylated. The secreted phosphatase (sPAP) is found predominantly in the prostate and seminal plasma, while the cellular isoform (cPAP) is broadly expressed at very low levels and is associated with the plasma and lysosomal membranes (3-5). Cellular PAP has been shown to dephosphorylate ErbB2 at various tyrosine residues effectively terminating signaling (6). Furthermore, the physical interaction between cPAP and ErbB2 appears to regulate androgen sensitivity in prostate cancer cells. Loss of cPAP in androgen-sensitive prostate cancer cells results in the development of a castration-resistant phenotype suggesting that ACPP plays a significant role in prostate cancer cell growth (7). ACPP is expressed in metastatic cells arising from prostate cancer - especially in prostate-derived bone metastasis - suggesting that it may be a relevant diagnostic indicator of prostate cancer re-emergence in bone (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, 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).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Nicastrin is a transmembrane glycoprotein serving as an essential component of the γ-secretase complex (1,2). Nicastrin is physically associated with presenilin and plays an important role in the stabilization and correct localization of presenilin to the membrane-bound γ-secretase complex (3). Nicastrin also serves as a docking site for γ-secretase substrates such as APP and Notch, directly binding to them and properly presenting them to γ-secretase to ensure the correct cleavage process (2,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TROP2 is a transmembrane glycoprotein encoded by gene TACSTD2 (tumor associated calcium signal transducer 2). TROP2 was first discovered as a biomarker of invasive trophoblast cells and later reported in many types of cancer cells as well as in various organs during development, and adult stem cells during homeostasis (1, 2). TROP2 has an extracellular domain with EGF thyroglobulin type-1 repeats, a transmembrane domain and a short cytoplasmic tail with a HIKE domain containing a PIP2 binding site and PKC phosphoryaltion site (Ser303) (1-4). TROP2 functions by regulating multiple signaling pathways including-interaction of extracellular domain with integrin beta1 to regulate FAK signaling, association of its transmembrane domain with claudin1 and claudin7 for tight junction formation, as well as regulation of intracellular calcium release by its PIP2 binding and activation of the ERK/MAPK pathway (1,2, 5-8). All of these functions are important for its role in tumor proliferation, metastasis and invasion (1,2). PKC can phosphorylate TROP2 at Ser303; the phosphorylation changes the cytoplasmic tail conformation and further promotes its signaling (9). TROP2 can be activated through intramembrane proteolysis first by TACE, followed further cleavage by presenilin 1 and presenilin2. The proteolysis process is required for its role in tumor cell proliferation (10,11).

$262
3 nmol
300 µl
SignalSilence® SAPK/JNK siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit SAPK/JNK expression by 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 stress-activated protein kinase/Jun-amino-terminal kinase SAPK/JNK is potently and preferentially activated by a variety of environmental stresses including UV and gamma radiation, ceramides, inflammatory cytokines, and in some instances, growth factors and GPCR agonists (1-6). As with the other MAPKs, the core signaling unit is composed of a MAPKKK, typically MEKK1-MEKK4, or by one of the mixed lineage kinases (MLKs), which phosphorylate and activate MKK4/7. Upon activation, MKKs phosphorylate and activate the SAPK/JNK kinase (2). Stress signals are delivered to this cascade by small GTPases of the Rho family (Rac, Rho, cdc42) (3). Both Rac1 and cdc42 mediate the stimulation of MEKKs and MLKs (3). Alternatively, MKK4/7 can be activated in a GTPase-independent mechanism via stimulation of a germinal center kinase (GCK) family member (4). There are three SAPK/JNK genes each of which undergoes alternative splicing, resulting in numerous isoforms (3). SAPK/JNK, when active as a dimer, can translocate to the nucleus and regulate transcription through its effects on c-Jun, ATF-2, and other transcription factors (3,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Ajuba belongs to the Zyxin/Ajuba family, members of which include LIMD1, LPP, Trip6 and Zyxin. Three LIM domains at the carboxy-terminus characterize this family of proteins. Zyxin/Ajuba family members associate with the actin cytoskeleton, are components of both cell-cell junction adhesive complex and integrin-mediated adhesive complex, and shuttle in and out of the nucleus (1). Ajuba is involved in Rac activation during cell migration and activates Aurora A in order to commit to mitosis (2-3). Ajuba and its family members also have an amino-terminal proline-rich pre-LIM region, and Ajuba augments ERK activation in a Ras-dependent manner (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: SSU72 is a protein phosphatase originally identified through its interaction with TFIIB as a factor required for transcription and RNA processing (1,2). While SSU72 has been known as a phosphatase of the RNA polymerase II carboxy-terminal domain at Ser5 of the heptapeptide repeat, additional studies suggest a role for SSU72 as a phosphatase for Ser7 of the heptapeptide repeat as well (3-9). The activities of SSU72 are thought to play a critical role in coupling transcription with pre-mRNA 3’ end processing (10-12). SSU72 is required for gene looping that connects the gene promoter with the terminator region, leading to proper initiation of transcription and enforcement of transcriptional directionality on promoters that may other wise act as bidirectional promoters (13-14). In addition to a role in transcription, SSU72 acts as a cohesin binding protein that regulates cohesion between sister chromatid arms during mitosis or meiosis (15).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 700 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 CD45 (D9M8I) XP® Rabbit mAb #13917.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The protein phosphatase (PTP) receptor CD45 is a type I transmembrane protein comprised of a pair of intracellular tyrosine phosphatase domains and a variable extracellular domain generated by alternative splicing (1). The catalytic activity of CD45 is a function of the first phosphatase domain (D1) while the second phosphatase domain (D2) may interact with and stabilize the first domain, or recruit/bind substrates (2,3). CD45 interacts directly with antigen receptor complex proteins or activates Src family kinases involved in the regulation of T- and B-cell antigen receptor signaling (1). Specifically, CD45 dephosphorylates Src-family kinases Lck and Fyn at their conserved negative regulatory carboxy-terminal tyrosine residues and upregulates kinase activity. Conversely, studies indicate that CD45 can also inhibit Lck and Fyn by dephosphorylating their positive regulatory autophosphorylation site. CD45 appears to be both a positive and a negative regulator that conducts signals depending on specific stimuli and cell type (1). Human leukocytes including lymphocytes, eosinophils, monocytes, basophils, and neutrophils express CD45, while erythrocytes and platelets are negative for CD45 expression (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Lamins and lamin associated proteins are the major components of nuclear lamina found between the inner nuclear membrane and the peripheral chromatin. These proteins play important roles in maintaining nuclear structure, chromatin organization, DNA replication, cell cycle regulation, and apoptosis (1-3). Lamins are type V intermediate filaments that are further classified into type A and type B lamin proteins. Type A lamins (including lamin A and the smaller lamin C splice variant) are predominately expressed in terminally differentiated cells, whereas type B lamins (lamin B1, lamin B2) are encoded by distinct genes and are expressed constitutively. Cleavage of lamins by caspases occurs during apoptosis as part of the disassembly of the cell (4-6). A number of lamina-associated proteins contribute to the nuclear lamina and include the lamin B receptor, LAP1, LAP2, emerin, MAN1, otefin, and YA. Several isoforms of lamina-associated polypeptide 2 (LAP2, also known as thymopoietin or TMPO) have been described, with the α, β, and γ isoforms most abundant in humans (7-10). Structurally similar LAP2β and LAP2γ are type II integral membrane proteins. LAP2α has a unique carboxy-terminus that lacks a transmembrane region and results in localization of LAP2α throughout the nucleus where it can associate with lamin A/C (10). LAP2α is also thought to contribute to the nuclear anchorage of retinoblastoma protein (Rb) and control cell cycle progression (11). LAP2α is also targeted for cleavage by caspases, which may contribute to changes in chromatin structure during apoptosis (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The family of Trk receptor tyrosine kinases consists of TrkA, TrkB, and TrkC. While the sequence of these family members is highly conserved, they are activated by different neurotrophins: TrkA by NGF, TrkB by BDNF or NT4, and TrkC by NT3 (1). Neurotrophin signaling through these receptors regulates a number of physiological processes, such as cell survival, proliferation, neural development, and axon and dendrite growth and patterning (1). In the adult nervous system, the Trk receptors regulate synaptic strength and plasticity. TrkA regulates proliferation and is important for development and maturation of the nervous system (2). Phosphorylation at Tyr490 is required for Shc association and activation of the Ras-MAP kinase cascade (3,4). Residues Tyr674/675 lie within the catalytic domain, and phosphorylation at these sites reflects TrkA kinase activity (3-6). Point mutations, deletions, and chromosomal rearrangements (chimeras) cause ligand-independent receptor dimerization and activation of TrkA (7-10). TrkA is activated in many malignancies including breast, ovarian, prostate, and thyroid carcinomas (8-13). Research studies suggest that expression of TrkA in neuroblastomas may be a good prognostic marker as TrkA signals growth arrest and differentiation of cells originating from the neural crest (10).

$303
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster

Application Methods: Western Blotting

Background: Cell death in the fruit fly Drosophila melanogaster is regulated by many of the same stimuli as mammalian cell death (1). The Drosophila genome contains seven caspase genes; three encode initiator caspases and four encode effector caspases (reviewed in 2). drICE is a cysteine protease that cleaves baculovirus p35 and lamin DmO in vitro and acts downstream of rpr (3). drICE is proteolytically processed during apoptosis into active p21 and p12 subunits. Comparison of the in vivo activity between drICE and Dcp-1 has shown that drICE is a more effective inducer of apoptosis than Dcp-1, which plays a role in determining the rate of cell death (4).