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Product listing: AHSA1 Antibody, UniProt ID O95433 #12841 to MCP-1 Antibody (Carboxy-terminal Antigen), UniProt ID P13500 #39091

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

Application Methods: Western Blotting

Background: Activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1 or AHA1) is a 42 kDa HSP90 co-chaperone that stimulates intrinsic HSP90 ATPase activity in eukaryotic cells to facilitate client protein folding and activation (1,2). Initially, HSP90 forms a ternary complex with a nascent client protein such as v-Src, c-Raf or CFTR, and the co-chaperone protein CDC37 (3,4). HSP90 then cycles through a series of conformational changes facilitated by ATP that results in the release of CDC37 and recruitment of AHSA1 - a process that is dependent on tyrosine phosphorylation of HSP90 and CDC37 (5). More recently, AHSA1 has been shown to have unique interactions with additional client proteins involved in RNA splicing and DNA repair, suggesting that AHSA1 may have also have a scaffolding role in recruiting client proteins to HSP90 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The cohesin protein complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). WAPL, also wings apart-like or WAPAL, is a chromatin-associated protein that binds to the cohesin protein complex and regulates its function and its interaction with chromatin (3,4). WAPL, through its interaction with cohesin, is important in the regulation of chromosome structure, cell cycle progression and appropriate chromosome segregation (5,6). Depletion of WAPL leads to segregation errors and DNA damage, and in p53 deficient cells leads to aneuploidy (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Aminopeptidase N (APN, CD13) is a widely expressed, membrane-bound proteolytic enzyme that breaks down peptides during digestion, cleaves cell surface antigens during antigen presentation, and acts as a receptor for human viruses, including several coronaviruses. This multifunctional protein is implicated in the regulation of many biological processes, including angiogenesis, cell proliferation, cell migration, inflammation and immune response (1,2). APN was originally identified as the cell surface antigen CD13, which is expressed in myeloid lineage hematopoietic cells and myeloid leukemia (3). Identified substrates of aminopeptidase N include the angiotensin I-III peptide hormones, the opioid peptide met-enkephalin, and cytokines MCP-1 and MIP-1 (4). Abnormal APN protein expression is seen in various forms of cancer, with high APN expression associated with poor survival in colon cancer and non-small cell lung cancer and silenced APN expression related to poor prognosis in prostate cancer (5-7).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Gremlin is a secreted antagonist of bone morphogenetic proteins that play important roles during development. Gene targeting generates gremlin deficient mice that die shortly after birth due to absent kidneys and defects in lung septation (1-3). Gremlin also plays a role in cardiomyogenesis and angiogenesis (4,5). TGF-β can induce gremlin expression under pathological conditions. Gremlin colocalizes with TGF-β in tubulointerstitial fibrosis associated with chronic allograft nephropathy and is expressed in diabetic nephropathy in vivo (6-8). Gremlin is widely expressed in cancer associated stromal cells and can enhance cancer cell proliferation (9).

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

Application Methods: Western Blotting

Background: Protein phosphatase type 2A (PP2A) is an essential protein serine/threonine phosphatase that is conserved in all eukaryotes. PP2A is a key enzyme within various signal transduction pathways as it regulates fundamental cellular activities such as DNA replication, transcription, translation, metabolism, cell cycle progression, cell division, apoptosis and development (1-3). The core enzyme consists of catalytic C and regulatory A (or PR65) subunits, with each subunit represented by α and β isoforms (1). Additional regulatory subunits belong to four different families of unrelated proteins. Both the B (or PR55) and B' regulatory protein families contain α, β, γ and δ isoforms, with the B' family also including an ε protein. B'' family proteins include PR72, PR130, PR59 and PR48 isoforms, while striatin (PR110) and SG2NA (PR93) are both members of the B''' regulatory protein family. These B subunits competitively bind to a shared binding site on the core A subunit (1). This variable array of holoenzyme components, particularly regulatory B subunits, allows PP2A to act in a diverse set of functions. PP2A function is regulated by expression, localization, holoenzyme composition and post-translational modification. Phosphorylation of PP2A at Tyr307 by Src occurs in response to EGF or insulin and results in a substantial reduction of PP2A activity (4). Reversible methylation on the carboxyl group of Leu309 of PP2A has been observed (5,6). Methylation alters the conformation of PP2A, as well as its localization and association with B regulatory subunits (6-8).

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

Application Methods: Western Blotting

Background: Raf kinase inhibitor protein (RKIP) is a member of the phosphatidylethanolamine-binding protein (PEBP) family that associates with Raf-1 and the MEK and MAP kinases (1). RKIP has been shown to form a complex with Raf-1, MEK, and Erk (2). Although MEK and Erk can simultaneously bind RKIP, the association between Raf-1 and RKIP and that of RKIP and MEK are mutually exclusive. Thus, RKIP competitively disrupts the Raf-1-MEK complex and effectively terminates signal transmission from Raf-1 to MAP kinases (2). The inhibitory effect of RKIP on MAP kinase signaling is eliminated by PKC phosphorylation of RKIP at Ser153 (3). PKC phosphorylation on Ser153 also promotes the association of RKIP with GRK2, which prevents GRK2-dependent internalization of GPCR (4). RKIP also interacts with modules of the NF-κB pathway, including NF-κB-inducing kinase (NIK), TAK1, IKKα and IKKβ (5). These interactions antagonize cytokine-induced activation of the NF-κB pathway (5). Restoration of RKIP expression is associated with the inhibition of prostate cancer metastasis, implying that RKIP may be a potential clinical target as a suppressor of tumor metastasis through inhibition of vascular invasion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: ETS-2 is a member of the E26 Transformation-specific Sequence (ETS) transcription factor family, members of which bind to a core GGAA/T DNA sequence in the promoter region of target genes to activate gene expression (1). ETS-2 activates expression of a wide variety of target genes, including MMPs, TERT, TCR, uPA, and oncogenic miRNAs (2-4). It's activity has been shown to be important for cell growth and differentiation, bone formation, autoimmune disease, and cancer progression (5-7). Phosphorylation by MAP kinase at Thr72 upregulates the function of ETS-2, suggesting that therapeutic strategies targeting ETS-2 may provide an alternative to MEK inhibitor therapy (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Brain-specific kinase 1 (BRSK1; SAD-B) and Brain-specific kinase 2 (BRSK2; SAD-A) are serine/threonine kinases closely related to AMPK. LKB1 phosphorylates Thr189 in the T-loop of BRSK1 and Thr174 in the T-loop of BRSK2, resulting in activation of the kinases (1). BRSK1 localizes to synaptic vesicles in the hippocampus and cerebellum, together with the active zone proteins Bassoon and CAST, and BRSK1 phoshorylates the active zone protein RIM1 (2). An alternatively spliced from of BRSK1 displays unique activity during the cell cycle, phosphorylating Ser131 of γ-tubulin and controling centrosome duplication (3). Neuronal polarization, including axon formation, is fundamental for normal brain development. BRSK1 -/- and BRSK2 -/- mice have defects in neuronal polarity and impaired corticogenesis (4). Knockdown of BRSK1 and BRSK2 in vitro diminishes axonal growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Bif-1/SH3GLB1/Endophilin-B1 is a member of the endophilin B family that was originally identified as a Bax binding protein through yeast two-hybrid screening (1,2). Bif-1 does not have significant homology to other Bcl-2 family members, but rather contains an N-terminal Bin-Amphiphysin-Rvs (BAR) domain, typically involved in membrane dynamics, and a C-terminal SH3 domain. Overexpression of Bif-1 promotes Bax conformational change and apoptosis (2,3). Likewise, loss of Bif-1 inhibits Bax and Bak activation, cytochrome c release, and caspase activation (3). Bif-1 is localized to membranes of intracellular organelles and has been suggested to play a role in membrane dynamics, including that during autophagy. Bif-1 directly binds to UVRAG, forming a complex with Beclin-1, resulting in increased PI3-kinase class III/Vps34 activity required for autophagosome maturation (4). Inhibition of GSK-3β, as seen during nutrient deprivation, results in increased expression of Bif-1, and can contribute to autophagic cell death (5). Research studies have shown that loss of Bif-1 promotes tumorigenesis, and decreased expression of Bif-1 has been noted in several cancer types (6-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dickkopf (DKK) family proteins consist of four members DKK1, DKK2, DKK3 and DKK4 that function as secreted Wnt antagonists by inhibiting Wnt coreceptors LRP5 and LRP6 (1,2). DKKs contain two cysteine-rich domains in which the positions of 10 cysteine residues are well conserved (3). Their expression is both temporally and spatially regulated during animal development (4). DKKs also bind with high affinity to transmembrane proteins Kremen1 and 2, which themselves also modulate Wnt signaling (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MKK3 and MKK6 are two closely related dual-specificity protein kinases that activate p38 MAP kinase (1-5). MKK3 and MKK6 both phosphorylate and activate p38 MAP kinase at its activation site, Thr-Gly-Tyr, but do not phosphorylate or activate Erk1/2 or SAPK/JNK. Phosphorylation of p38 MAP kinase dramatically stimulates its ability to phosphorylate protein substrates such as ATF-2 and Elk-1. MKK3 and MKK6 are both activated by different forms of cellular stress and inflammatory cytokines (4,5). Activation of MKK3 and MKK6 occurs through phosphorylation at Ser189 and Thr222 on MKK3 (2) and Ser207 and Thr211 on MKK6 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Pumilio 1 and Pumilio 2 (PUM1, PUM2, or Pumilio homolog 1 and 2, respectively) are evolutionarily conserved RNA binding proteins that are thought to repress translation and stability of mRNA targets by binding to the 3'-UTR of specific RNA sequences (1). Pumilio proteins have been implicated in the regulation of genes involved in embryogenesis and germline cell development (2). Research studies have shown that PUM2 may have a role in neural stem cell fate decisions (3).

$262
3 nmol
300 µl
SignalSilence® Rictor siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit rictor 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: Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian TOR (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor-derived signals (1). mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, Sin1, and rictor (1). The mTOR-rictor complex phosphorylates Ser473 of Akt/PKB in vitro (2). This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3-L1 adipocytes (3). This complex has also been shown to phosphorylate the rapamycin-resistant mutants of S6K1, another effector of mTOR (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Arginase-2 is a mitochondrial enzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea (1). Research studies have shown that in acute myeloid leukemia (AML) patients, arginase-2 is released from AML blasts to the plasma, leading to the suppression of T-cell proliferation (2). It was also shown that arginase-2 is required for the immunosuppressive properties of neonatal CD71(+) erythroid cells, which inhibits neonatal host defense against infection (3). In addition, the expression of arginase-2 in dendritic cells is repressed by microRNA-155 during maturation (4). This repression is essential for T-cell activation and response (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GPR37 is a G protein-coupled receptor (GPCR) that was originally identified as an orphan receptor highly expressed in the brain and testis (1). It shares significant homology with the receptors of endothelin and bombesin peptides (1). Neuropeptide head activator from the invertebrate Hydra was identified as a high-affinity ligand of GPR37 (2), however, to date, no mammalian ortholog of this peptide that could represent an endogenous GPR37 ligand has been identified. Recently, GPR37 was deorphanized as the receptor for the endogenous peptides prosaptide and prosaposin (3). GPR37 is a substrate of the E3 ubiquitin ligase parkin, and is often referred to as “parkin-associated endothelin-like receptor,” or “Pael-R” (4). GPR37 has been implicated in the pathogenesis of Parkinson’s Disease as it aggregates in the substantia nigra of some PD patients (4,5). Interestingly, prosaposin exerts neuroprotective, neurotrophic, and gliotrophic actions (6), and GPR37 was identified as a negative regulator of oligodendrocyte differentiation and myelination (7), suggesting that it could represent a potential target for demyelinating pathologies.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Parkinson’s disease (PD), the second most common neurodegenerative disease after Alzheimer’s, is a progressive movement disorder characterized by rigidity, tremors and postural instability. The pathological hallmark of PD is progressive loss of dopaminergic neurons in the substantia nigra of the ventral midbrain and the presence of intracellular Lewy bodies (protein aggregates of α-synuclein, ubiquitin and other components) in surviving neurons of the brain stem (1). Various genes and loci (α-synuclein/PARK1 and 4, parkin/PARK2, UCH-L1/PARK5, PINK1/PARK6, DJ-1/PARK7, LRRK2/PARK8, ATP13A2/PARK9) are genetically linked to PD (2).PARK9, also known as ATP13A2, is a member of the P-type ATPase superfamily and is involved in the lysosomal degradation pathway, clearing α-synuclein aggregates (3,4). The protein has 10 transmembrane domains and wild-type PARK9 localizes to the lysosomal membrane. In contrast, all three known mutations, which have premature stop codons resulting in a truncated protein, are retained in the endoplasmic reticulum and degraded by the proteasome. PARK9 is predominantly expressed in the brain and has been linked to Kufor-Rakeb Syndrome, a monogenic form of recessively inherited, atypical parkinsonism that is characterized by juvenile-onset, with pyramidal degeneration and cognitive dysfunction (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Seipin/BSCL2 is a homo-oligomeric membrane protein at the endoplasmic reticulum lipid droplet junction (1). Studies have demonstrated that Seipin/BSCL2 plays an important role in adipogenesis, lipid droplet homeostasis, liposis, brain development, and spermatogenesis. However, the exact function of BSCL2/Seipin is still not clear (2-5). BSCL2/Seipin is mutated in several human diseases, including Berardinelli-Seip congenital lipodystrophy, an autosomal recessive disorder characterized by a near absence of adipose tissues, severe insulin resistance, hypertriglyceridemia, hepatic steatosis, and early onset of diabetes (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Class 3 secreted semaphorin (Sema3A) is a chemorepellent that acts upon a wide variety of axons. As such, it induces a dramatic redistribution and depolymerization of actin filaments that results in growth cone collapse. Plexins are single membrane-spanning signaling proteins encompassing Plexin A1, A2, A3, and A4. Plexins form a complex with neuropilin-1 and -2 and the cell adhesion protein L1 to form a functional semaphorin receptor (1,2). The GTPase Rnd1 binds to the cytoplasmic domain of Plexin A1 to trigger cytoskeletal collapse. In contrast, the GTPase RhoD blocks Rnd1-mediated Plexin A1 activation and repulsion of sympathetic axons by Sema3A (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: A Disintegrin and Metalloprotease with Thrombospondin Motifs (ADAMTS) proteins comprise a large family of secreted zinc metalloproteases that play important roles in various processes, including organogenesis, hemostasis, and angiogenesis (1,2). ADAMTS proteases show structural similarity to ADAM proteases, but are further defined by the presence of repeated carboxy-terminal motifs homologous to the anti-angiogenic type 1 repeats of thrombospondin-1 (3). Functions ascribed to ADAMTS proteases include regulating the extracellular bioavailability of cytokines and growth factors (4, 5), regulating cell adhesion to the extracellular matrix (ECM), and remodeling of the ECM (6).

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

Application Methods: Western Blotting

Background: Coat Protein Complex II (COPII) is composed of five cytosolic proteins: Sec23/24 complex, Sec13/31 complex, and Sar1. COPII coat is located at the ER/Golgi interface and is involved in transport of newly synthesized proteins from the ER to the Golgi apparatus (1). COPII formation is initiated through the binding of the activated G protein, Sar1, to the Sec23/24 complex, thereby forming a prebudding complex that directly binds target molecules (1-3). The prebudding complex further recruits Sec13/31 to form mature COPII coat (4,5). The Sec24 subunit of COPII coat is thought to play a critical role in cargo selection (2,6). It binds directly to cargo proteins at the ER and brings them to COPII vesicles through interaction with Sec23. There are four Sec24 isoforms in human cells: Sec24A, Sec24B, Sec24C, and Sec24D (7). In mice, mutations in Sec24B have been linked to developmental defects (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Peptide ELISA (DELFIA), Western Blotting

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

$262
3 nmol
300 µl
SignalSilence® ATM siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit ATM 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: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Tudor domain-containing protein 3 (TDRD3) contains a tudor domain through which it binds to asymmetric di-methyl histone H3 (Arg17) and asymmetric di-methyl histone H4 (Arg3). Both of these histone marks are associated with transcription activation (1,2). TDRD3 is targeted to estrogen responsive genes where it performs as a coactivator (1). TDRD3 acts as a scaffolding protein to recruit Topoisomerase III B (TOP3B) to target genes to reduce transcription-generated R loops by relaxing negatively supercoiled DNA thereby reducing genomic instability (3). In addition to the nucleus, TDRD3 also resides in the cytoplasm where it associates with actively translating polyribosomes and accumulates into stress granules upon exposure to stress, implicating its role in post-transcriptional regulation of RNA (2,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The RecQ family is a group of DNA helicases that play an important role in global genomic stability (1). Mutations in three of the five known human RecQ proteins (BLM, WRN, and RECQL4) give rise to clinically distinct disorders that are characterized by features such as premature aging and predisposition to cancer (2,3). The clinical distinction of each disease associated with these mutations points to distinct roles that members of this helicase family play in DNA metabolism. The RecQL5 helicase has not yet been associated with any human disease, but RecQL5 -/- mice exhibit an increased incidence of cancer (4,5). It has recently been shown that RecQL5 protects genome stability through two parallel mechanims: helicase action and interaction with the initiation form of RNA Polymerase II (6). It has also been shown that RecQL5 -/- mouse embryonic stem cells display an elevated frequency of sister chromatic exchange (SCE), suggesting a role in suppression of homologous recombination and/or crossover events (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Salvador homolog (SAV1), originally named WW45, was first identified as a 45 kDa protein containing a pair of WW domains and a coiled-coil region (1). SAV1 was subsequently shown to function as a scaffold protein, in a protein complex that includes the kinases MST2 and LATS1, and the transcriptional co-activator YAP (2). This protein complex comprises the core components of the Hippo signaling pathway, which regulates important cellular functions, including contact inhibition and apoptosis, that function to regulate tissue growth and organ size (3,4). A genetic screen in Drosophila identified a role for SAV1 in cell cycle regulation and apoptosis (5), while embryonic mice lacking Sav1 displayed hyperplastic growth and epithelial differentiation effects (6). These findings, together with the observation that SAV1 is mutated a number of human cancer cell lines, suggest that SAV1 functions as a tumor suppressor in the Hippo signaling pathway (5, 7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Monocyte chemotactic protein-1 (MCP-1), also known as CCL2, monocyte chemotactic activating factor (MCAF) or glioma-derived chemotactic factor-2 (GDCF-2), is the product of the human JE gene and a member of the family of C-C (or β) chemokines (1-4). The predicted molecular weight of MCP-1 protein is 11-13 kDa, but it may migrate at 20-30 kDa due to glycosylation. MCP-1 is secreted by a variety of cell types in response to pro-inflammatory stimuli and was originally described for its chemotactic activity on monocytes. This activity has led to studies demonstrating its role in diseases characterized by monocyte infiltrates such as psoriasis (5), rheumatoid arthritis (6) and atherosclerosis (7). MCP-1 may also contribute to tumor progression and angiogenesis (8). Signaling by MCP-1 is mediated by the G-protein coupled receptor CCR2 (9).