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Product listing: LIS1 Antibody, UniProt ID P43034 #12453 to SLK Antibody, UniProt ID Q9H2G2 #41255

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

Application Methods: Western Blotting

Background: LIS1 is a cytoskeleton-interacting protein that contains an N-terminal dimerization domain and a C-terminal β-propeller domain that interacts with the motor domain of dynein (1-3). Research studies have shown that mutations in the LIS1 gene are involved in lissencephaly, a disease characterized by severe defects in brain development (4). LIS1 also plays a critical role in cortical migration and development in the brain (5). LIS1 activity is required for retrograde translocation of excitatory synapses in developing interneuron dendrites in a microtubule-dependent fashion (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: RCC2/TD-60 is a member of the RCC1 (regulator of chromosome condensation 1) family of guanine nucleotide exchange factors. RCC2/TD-60 is associated with the chromosome passenger complex (CPC), which also consists of aurora B kinase, borealin, INCENP (inner centromere protein) and survivin. The CPC acts at various stages of mitosis, interacts with microtubules and is required for proper chromosome segregation and cytokinesis. Regulation of aurora B kinase is key in the regulation of the CPC (reviewed in 1,2). In late mitosis, RCC2/TD-60 is required for spindle assembly and recruitment of survivin and aurora B (3). RCC2/TD-60 is also required for aurora B activation in vitro and localization of the CPC to centromeres (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: Spi-B belongs to the ETS family of transcription factors and activates transcription through direct binding to the PU box (1). Spi-B was identified based on its homology with PU.1/Spi-I (1). The function of Spi-B is most well studied in B cells and plasmacytoid dendritic cells (pDCs). B cells from mice deficient in Spi-B proliferate poorly and die in response to signaling through the B cell receptor (2). In addition, Spi-B(-/-) mice have a defect in germinal center formation (2). Spi-B plays a role in both the development and function of pDCs. It is highly expressed by pDCs and not by monocyte-derived DCs, and overexpression of Spi-B in hematopoietic progenitor cells inhibits development of other lymphoid lineages (3). pDCs from Spi-B(-/-) mice produce less interferon in response to TLR7 and TLR9 stimulation and have lower expression of pDC-specific surface markers (4). Finally, Spi-B is required for differentiation of intestinal microfold cells (5,6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The flightless-I (fliI) gene was first identified in Drosophila mutant screens for genes involved in flight behavior. Homozygous mutant alleles at the fliI locus are embryonic lethal, whereas heterozygous mutations yield a "flightless" phenotype resulting from defects in flight muscle fiber development (1). The encoded protein (flightless-I, FLII) is a highly conserved member of the gelsolin superfamily, defined by the presence of C-terminal gelsolin motifs that function as actin-binding domains (2). Genetic knock-out studies in mice and worms confirmed that Flightless-I plays a critical and highly conserved role in embryonic development, likely through its effects on actin remodeling of the cytoskeleton (3,4). Postnatally, Flightless-I is recognized to play an important role in wound repair (5). Flightless-I protein levels are increased in many wound types, and depletion of Flightless-I protein levels has been shown to accelerate wound repair by promoting fibroblast proliferation and epithelial migration (6-8). Studies in animal models suggest that Flightless-I may inhibit the wound repair process by modulating TGF-β signaling dynamics in the wound environment (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Heterotrimeric guanine nucleotide-binding proteins, G proteins, transduce ligand binding to G protein-coupled receptors (GPCRs) into intracellular responses (1). G proteins are comprised of 3 subunits, alpha (Gα), beta (Gβ), and gamma (Gγ). Upon activation of GPCRs, the receptor promotes the exchange of GDP to GTP of Gα, changing the confirmation of the switch regions within Gα. The receptor bound heterotimeric G protein (inactive) is then released, and dissociates into the GTP-bound Gα (active) monomer and the Gβ/Gγ heterodimer (1,2). Gα activates adenylyl cyclase, which converts ATP to the second messenger cAMP. Gα also activates phosphoinositide-specific phospholipase C (PLC), which catalyzes hydrolysis of the phospholipid of phosphatidylinositol 4,5-biphosphate (PIP2), releasing the second messengers IP3 and 1,2-diacylglycerol (DAG). IP3 activates IP3 receptors to release Ca2+ from the ER. DAG is an activator of protein kinase C (PKC), which in turn activates the Erk1/2 pathway (1,3). The primary function of the Gβ/Gγ heterodimer is to inhibit Gα, although it may also activate second messengers (e.g. PLC pathway) or gate ion channels (e.g. GIRK) (1). Guanine nucleotide-binding protein b3 (GNB3) is an isoform of the b subunit. Research studies have shown that a polymorphism in the GNB3 gene, C825T, is associated with hypertension, obesity, and depression (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein Q and R belong to a family of hnRNP proteins that are involved in RNA binding, RNA biosynthesis, and mRNA transport from the nucleus to the cytoplasm (1-3). These two proteins are encoded by different genes but have 83% homology. hnRNP Q has three alternative splice variants (hnRNP Q1-3) (1-3). Methylation of carboxy-terminal arginine residues is required for nuclear localization (4). hnRNP Q binds to AU-rich mRNA in conjunction with AUF1 and regulates mRNA decay (5). hnRNP Q isoforms play a crucial role in mediating nuclear function of survival of motor neuron (SMN) complex (6,7) and modulating RNA biosynthesis and hepatitis C virus replication (8). hnRNP R was identified recently and its function is still under investigation (9), however hnRNP R does not duplicate the biological function of hnRNP Q. Both hnRNP Q and R are present in cytoplasmic mRNP granules containing untranslated mRNAs (10) and both interact with SMN (11).

$262
3 nmol
300 µl
SignalSilence® p70/85 S6 Kinase siRNA I allows the researcher to specifically inhibit p70/85 S6 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: p70 S6 kinase is a mitogen activated Ser/Thr protein kinase that is required for cell growth and G1 cell cycle progression (1,2). p70 S6 kinase phosphorylates the S6 protein of the 40S ribosomal subunit and is involved in translational control of 5' oligopyrimidine tract mRNAs (1). A second isoform, p85 S6 kinase, is derived from the same gene and is identical to p70 S6 kinase except for 23 extra residues at the amino terminus, which encode a nuclear localizing signal (1). Both isoforms lie on a mitogen activated signaling pathway downstream of phosphoinositide-3 kinase (PI-3K) and the target of rapamycin, FRAP/mTOR, a pathway distinct from the Ras/MAP kinase cascade (1). The activity of p70 S6 kinase is controlled by multiple phosphorylation events located within the catalytic, linker and pseudosubstrate domains (1). Phosphorylation of Thr229 in the catalytic domain and Thr389 in the linker domain are most critical for kinase function (1). Phosphorylation of Thr389, however, most closely correlates with p70 kinase activity in vivo (3). Prior phosphorylation of Thr389 is required for the action of phosphoinositide 3-dependent protein kinase 1 (PDK1) on Thr229 (4,5). Phosphorylation of this site is stimulated by growth factors such as insulin, EGF and FGF, as well as by serum and some G-protein-coupled receptor ligands, and is blocked by wortmannin, LY294002 (PI-3K inhibitor) and rapamycin (FRAP/mTOR inhibitor) (1,6,7). Ser411, Thr421 and Ser424 lie within a Ser-Pro-rich region located in the pseudosubstrate region (1). Phosphorylation at these sites is thought to activate p70 S6 kinase via relief of pseudosubstrate suppression (1,2). Another LY294002 and rapamycin sensitive phosphorylation site, Ser371, is an in vitro substrate for mTOR and correlates well with the activity of a partially rapamycin resistant mutant p70 S6 kinase (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Peroxiredoxin 6 (PRDX6) belongs to an antioxidant enzyme family of non-seleno peroxidases. PRDX6 is a unique member of the PRDX family, exhibiting both glutathione peroxidase and phospholipase A2 activities (1,2). PRDX6 regulates phospholipid turnover in addition to protecting cells against oxidative injury. PRDX6 is expressed in all major organs, with a particularly high level in lung, where it regulates lung surfactant phospholipid synthesis and turnover (3-5). Research studies have shown that PRDX6 is aberrantly expressed in various cancers, and can promote cancer cell metastasis and invasion (6,7). Elevated expression of PRDX6 and related PRDX family members has also been shown to contribute to drug resistance in cancer cells (8,9). PRDX6 is also expressed in neutrophils, where it has been shown to activate NADPH oxidase (NOX2) (10-12).

SignalSilence® Akt siRNA II from Cell Signaling Technology allows the researcher to specifically inhibit Akt 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 by western analysis.

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: Vasopressin is a neuroendocrine peptide that is released to the circulation by magnocellular neurons whose cell bodies are mainly found in the paraventricular and the supraoptic nuclei of the hypothalamus. It was first isolated from pituitary gland extracts and synthesized in 1951 (1). Vasopressin acts by activating G protein-coupled, V1a, V1b (also known as V3) and V2 receptors and plays a fundamental role in the maintenance of water homeostasis. One of its main functions is body water retention (2), hence its alternative name antidiuretic hormone or ADH. Vasopressin also leads to increased arterial blood pressure by raising peripheral vascular resistance (3). Vasopressin is also involved in other physiological processes such as acute heart failure (4), pain (5), and metabolic syndrome (6).

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

Application Methods: Western Blotting

Background: Initiation of eukaryotic DNA replication is a stringently regulated process that requires the cooperation of many proteins and protein complexes to occur efficiently, at the origins of replication, and once per cell cycle. The initiation of DNA replication requires a protein complex composed of two DNA polymerase α subunits and a pair of primase subunits. Primase activity catalyzes de novo synthesis of an RNA/DNA primer (initiator DNA) on the leading and lagging strands, while polymerase activity extends the initiator DNA (1). The 48 and 58 kDa primase subunits cooperate in the synthesis of small RNA primers. p48 is the catalytically active subunit (2), while p58 couples p48 to the polymerase to allow the transfer of primers to the active site. The p58 subunit may also play a role in regulation of primer length (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway (1-3). The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are condensin complex subunits that enable chromosome condensation and compaction during migration to opposite poles during anaphase (1,2). Condensin is a general regulator of chromosome architecture that may also regulate gene expression and DNA repair. Condensin complex subunits SMC2 and SMC4 form a functional ATPase essential for chromatin condensation, while three auxiliary subunits regulate ATPase activity. Both SMC2 and SMC4 are found within two distinct condensin complexes (condensin I and II) in higher eukaryotes. Condensin I contains auxiliary subunits NCAPD2, NCAPG, and NCAPH, while condensin II contains related auxiliary proteins NCAPD3, NCAPG2, and NCAPH2 (1,2).Each condensin complex exhibits different localization patterns during the cell cycle and provides for distinct functions during mitosis (3-5). Condensin I is cytoplasmic during interphase and binds chromatin following the breakdown of the nuclear envelope at the end of prophase. Condensin I is required for complete dissociation of cohesin from chromosome arms, for chromosome shortening, and for normal timing of progression through pro-metaphase and metaphase. Mutations in corresponding condensin I genes result in cytokinesis defects due to the persistence of anaphase fibers. Condensin II is nuclear during interphase, but does not bind to chromatin until early prophase where it remains bound until the end of telophase. Condensin II is required for initial chromatin condensation during early prophase. Mutations in corresponding condensin II genes produce high numbers of anaphase bridges resulting from incomplete chromosome segregation. Condensin II complex subunit D3 (NCAPD3) plays a pivotal role in the loading of condensin II onto chromatin and the regulation of chromatin condensation (6,7). NCAPD3 protein contains HEAT repeat clusters that bind to mono-methyl histone H4 Lys20, a histone mark prevalent during mitosis and important for DNA repair and chromatin condensation (6). Increased mono-methyl histone H4 Lys20 levels caused by dissociation of the histone demethylase PHF8 from chromatin and increased expression of the methyltransferase SET8, leads to increased binding of NCAPD3 and condensin II to chromosomes early in mitosis (6). Phosphorylation of NCAPD3 at Thr1415 by CDK1 kinase (cdc2) leads to the recruitment of PLK1 kinase, which hyperphosphorylates condensin II and facilitates mitotic chromosome assembly (7).

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

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The E2F family consists of 8 transcription factors that regulate genes that control cell cycle progression by complexing with DP and Rb proteins (1-4). E2F transcriptional activation is generally opposed by associating with RB proteins, pRB, p107, and p130 (5-7). E2F-1, -2, and -3a function as activators that can help quiescent cells enter S phase, while E2F-3b, -4, and -5 repress cell growth through the recruitment of HDAC’s and other corepressors to target genes (8-10). E2F-6 diverges considerably from other family members, and has repressive properties governed not through interaction with Rb proteins, but by recruiting the polycomb repressive complex (11,12). E2F-7, and -8 are unique in that they have two DNA-binding domains and do not heterodimerize with DP proteins. These E2F family members repress transcription and delay progression of the cell cycle through the regulation of E2F-1 (13-15)

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

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: In mammalian cells, the significance of histone H2B ubiquitination in chromatin epigenetics came from the identification of the budding yeast protein Bre1 (1,2). Together with the ubiquitin-conjugating enzyme Rad6, Bre1 serves as the E3 ligase in the monoubiquitination of the yeast histone H2B within transcribed regions of chromatin (1-3). Subsequently, the mammalian orthologs of yeast Bre1, RNF20 and RNF40, were identified (4,5). These two proteins form a tight heterodimer that acts as the major E3 ligase responsible for histone H2B monoubiquitination at Lys120 in mammalian cells, a modification linked to RNA Pol II-dependent transcription elongation in undamaged cells. Researchers have shown that DNA double-strand breaks (DSBs) are also capable of inducing monoubiquitination of H2B. This process depends upon the recruitment to DSB sites, as well as ATM-dependent phosphorylation of the RNF20-RNF40 heterodimer, thus highlighting a role for this E3 ligase in DSB repair pathways (6). Indeed, investigators have shown that loss of RNF20-RNF40 function promotes replication stress and chromosomal instability, which may constitute an early step in malignant transformation that precedes cell invasion (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), 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. RecQL1 is the most abundant protein of the RecQ family and was the first family member to be discovered. No disease associations have been reported with RecQL1 and its biological activities are not well understood (4). It has recently been shown that depletion of RecQL1 negatively affects genomic maintenance and cellular proliferation – which may point to a role in DNA damage repair and cell cycle progression (5,6). Upregulation of RecQL1 along with other RecQ family members has been reported in cells in response to oncogenic viral infection (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The solute carrier family 39 (zinc transporter) member 7 (SLC39A7, ZIP7) is an ER and Golgi membrane protein that regulates cellular zinc homeostasis by controlling release of zinc from these organelles to the cytoplasm (1,2). Zinc release mediated by ZIP7 results in activation of protein kinases that are involved in cell proliferation and migration (3,4). The protein kinase CK2 phosphorylates and activates ZIP7 in response to extracellular signals, such as growth factor stimulation (4,5). Increased expression of ZIP7 is observed in breast cancer tissues (6). Research studies indicate that ZIP7 is responsible for activation of multiple tyrosine kinases in aggressive, tamoxifen-resistant breast cancer (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) were first identified as molecules that can induce ectopic bone and cartilage formation (1,2). BMPs belong to the TGF-β superfamily, playing many diverse functions during development (3). BMPs are synthesized as precursor proteins and then processed by cleavage to release the C-terminal mature BMP. BMPs initiate signaling by binding to a receptor complex containing type I and type II serine/threonine receptor kinases that then phosphorylate Smad (mainly Smad1, 5, and 8), resulting in the translocation of Smad into the nucleus. BMP was also reported to activate MAPK pathways in some systems (3,4).

$262
3 nmol
300 µl
SignalSilence® Rictor siRNA II 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, Mouse, Rat

Application Methods: Western Blotting

Background: F3/contactin (CNTN, contactin 1) is a glycosylphosphatidylinositol (GPI)-anchored neural cell adhesion protein belonging to the immunglobulin protein superfamily (1). During early mammalian development, F3/contactin is expressed in granule neuronal progenitor (GNP) cells, where it was shown to promote GNP differentiation, in part by antagonizing sonic hedgehog (SHH)-mediated proliferation (2). Biochemical studies have shown that F3/contactin interacts with the phosphatase PTPRZ on the surface of oligodendrocyte precursor cells, an association that was shown to be essential for oligodendrocyte maturation (3). F3/contactin expression is also abundant in post-mitotic neurons, where its functions as a neural cell adhesion protein have been suggested to play an important role in synaptic plasticity and memory (4). Although primarily associated with neuronal development and function, F3/contactin expression has also been implicated in extra-neuronal tumorigenesis. For example, expression of F3/contactin was detected in both primary prostate tumors, and lymph node and bone metastases, while patient tumor samples with detectable F3/contactin expression were associated with tumor progression and reduced recurrance-free survival (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: C-reactive protein (CRP) is a pentraxin family protein involved in several host defense-related functions as a result of its ability to bind to foreign pathogens and damaged host cells (1). CRP is a cyclic, non-covalent pentameric protein and normal constituent of human sera that is produced primarily by hepatocytes (2). Secretion of CRP is induced by proinflammatory cytokines, including IL-6 and IL-1β, and significantly increases during acute phase responses to tissue injury, infection, or other inflammatory stimuli (3,4). The presence of CRP is often utilized as an inflammation marker, and monitoring CRP levels in plasma is a useful tool in assessing disease progression or treatment effectiveness. CRP is also regarded as a risk assessment factor for the development and progression of cardiovascular disease (5).CRP binds to phosphorylcholine that is present on the surface of damaged tissues and in the bacterial cell wall of certain pathogens (6). Through this calcium-dependent interaction, CRP promotes agglutination and initiates the activation of the complement cascade. This results in enhanced opsonization through CRP interaction with FcγRI and FcγRIIA, which facilitates phagocytosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of nine proteins is divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All CHD proteins contain two tandem amino-terminal chromodomains, a SWI/SNF-related ATPase domain, and a carboxy-terminal DNA-binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes energy from ATP hydrolysis to modify chromatin structure. CHD proteins are often found in large, multiprotein complexes with their transcriptional activation or repression activity governed by other proteins within the complex. CHD3 (also known as Mi2-α) and CHD4 (also known as Mi2-β) are central components of the nucleosome remodeling and histone deacetylase (NuRD) transcriptional repressor complex, which also contains HDAC1, HDAC2, RBAP48, RBAP46, MTA1, MTA2, MTA3, and MBD3 (3-8). Both CHD3 and CHD4 contain two plant homeodomain (PHD) zinc finger domains that bind directly to HDAC1 and HDAC2.

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: SLIT2 is an extracellular matrix-associated SLIT family member that functions as a ligand for roundabout (ROBO) family receptors (1). Activation of ROBO receptors by SLIT2 regulates various biological processes, including promoting cellular senescence via WNT inhibition (2), suppressing migration by enhanced β-catenin/E-cadherin association, regulating actin polymerization (4, 5), and suppressing cell proliferation induced by SDF1 and MCP1 (6, 7). In development, the SLIT-ROBO pathways play important roles in neuronal axon guidance, angiogenesis, and both kidney and mammary gland organogenesis. SLIT2 expression has been reported to suppress cancer cell growth, invasion, and metastasis, suggesting that modulation of SLIT2-ROBO signaling may have therapeutic potential in cancer biology (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: DRAK2 (DAP kinase related apoptosis inducing protein kinase 2) is a member of the novel DAP (death associated protein) pro-apoptotic kinase family (1). Overexpression of DRAK2 in NIH/3T3 cells induces morphological changes associated with apoptosis, which are likely to occur in a p53-dependent manner (1,2). DRAK2 is preferentially expressed in lymphoid tissues and regulates the TCR activation threshold during thymocyte selection (3). Indeed, T cells from DRAK2(-/-) mice exhibit enhanced sensitivity to T cell receptor-mediated stimulation and have a reduced requirement for co-stimulation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: SLK (Ste20-like Kinase) is a member of the germinal center kinase (GCK) family of proteins. SLK has a kinase domain located at the N terminus (1). The autophosphorylation of SLK at Thr183 and Ser189 is required for the upregulation of SLK kinase activity (1, 2). The protein also has a caspase cleavage site DXXD and a SH3 binding site PXXP located in the middle part of its sequence, and a regulatory C terminal coiled-coil domain for homodimerization and adaptor binding (1-4). SLK plays important roles in development, tissue regeneration and cancer cell migration by regulating several signaling pathways (5-7). SLK phosphorylates and activates ASK1 to induce downstream p38 phosphorylation and apoptosis (8,9). During cell cycle, SLK phosphorylates Polo-like kinase (PLK) at Thr210 to promote G2/M transition (10,11). SLK also promotes cell division by direct phosphorylation of ERMs and dynactin to activate microtubule reorganization and spindle orientation (12, 13). During focal adhesion and cell migration process, SLK is activated and colocalized to the focal adhesion complex where it promotes complex turnover by phosphorylating paxillin at Ser250 (14, 15).