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Product listing: OGDH (E1W8H) Rabbit mAb, UniProt ID Q60597 #26865 to AID (L7E7) Mouse mAb, UniProt ID Q9GZX7 #4975

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

Application Methods: Immunoprecipitation, Western Blotting

Background: 2-oxoglutarate dehydrogenase (OGDH) is one of three enzymes in the α ketoglutarate dehydrogenase complex (OGDC) that is responsible for catalyzing a rate-regulating step of the tricarboxylic acid (Krebs) cycle. Together with dihydrolipoamide S-succinyltransferase (DLST) and dihydrolipoamide dehydrogenase (DLD), OGDH helps to convert 2-oxoglutarate to succinyl-CoA and CO2 within eukaryotic mitochondria (1). Regulation of this enzyme complex is important for mitochondrial energy metabolism within cells (2). Research studies indicate that OGDH activity within the mitochondrial matrix is regulated by multiple factors, including calcium, the adenine nucleotides ATP and ADP, and NADH (2).

$348
400 µl
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. PTEN (D4.3) XP® Rabbit mAb (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of PTEN protein.
APPLICATIONS
REACTIVITY
Dog, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

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

Application Methods: Western Blotting

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as Class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT2, a mammalian homolog of Sir2, deacetylates α-tubulin at Lys40 and histone H4 at Lys16 and has been implicated in cytoskeletal regulation and progression through mitosis (2,3). SirT2 protein is mainly cytoplasmic and is associated with microtubules and HDAC6, another tubulin deacetylase (2). Deacetylation of α-tubulin decreases its stability and may be required for proper regulation of cell shape, intracellular transport, cell motility, and cell division (2,4). The abundance and phosphorylation state of SirT2 increase at the G2/M transition of the cell cycle, and SirT2 relocalizes to chromatin during mitosis when histone H4 Lys16 acetylation levels decrease (3,5). Overexpression of SirT2 prolongs mitosis, while overexpression of the CDC14B phosphatase results in both decreased phosphorylation and abundance of SirT2, allowing for proper mitotic exit (5). Thus, the deacetylation of both histone H4 and α-tubulin by SirT2 may be critical for proper chromatin and cytoskeletal dynamics required for completion of mitosis.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Rat

Application Methods: Western Blotting

Background: CrkL, a 39 kDa adaptor protein, has a key regulatory role in hematopoietic cells. CrkL has one SH2 and two SH3 domains, with 60% homology to CrkII (1). The amino-terminal SH3 domain of CrkL binds proteins such as C3G, SOS, PI3K, c-Abl and BCR/Abl. The SH2 domain of CrkL can bind to tyrosine-phosphorylated proteins such as Cbl, HEF1, CAS and paxillin (2,3). CrkL is involved in various signaling cascades initiated by different cytokines and growth factors. The biological outcomes of the Crk-activated signal transduction include the modulation of cell adhesion, cell migration and immune cell responses (4). CrkL is a prominent substrate of the BCR/Abl oncoprotein in chronic myelogenous leukemia and binds to both BCR/Abl and c-Abl (5). CrkL is prominently and constitutively tyrosine phosphorylated in CML neutrophils and is not phosphorylated in normal neutrophils. Moreover, stimulation of normal neutrophils with cytokines and agonists does not induce tyrosine phosphorylation of this protein (6), indicating that it may be a useful target for therapeutic intervention or as a disease marker. Tyr207 in CrkL is the BCR/Abl phosphorylation site (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Tight junctions, or zonula occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces. Tight junctions are composed of claudin and occludin proteins, which join the junctions to the cytoskeleton (1,2). The claudin family is composed of 23 integral membrane proteins, and their expression, which varies among tissue types, may determine both the strength and properties of the epithelial barrier. Alteration in claudin protein expression pattern is associated with several types of cancer (2,3). Claudin-1 is expressed primarily in keratinocytes (4) and normal mammary epithelial cells, but is absent or reduced in breast carcinomas and breast cancer cell lines (5,6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Diffuse intrinsic pontine glioma (DIPG) is an aggressive brainstem astrocyte tumor arising mostly in children, leading to a long-term survival rate of less than 10%. Multiple whole-genome sequencing studies of DIPG patients identified commonly occurring mutations in the H3F3A gene encoding histone H3.3. One of these mutations, a lysine to methionine amino acid substitution (K27M), is found in up to 78% of DIPGs and 22% of non-brainstem pediatric gliomas (1-3). This mutation is associated with poor prognosis, with a mean survival time of 0.73 years for patients with the K27M mutation versus 4.6 years for patients without the mutation (1-3). Expression of the K27M mutant histone H3 is accompanied by a dramatic reduction in the levels of polycomb repressive complex 2 (PRC2)-mediated trimethylation of histone H3, changes in the distribution of PRC2 on the genome, and altered expression of genes associated with various cancer pathways (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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: Immunoprecipitation, Western Blotting

Background: Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate (1).Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells (2-4), which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers (5,6). Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo (5). Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells (7).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluroescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Stat1 (Tyr701) (58D6) Rabbit mAb #9167.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry)

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

$65
1 ml
$296
5 x 1ml
5 ml
The SimpleChIP® Universal qPCR Master Mix is an optimized 2X reaction mix for real-time qPCR detection and quantitation of target DNA sequences using the SYBR/FAM channel of most real-time qPCR instruments. It contains Hot Start Taq DNA Polymerase and has been formulated with a unique passive reference dye that is compatible across a variety of instrument platforms (including those that require a high or low ROX reference signal). It also features dUTP for carryover prevention and a non-fluorescent, visible dye to monitor reaction setup. This dye does not spectrally overlap with fluorescent dyes used for qPCR and will not interfere with real-time detection.This product is provided in 1 ml volumes sufficient for preparation of 100 qPCR reactions, and is compatible with both enzymatic and sonication-fragmented DNA samples from SimpleChIP® enzymatic and sonication ChIP kits. This master mix formulation is supplied at 2X concentration and contains all PCR components required for amplification and quantitation of DNA, except primers and a DNA template.
REACTIVITY
All Species Expected

Background: Dye-based quantitative PCR (qPCR) uses real-time fluorescence of a double-stranded DNA (dsDNA) binding dye, most commonly SYBR® Green I, to measure DNA amplification as it occurs during each cycle of PCR. At a point where the fluorescence signal is confidently detected over the background fluorescence, a quantification cycle, or CT value, can be determined. CT values can be used to evaluate relative target abundance between two or more samples, or to calculate absolute target quantities in reference to an appropriate standard curve, derived from a series of known dilutions. qPCR is commonly used to detect and quantify target genes in genomic DNA that is enriched by chromatin immunoprecipitation (ChIP).

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

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr kinases characterized by two nonidentical, functional kinase domains (1) and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs) (2). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation (3). RSK1-3 are activated via coordinated phosphorylation by MAPKs, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters (3).

$305
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 c-Jun (60A8) Rabbit mAb #9165.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: c-Jun is a member of the Jun family containing c-Jun, JunB, and JunD, and is a component of the transcription factor activator protein-1 (AP-1). AP-1 is composed of dimers of Fos, Jun, and ATF family members and binds to and activates transcription at TRE/AP-1 elements (reviewed in 1). Extracellular signals including growth factors, chemokines, and stress activate AP-1-dependent transcription. The transcriptional activity of c-Jun is regulated by phosphorylation at Ser63 and Ser73 through SAPK/JNK (reviewed in 2). Knock-out studies in mice have shown that c-Jun is essential for embryogenesis (3), and subsequent studies have demonstrated roles for c-Jun in various tissues and developmental processes including axon regeneration (4), liver regeneration (5), and T cell development (6). AP-1 regulated genes exert diverse biological functions including cell proliferation, differentiation, and apoptosis, as well as transformation, invasion and metastasis, depending on cell type and context (7-9). Other target genes regulate survival, as well as hypoxia and angiogenesis (8,10). Research studies have implicated c-Jun as a promising therapeutic target for cancer, vascular remodeling, acute inflammation, and rheumatoid arthritis (11,12).

Akt Isoform Specific Antibody Sampler Kit provides an economical means of distinguishing between the three Akt isoforms, Akt1, Akt2 and Akt3, as well as a pan-Akt antibody. The kit provides enough primary and secondary antibodies to perform two Western blot experiments.

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
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MTHFD2 is a bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase involved in mitochondrial folate metabolism (1). MTHFD2 expression is developmentally regulated, as it is expressed in embryos but not in most adult tissues. Recent research studies have shown that MTHFD2 is consistently overexpressed in many cancer types and correlated with poor survival in breast cancer (2-5). Overexpression of MTHFD2 promotes cell proliferation while its depletion induces cell death in human cancer cells (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: Striatal enriched phosphatase (STEP, also known as PTPN5), is a protein tyrosine phosphatase expressed in dopaminoceptive neurons of the central nervous system (1). Alternative splicing produces the cytosolic STEP46 and the membrane-associated STEP61 isoforms of STEP. Dopamine activates D1 receptors and PKA, which in turn phosphorylate both isoforms of STEP. Phosphorylation of STEP61 occurs at Ser160 and Ser221, while STEP46 is phosphorylated at Ser49 (equivalent to Ser221 of STEP61) (2). NMDA-mediated activation of STEP is an important mechanism for regulation of Erk activity in neurons (3). Furthermore, STEP is involved in the regulation of both NMDAR and AMPAR trafficking (4,5). Due to its importance in cognitive function, STEP may play a role in Alzheimer's disease (1).

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

Application Methods: Western Blotting

Background: HSPB8 (HSP22) is a member of the small heat shock protein superfamily and the human protein is most closely related to HSP27. Similar to most other small HSPs (sHSPs), HSPB8 is predominantly transcribed in skeletal muscle and heart (1). In a two hybrid screen, HSPB8 interacted preferentially with a triple aspartate form of HSP27 which mimics HSP27 phosphorylated at Ser15, Ser78, and Ser82, as compared to wild-type HSP27 (2). HSPB8 has two binding domains (N- and C-terminal) that are specific for different binding partners, and has the ability to bind to itself and other sHSPs such as HSPB7 and HSPB2 (3). The chaperone-like activity is of great importance to the function of HSP22 in various processes including proliferation, apoptosis and macroautophagy (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated EGR1 (44D5) Rabbit mAb #4154.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: EGR family members are transcriptional factors that contain three repetitive zinc finger DNA binding domains which bind to EGR response elements (ER) to regulate target gene expression (1). The expression of EGR family members is induced by growth factors, with EGR1 expression being induced by NGF (1,2). Increased EGR1 expression activates transcription of other signaling molecules, including CDK5 and tyrosine hydroxylase, and exerts long term effects on neural cell growth and differentiation (2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: FMS-related tyrosine kinase 3 (FLT3, also called Flk2), is a member of the type III receptor tyrosine kinase family, which includes c-Kit, PDGFR and M-CSF receptors. FLT3 is expressed on early hematopoietic progenitor cells and supports growth and differentiation within the hematopoietic system (1,2). FLT3 is activated after binding with its ligand FL, which results in a cascade of tyrosine autophosphorylation and tyrosine phosphorylation of downstream targets (3). The p85 subunit of PI3 kinase, SHP2, GRB2 and Shc are associated with FLT3 after FL stimulation (4-6). Tyr589/591 is located in the juxtamembrane region of FLT3 and may play an important role in regulation of FLT3 tyrosine kinase activity. Somatic mutations of FLT3 consisting of internal tandem duplications (ITDs) occur in 20% of patients with acute myeloid leukemia (7).

The Parkinson's Research Antibody Sampler Kit provides an economical means of detecting target proteins related to Parkinson's disease. The kit contains enough primary and secondary antibody to perform two western blots per primary.
The ER Protein Folding Antibody Sampler Kit contains reagents to investigate the initiation of translation within the cell. The kit contains enough primary and secondary antibodies to perform two Western blot experiments per primary antibody.
$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

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

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

Background: Lipin 1 was identified as a nuclear protein required for adipose tissue development (1). The expression of Lipin 1 is induced during adipocyte differentiation (1). The abnormal development of adipose tissues caused by mutations in the lipin 1 gene results in lipodystrophy, a condition associated with low body fat, fatty liver, hypertriglyceridemia, and insulin resistance (1). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (2-4). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in liver, and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (5). Lipin 1 is regulated by mTOR, illustrating a connection between adipocyte development and nutrient-sensing pathways (6). It also mediates hepatic insulin signaling by TORC2/CRTC2 (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Actin proteins are major components of the eukaryotic cytoskeleton. At least six vertebrate actin isoforms have been identified. The cytoplasmic β- and γ-actin proteins are referred to as “non-muscle” actin proteins as they are predominantly expressed in non-muscle cells where they control cell structure and motility (1). The α-cardiac and α-skeletal actin proteins are expressed in striated cardiac and skeletal muscles, respectively. The smooth muscle α-actin and γ-actin proteins are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. The α-smooth muscle actin (ACTA2) is also known as aortic smooth muscle actin. These actin isoforms regulate the contractile potential of muscle cells (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Activation-induced cytidine deaminase (AID) is thought to modify RNA due to its high homology to the RNA editing enzyme APOBEC-1. This function, however, has not been confirmed in in vitro studies, which show that AID has significant cytidine deaminase activity, and that this activity is blocked by zinc chelation (1).The B cell immune system must specifically recognize several infectious agents, which vastly outnumber immunoglobulin gene segments present in a given organism. Mechanisms such as somatic hypermutation, isotype switch recombination and gene conversion introduce diversity and specificity to the immune system. Analysis of mouse models and patients with AID deficiency has established a link between all three of these mechanisms and AID function (2). AID protein is detected in germinal center centroblast and germinal center derived lymphomas (Burkitt lymphoma), but not in pre-germinal center B cells or post-germinal center neoplasms (B cell chronic lymphocytic leukemia and multiple myeloma) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Activation-induced cytidine deaminase (AID) is thought to modify RNA due to its high homology to the RNA editing enzyme APOBEC-1. This function, however, has not been confirmed in in vitro studies, which show that AID has significant cytidine deaminase activity, and that this activity is blocked by zinc chelation (1).The B cell immune system must specifically recognize several infectious agents, which vastly outnumber immunoglobulin gene segments present in a given organism. Mechanisms such as somatic hypermutation, isotype switch recombination and gene conversion introduce diversity and specificity to the immune system. Analysis of mouse models and patients with AID deficiency has established a link between all three of these mechanisms and AID function (2). AID protein is detected in germinal center centroblast and germinal center derived lymphomas (Burkitt lymphoma), but not in pre-germinal center B cells or post-germinal center neoplasms (B cell chronic lymphocytic leukemia and multiple myeloma) (3).