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Product listing: LIN28A (D1A1A) XP® Rabbit mAb, UniProt ID Q9H9Z2 #8641 to Cleaved Caspase-8 (Asp387) (D5B2) XP® Rabbit mAb (Mouse Specific), UniProt ID O89110 #8592

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: LIN28A and LIN28B are conserved, developmentally regulated RNA binding proteins that inhibit the processing and maturation of the let-7 family of miRNAs (1,2). The let-7 miRNAs have been implicated in repression of oncogenes such as Ras, Myc, and HMGA2 (3). It has recently been shown that upregulation of LIN28A and LIN28B in primary human tumors and human cancer cell lines is correlated with downregulation of let-7 miRNAs (4). LIN28 genes are reported to be involved in primordial germ cell development and germ cell malignancy (5). In addition, allelic variation in LIN28B is associated with regulating the timing of puberty in humans (6). Overexpression of LIN28A, in conjunction with Oct-4, Sox2, and Nanog, can reprogram human fibroblasts to pluripotent, ES-like cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The methylation state of lysine residues in histone proteins is a major determinant of the 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 jumonji domain-containing protein 2 (JMJD2) family, also known as the JmjC domain-containing histone demethylation protein 3 (JHDM3) family, contains four members: JMJD2A/JHDM3A, JMJD2B/JHDM3B, JMJD2C/JHDM3C, and JMJD2D/JHDM3D. In addition to the JmjC domain, these proteins also contain JmjN, PHD, and tudor domains, the latter of which has been shown to bind to methylated histone H3 at Lys4 and Lys9, and methylated histone H4 at Lys20 (4,5). JMJD2 proteins have been shown to demethylate di- and tri-methyl histone H3 at Lys9 and Lys36 and function as both activators and repressors of transcription (6-11). JMJD2A, JMJD2C, and JMJD2D function as coactivators of the androgen receptor in prostate tumor cells (7). In contrast, JMJD2A also associates with Rb and NCoR corepressor complexes and is necessary for transcriptional repression of target genes (8,9). JMJD2B antagonizes histone H3 Lys9 tri-methylation at pericentric heterochromatin (10). JMJD2C, also known as GASC1, is amplified in squamous cell carcinomas and metastatic lung carcinoma and inhibition of JMJD2C expression decreases cell proliferation (11,12). JMJD2C has also been identified as a downstream target of Oct-4 and is critical for the regulation of self-renewal in embryonic stem cells (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Basic leucine zipper transcriptional factor ATF-like (BATF) is a basic leucine zipper (bZIP) transcription factor and is part of the AP-1/ATF family that forms inhibitory dimers with members of the Jun family (1-3). Expression of BATF is largely restricted with highest levels found in mature T cells, and it is induced in B cells following immune responses including viral infection (1,2). BATF expression is also induced by IL-6 via a Stat3-dependent mechanism (4). BATF plays an important role in the differentiation of immune cell lineages (5-7). Studies of BATF-deficient mice have demonstrated a critical role for BATF in the formation of IL-17-expressing Th17 cells, in part, by regulating the expression of IL-17 (5,6). BATF knockouts are resistant to experimental autoimmune encephalomyelitis (EEA), consistent with the role of Th17 cells in this model for autoimmunity (5). Additional studies have found that BATF is important in generating antibody class switching. BATF is required for the generation of follicular helper T cells (Tfh), by regulating BCL6 and c-Maf (6,7). In B cells, BATF controls the expression of activation-induced cytidine deaminase (AID) and regulates class-switched antibody responses (7). Taken together, these studies suggest that BATF is a key regulator of distinct populations of immune cells.

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Ribonucleotide reductase catalyzes the rate-limiting step in the synthesis of deoxynucleotide triphosphates (dNTPs). The regulatory M1 subunit (RRM1) is present throughout the cell division cycle, but downregulated in quiescent cells (1). Research studies have demonstrated that RRM1 is involved in carcinogenesis and tumor progression, and its expression is correlated with resistance to chemotherapy in non-small cell lung cancer (2-4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: LASP1 is a cytoskeletal scaffold protein belonging to the LIM protein subfamily (1,2). LASP1 consists of an N-terminal LIM domain, followed by two nebulin repeats, and a C-terminal SH3 domain (1,3). The nebulin repeats interact with actin, while the SH3 domain interacts with palladin (4,5), suggesting LASP1 functions as an actin-binding protein, possibly in cytoskeletal organization. LASP1 has been shown to localize to focal adhesions, lamellipodia, and membrane ruffles (6-8) and might be involved in membrane migration. Overexpression of LASP1 has been associated with metastatic cancers, such as breast and ovarian cancer (2). In these cases, membrane, cytoplasmic, and nuclear localization of LASP1 in the tumor cell has been reported, suggesting LASP1 involvement in membrane and nuclear signaling (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear Receptor Binding Factor-2 (NRBF-2), also referred to as Comodulator of PPAR and RXRα-2 (COPR-2), has been shown to interact with the AF-2 region of several nuclear hormone receptors with varying affinities such as PPARα, RARα, RARγ, and RXRα (1,2). NRBF-2 contains a LLYLL motif, which matches the LXXLL NR box consensus and is required for functional NRBF-2/nuclear receptor complex formation and repression of receptor function. NRBF-2 also contains a unique autonomous activation domain and, thus, does not completely abrogate nuclear receptor function, suggesting that NRBF-2 might serve as a molecular rheostat to fine-tune the transcriptional activity of liganded nuclear receptors (1,2).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-p38 MAPK (Thr180/Tyr182) (D3F9) XP® Rabbit mAb #4511.
APPLICATIONS
REACTIVITY
Human, Mink, Monkey, Mouse, Pig, Rat, S. cerevisiae

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: p38 MAP kinase (MAPK), also called RK (1) or CSBP (2), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (1-4). Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors (1-5). MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 (3) and to phosphorylate the transcription factors ATF-2 (5), Max (6), and MEF2 (5-8). SB203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-imidazole) is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27 (9). SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases (10).

$262
3 nmol
300 µl
SignalSilence® DDX5 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit DDX5 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: DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).

$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).

$262
3 nmol
300 µl
SignalSilence® FoxO3a siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit FoxO3a 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
Mouse

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors defined by the presence of a winged helix DNA binding domain called a Forkhead box (1). In humans, there are over 40 known Fox protein family members, divided into 19 subfamilies, which have evolved to regulate gene transcription in diverse and highly specialized biological contexts throughout development (2). Mutations that disrupt the expression of Fox gene family members have consequently been implicated in a broad array of human disorders, including immunological dysfunction, infertility, speech/language disorders, and cancer (3,4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin is a major hormone controlling critical energy functions, such as glucose and lipid metabolism. Insulin binds to and activates the insulin receptor (IR) tyrosine kinase, which phosphorylates and recruits adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of the Glut4 glucose transporter from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt Ser/Thr kinase (AS160, TBC1D4) is a Rab GTPase-activating protein that regulates insulin-stimulated Glut4 trafficking. AS160 is expressed in many tissues including brain, kidney, liver, and brown and white fat (2). Multiple Akt phosphorylation sites have been identified on AS160 in vivo, with five sites (Ser318, Ser570, Ser588, Thr642, and Thr751) showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrate that insulin-stimulated phosphorylation of AS160 is a crucial step in Glut4 translocation (3) and is reduced in some patients with type 2 diabetes (4). The interaction of 14-3-3 regulatory proteins with AS160 phosphorylated at Thr642 is a necessary step for Glut4 translocation (5). Phosphorylation of AS160 by AMPK is involved in the regulation of contraction-stimulated Glut4 translocation (6).

$262
3 nmol
300 µl
SignalSilence® CDK2 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit CDK2 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: Cyclin-dependent kinase 2 (p33CDK2) is an important component of the cell cycle machinery. Like p34cdc2, kinase activity is regulated by phosphorylation state as well as association with a cyclin subunit and a CDK inhibitor. Inhibitory phosphorylation occurs on Thr14 and Tyr15 (1). Inhibition of CDK2-cyclin complexes can also be attributed to association with p27 Kip1 and p21 Waf1/Cip1 (2). Activation of CDK2 complexes requires dephosphorylation of Thr14 and Tyr15 by cdc25 phosphatase and phosphorylation of Thr160 (3), which is mediated by CAK, a complex of CDK7 and cyclin H (4). CDK2/cyclin E kinase activity is important for the G1 to S transition and phosphorylation of the Rb protein. During S-phase, active CDK2/cyclin A complexes predominate and phosphorylate E2F and the active CDK2 complex persists in the nucleus throughout G2 (5).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Lamin A/C (4C11) Mouse mAb #4777.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication, and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear dysregulation and cell death (5,6).

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

Application Methods: Western Blotting

Background: Transketolase (TKT) is a homodimer in the pentose phosphate pathway (PPP) that catalyzes the interketol transfer between ketoses and aldoses (1,2). This enzyme, along with transaldolase, connects the nonoxidative branch of the PPP with glycolysis (1-3). Several regions of TKT are evolutionarily conserved from gram-negative bacteria to mammals (3). There is evidence that hypoxic (4) and non-hypoxic induction of HIF1-α (5) increases the expression of TKT. Because cancer cells rely on TKT in altered cell metabolism for nucleic acid synthesis, work has been done to develop inhibitors of TKT as novel cancer treatments (5-8).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PDI (C81H6) Rabbit mAb #3501.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

The Cytoskeletal Marker Antibody Sampler Kit provides an economical means to evaluate the presence and status of select cytoskeleton associated proteins. The kit provides enough primary antibodies to perform two western blots per primary antibody.
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Carbonic anhydrases (CA) are a family of ancient zinc metalloenzymes found in almost all living organisms. All CA can be divided into 3 distinct classes (α, β, and γ) that evolved independently and have no significant homology in sequence and overall folding. All functional CA catalyze the reversible hydration of CO2 into HCO3- and H+ and contain a zinc atom in the active sites essential for catalysis. There are many isoforms of CA in mammals and they all belong to the α class (1,2).

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

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

Background: TIAR is a member of the RNA-recognition motif (RRM) family of RNA-binding proteins (1,2). It functions as a translational repressor under conditions of cellular damage (3,4). In response to cellular stress, TIAR associates with eIF1, eIF3, and the 40S ribosomal subunit and forms noncanonical preinitiation complexes that are translationally inactive (3,4). TIAR then aggregates with its family member TIA1 and facilitates the accumulation of the translationally inactive preinitiation complexes into discrete cytoplasmic foci called stress granules. The two major isoforms of TIAR are the products of alternative mRNA splicing (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Malate dehydrogenase (MDH) is a key enzyme in the tricarboxylic acid cycle and malate/aspartate shuttle (1,2). MDH is widely expressed in organisms from most bacteria to all eukaryotes (2). The cytoplasmic MDH isoenzyme (cMDH or MDH1) primarily reduces oxaloacetate to malate in the malate/aspartate shuttle (1-3). The major function of the mitochondrial MDH isoenzyme (mMDH or MDH2) is to oxidize malate to oxaloacetate in the tricarboxylic acid cycle (1,2).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated HER2/ErbB2 (D8F12) XP® Rabbit mAb #4290.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The ErbB2 (HER2) proto-oncogene encodes a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity (1). While ErbB2 lacks an identified ligand, ErbB2 kinase activity can be activated in the absence of a ligand when overexpressed and through heteromeric associations with other ErbB family members (2). Amplification of the ErbB2 gene and overexpression of its product are detected in almost 40% of human breast cancers (3). Binding of the c-Cbl ubiquitin ligase to ErbB2 at Tyr1112 leads to ErbB2 poly-ubiquitination and enhances degradation of this kinase (4). ErbB2 is a key therapeutic target in the treatment of breast cancer and other carcinomas and targeting the regulation of ErbB2 degradation by the c-Cbl-regulated proteolytic pathway is one potential therapeutic strategy. Phosphorylation of the kinase domain residue Tyr877 of ErbB2 (homologous to Tyr416 of pp60c-Src) may be involved in regulating ErbB2 biological activity. The major autophosphorylation sites in ErbB2 are Tyr1248 and Tyr1221/1222; phosphorylation of these sites couples ErbB2 to the Ras-Raf-MAP kinase signal transduction pathway (1,5).

The Actin Nucleation and Polymerization Antibody Sampler Kit provides an economical means to evaluate the presence and status of actin nucleation and polymerization. The kit contains enough primary antibody to perform two western blots per primary.
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SINTBAD, identified based on homology to NAP1, is an adaptor protein for TBK1 and IKKε, two related kinases that play a pivotal role in innate immune response (1). These kinases trigger the phosphorylation and subsequent activation of the transcription factor IRF-3, resulting in gene regulation required for immune responses (2). The precise mechanism by which SINTBAD activates TBK1 and IKKε is still unclear. Expression of a central region of SINTBAD termed a TBD (TBK binding domain) can function as a dominant negative protein and interfere with IRF-3 activation. SINTBAD and NAP1 can also bind to NDP52, a protein that associates with poly-ubiquitinated proteins, such as those produced on the surfaces of bacteria, and can trigger autophagy (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Na+/H+ exchanger regulatory factor (NHERF1 or EBP-50) is one of several related PDZ domain-containing proteins (1). NHERF1 was first identified as a necessary cofactor for cyclic AMP-associated inhibition of Na+/ H+ exchanger isoform 3 (NHE3) (2). NHERF1 is a multifunctional adaptor protein that interacts with receptors and ion transporters via its PDZ domains, and with the ERM family of proteins, including merlin, via its carboxy-terminus (2,3). NHERF1 may play an important role in breast cancer. Estrogen has been found to induce NHERF1 in estrogen receptor-positive breast cancer cells (2,3). Furthermore, NHERF1 has been shown to bind to PDGFR, which is activated in breast carcinomas. NHERF1 has been found to promote the formation of a ternary complex containing PTEN, NHERF1, and PDGFR. Therefore, NHERF1 may function to recruit PTEN to PDGFR to inhibit the activation of PI3K/Akt signaling in normal cells; this mechanism may be disrupted in cancer (4). NHERF1 also binds to the cystic fibrosis transmembrane conductance regulator (CFTR), which functions as an ion channel and has disease-causing mutations in cystic fibrosis (5). Other proposed functions of NHERF1 include testicular differentiation, endosomal recycling, membrane targeting, protein sorting, and trafficking (6).

$307
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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Presenilin Enhancer 2 (PEN2) is a small integral membrane glycoprotein that contains two recognized transmembrane domains. Both the N- and C-terminal domains are oriented into the lumen of the endoplasmic reticulum (1). PEN2, along with Presenilin 1, Presenilin 2, Nicastrin, and APH-1 form the protein complex γ-secretase (2). The proteinase BACE catalyses the initial step in APP processing by cleaving and releasing soluble APPβ (3). The remaining membrane bound APP is then cleaved by the γ-secretase complex, causing the release of amyloid β-peptide, the main constituent of amyloid plaques. These plaques are a hallmark of Alzheimer’s disease pathology (2). In addition to APP, the γ-secretase complex cleaves several other proteins and necessary presenilin-dependent signaling cascades, including the Notch pathway (4). It was found that PEN2 is an important part of the γ-secretase complex, and knocking it down results in reduced amounts of the complex, resulting in a loss of γ-secretase activity (5).

$305
100 µl
This Cell Signaling Technology antibody is conjugated by the covalent reaction of hydrazinonicotinamide-modified antibody with formylbenzamide-modified horseradish peroxidase (HRP). The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Akt (pan) (C67E7) Rabbit mAb #4691.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: 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).

The Nuclear Receptor Antibody Sampler Kit provides an economical means to evaluate the presence and status of nuclear receptors. This kit contains enough primary antibody to perform two western blots per primary.
$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated 4E-BP1 (53H11) Rabbit mAb #9644.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Translation repressor protein 4E-BP1 (also known as PHAS-1) inhibits cap-dependent translation by binding to the translation initiation factor eIF4E. Hyperphosphorylation of 4E-BP1 disrupts this interaction and results in activation of cap-dependent translation (1). Both the PI3 kinase/Akt pathway and FRAP/mTOR kinase regulate 4E-BP1 activity (2,3). Multiple 4E-BP1 residues are phosphorylated in vivo (4). While phosphorylation by FRAP/mTOR at Thr37 and Thr46 does not prevent the binding of 4E-BP1 to eIF4E, it is thought to prime 4E-BP1 for subsequent phosphorylation at Ser65 and Thr70 (5).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Apoptosis induced through the CD95 receptor (Fas/APO-1) and tumor necrosis factor receptor 1 (TNFR1) activates caspase-8 and leads to the release of the caspase-8 active fragments, p18 and p10 (1-3). Activated caspase-8 cleaves and activates downstream effector caspases such as caspase-1, -3, -6, and -7. Caspase-3 ultimately elicits the morphological hallmarks of apoptosis, including DNA fragmentation and cell shrinkage.