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Product listing: LAT1 Antibody, UniProt ID Q01650 #5347 to GAP43 Antibody, UniProt ID P17677 #5307

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: L-type amino acid transporter 1 (LAT1), also known as Solute carrier family 7 member 5 (SLC7A5), is a high-affinity neutral transporter of larger amino acids. It facilitates the cellular amino acid uptake in a sodium independent manner (1-2) and selectively transports D-and L-isomers of small neutral amino acids (3). LAT1 also regulates amino acid exchange in conjunction with solute carrier family 1 member 5 (SLC1A5) (2,4-6). Transport of thyroid hormones across the placenta is established via LAT1 during normal fetal development (7). LAT1 promotes neuronal cell proliferation by regulating the transport of amino acids across the blood brain barrier (8). LAT1 is upregulated in various cancer types including breast cancer, lung cancer, prostate cancer, and gliomas (9,10). High expression of LAT1 is detected in non-small cell lung cancer with lymph node metastases(9,11,12). Increased LAT1 expression is a novel biomarker of high grade malignancy in prostate cancers (12). Inhibition of LAT1 suppresses tumor cell growth in several tumor types (10,13).

$305
100 µl
This Cell Signaling Technology (CST) antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody (β-Tubulin (9F3) Rabbit mAb #2128).
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Sodium-dependent neutral amino acid transporter type 2 (ASCT2 or SLC1A5) is a neutral amino acid transporter that regulates the uptake of essential amino acids in conjunction with the SLC7A5 bilateral transporter (1,2). ASCT2 appears to be the major glutamine transporter in hepatoma cells and is thought to provide essential amino acids needed for tumor growth (3). Additional evidence suggests that ASCT2 plays a role in activating mTORC1 signaling and is required to suppress autophagy (4,5). Cell surface ASCT2 serves as a receptor for several mammalian interference retroviruses associated with cases of infectious immunodeficiency; variation in a small region of an extracellular loop (ECL2) may be responsible for species-specific differences in receptor function (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Neural precursor expressed, developmentally down-regulated protein 4 (NEDD4) was originally identified as a gene that is highly expressed in the early mouse embryonic central nervous system (1). Subsequently, a family of NEDD4-like proteins have been defined that includes seven members in humans (2). NEDD4 and NEDD4-like (NEDD4L) proteins contain multiple functional domains including a calcium-dependent phospholipid and membrane binding domain (C2 domain), two to four protein binding domains (WW domains), and an E3 ubiquitin-protein ligase domain (HECT domain). NEDD4 and NEDD4L have been shown to downregulate both neuronal voltage-gated Na+ channels (NaVs) and epithelial Na+ channels (ENaCs) in response to increased intracellular Na+ concentrations (3,4). The WW domains of NEDD4 bind to PY motifs (amino acid sequence PPXY) found in multiple NaV and ENaC proteins; ubiquitination of these proteins is mediated by the HECT domain of NEDD4 and results in their internalization and removal from the plasma membrane. Research studies have shown that mutation of the PY motifs in ENaC proteins is associated with Liddle's syndrome, an autosomal dominant form of hypertension (5). In addition to targeting sodium channels, NEDD4L has also been shown to negatively regulate TGF-β signaling by targeting Smad2 for degradation (6). Mouse and human NEDD4 are rapidly cleaved by caspase proteins during apoptosis, although the significance of this cleavage is not clear (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Lysyl-tRNA synthetase (LysRS) is a multifunctional protein that has both regular and mitochondrial forms. The regular form of LysRS belongs to a family of aminoacyl-tRNA synthetases (aaRSs) that catalyze amino acid attachment to its cognate tRNA. In mammalian systems, LysRS forms a multisystem complex (MSC) with several other aaRSs (1-3). In addition to its conventional function, LysRS regulates diadenosine tetraphosphate (Ap4A) production (3). Cellular and metabolic stress increases the level of Ap4A, which functions as a cellular alarm system (3-5). Following FcεRI aggregation in mast cells, MAPK/Erk kinase (MEK) phosphorylates LysRS at Ser207 (5). Serine phosphorylation of LysRS leads to the release of LysRS from MSC and its translocation into the nucleus (5), as well as increased synthesis of Ap4A (5,6). LysRS binds to microphthalmia transcription factor (MITF) and MITF repressor Hint-1. Upon binding of Ap4A, Hint-1 is released from the complex that in turn allows the transcription of MITF-responsive genes (5-7). LysRS is also involved in HIV viral assembly through incorporation into HIV-1 virions via an interaction with HIV-1 Gag (8). Research studies have shown that in the presence of mutant Cu,Zn-superoxide dismutase (SOD1), mitochondrial LysRS tends to be misfolded and degraded by proteasomal degradation, contributing to mitochondrial dysfunction in Amyotrophic Lateral Sclerosis (ALS) (9). LysRS is also secreted and has cytokine-like functions (10). LysRS was also found to be an autoantigen in autoimmune responses (11).

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

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

Background: Members of the Smad family of signal transduction molecules are components of a critical intracellular pathway that transmit TGF-β signals from the cell surface into the nucleus. Three distinct classes of Smads have been defined: the receptor-regulated Smads (R-Smads), which include Smad1, 2, 3, 5, and 8; the common-mediator Smad (co-Smad), Smad4; and the antagonistic or inhibitory Smads (I-Smads), Smad6 and 7 (1-5). Activated type I receptors associate with specific R-Smads and phosphorylate them on a conserved carboxy terminal SSXS motif. The phosphorylated R-Smad dissociates from the receptor and forms a heteromeric complex with the co-Smad (Smad4), allowing translocation of the complex to the nucleus. Once in the nucleus, Smads can target a variety of DNA binding proteins to regulate transcriptional responses (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, Zebrafish

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microtubules, microfilaments (actin filaments), and intermediate filaments. Globular tubulin subunits comprise the microtubule building block, with α/β-tubulin heterodimers forming the tubulin subunit common to all eukaryotic cells. γ-tubulin is required to nucleate polymerization of tubulin subunits to form microtubule polymers. Many cell movements are mediated by microtubule action, including the beating of cilia and flagella, cytoplasmic transport of membrane vesicles, chromosome alignment during meiosis/mitosis, and nerve-cell axon migration. These movements result from competitive microtubule polymerization and depolymerization or through the actions of microtubule motor proteins (1).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments and microtubules. Major types of intermediate filaments are distinguished and expressed in particular cell types: cytokeratins (epithelial cells), glial fibrillary acidic protein or GFAP (glial cells), desmin (skeletal, visceral and certain vascular smooth muscle cells), vimentin (mesenchyme origin) and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Vimentin is present in sarcomas, but not carcinomas, and its expression is examined relative to other markers to distinguish between the two forms of neoplasm (3). Desmin is a myogenic marker expressed in early development that forms a network of filaments that extends across the myofibril and surrounds Z discs. The desmin cytoskeleton provides a connection among myofibrils, organelles and the cytoskeleton (4). Desmin knockout mice develop cardiomyopathy, skeletal and smooth muscle defects (5). In humans, desmin related myopathies might be caused by mutations in the corresponding desmin gene or in proteins with which desmin interacts, including αB-crystallin and synemin. Disorganized desmin filaments and the accumulation of protein aggregates comprised predominantly of desmin characterize desmin-related myopathies (reviewed in 6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Structural maintenance of chromosomes 2 (SMC2) and 4 (SMC4) proteins are subunits of the condensin complex, which enables chromosome condensation and maintains the compaction of chromosomes as they separate to opposite poles during anaphase (1-3). In addition to regulating chromosome condensation, condensin is a general regulator of chromosome architecture and may function to regulate gene expression and DNA repair. SMC proteins contain a hallmark bipartite ATPase domain of the ABC ATPase superfamily, which consists of an N-terminal Walker A motif nucleotide-binding domain and C-terminal Walker B motif catalytic domain that interact to form a functional ATPase (1-3). The two ATPase domains are connected by two coiled coil domains separated by a central hinge region that facilitates protein-protein interactions between partnering SMC proteins. In the case of the condensin complex, SMC2 and SMC4 interact to form a functional ATPase required for chromatin condensation; however, the mechanism by which this ATPase activity regulates chromsome architecture is still being determined. In addition to SMC proteins, condensin contains three auxiliary subunits, which function to regulate condensin ATPase activity. Higher eukaryotes contain two distinct condensin complexes (condensin I and II), both of which contain SMC2 and SMC4 (1-3). Condensin I also contains the auxiliary subunits CAP-D2, CAP-G and CAP-H, while condensin II contains the related auxiliary proteins CAP-D3, CAP-G2 and CAP-H2. The two condensin complexes show different localization patterns during the cell cycle and on chromosomes and both are required for successful mitosis, suggesting distinct functions for each complex (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dicer is a member of the RNase III family that specifically cleaves double-stranded RNAs to generate microRNAs (miRNAs) (1). After long primary transcript pri-miRNAs are processed to stem-looped pre-miRNAs by Drosha (2), pre-miRNAs are transported to the cytoplasm and further processed by Dicer to produce 22-nucleotide mature miRNAs (3). The mature miRNA then becomes a part of the RNA-Induced Silencing Complex (RISC) and can bind to the 3' UTR of the target mRNA (3).

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

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

Background: Phosphorylation of the eukaryotic initiation factor 2 (eIF2) α subunit is a well-documented mechanism to downregulate protein synthesis under a variety of stress conditions. eIF2 binds GTP and Met-tRNAi and transfers Met-tRNA to the 40S subunit to form the 43S preinitiation complex (1,2). eIF2 promotes a new round of translation initiation by exchanging GDP for GTP, a reaction catalyzed by eIF2B (1,2). Kinases that are activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2), or heme deficiency (HRI) can phosphorylate the α subunit of eIF2 (3,4). This phosphorylation stabilizes the eIF2-GDP-eIF2B complex and inhibits the turnover of eIF2B. Induction of PKR by IFN-γ and TNF-α induces potent phosphorylation of eIF2α at Ser51 (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GFAT1, glutamine:fructose-6-phosphate aminotransferase 1, is the rate-limiting enzyme of the hexosamine biosynthesis pathway (1). This enzyme catalyzes the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate and glutamate (2). The hexosamine biosynthesis pathway generates the building blocks for protein and lipid glycosylation (2). Furthermore, studies suggest that increased activity of this pathway is a contributing factor to hyperglycemia-induced insulin resistance (1,2). GFAT1 is more active in non-insulin-dependent diabetes mellitus (NIDDM) patients (3). Transgenice mice overexpressing this enzyme in skeletal muscle and adipose tissue show an insulin resistance phenotype (4,5). GFAT2, an isoenzyme of GFAT1, was later identified (6, 7). Studies show that the regulation of GFAT2 is different from that of GFAT1, suggesting differential regulation of the hexosamine pathway in different tissues (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Antiviral innate immunity depends on the combination of parallel pathways triggered by virus detecting proteins in the Toll-like receptor (TLR) family and RNA helicases, such as Rig-I (retinoic acid-inducible gene I) and MDA-5 (melanoma differentiation-associated antigen 5), which promote the transcription of type I interferons (IFN) and antiviral enzymes (1-3). TLRs and helicase proteins contain sites that recognize the molecular patterns of different virus types, including DNA, single-stranded RNA (ssRNA), double-stranded RNA (dsRNA), and glycoproteins. These antiviral proteins are found in different cell compartments; TLRs (i.e. TLR3, TLR7, TLR8, and TLR9) are expressed on endosomal membranes and helicases are localized to the cytoplasm. Rig-I expression is induced by retinoic acid, LPS, IFN, and viral infection (4,5). Both Rig-I and MDA-5 share a DExD/H-box helicase domain that detects viral dsRNA and two amino-terminal caspase recruitment domains (CARD) that are required for triggering downstream signaling (4-7). Rig-I binds both dsRNA and viral ssRNA that contains a 5'-triphosphate end not seen in host RNA (8,9). Though structurally related, Rig-I and MDA-5 detect a distinct set of viruses (10,11). The CARD domain of the helicases, which is sufficient to generate signaling and IFN production, is recruited to the CARD domain of the MAVS/VISA/Cardif/IPS-1 mitochondrial protein, which triggers activation of NF-κB, TBK1/IKKε, and IRF-3/IRF-7 (12-15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. These proteins are involved in the formation of cytoplasmic vacuoles called autophagosomes that are delivered to lysosomes for degradation.The class III type phosphoinositide 3-kinase (PI3KC3)/Vps34 regulates vacuolar trafficking as well as autophagy (4,5). Multiple proteins have been shown to be associated with Vsp34, including: p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, which can determine Vsp34 function (6-11). UVRAG (UV radiation resistance-associated gene) is associated with the Beclin-1/PI3KC3 complex and promotes PI3KC3 enzymatic activity and autophagy, while suppressing proliferation (11). Beclin-1 binding to UVRAG promotes both autophagosome maturation and endocytic trafficking (12). UVRAG is also a potential tumor suppressor protein with frameshift mutations observed in colon and gastric carcinomas (13,14).

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

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

Background: Apoptosis-inducing factor (AIF, PDCD8) is a ubiquitously expressed flavoprotein that plays a critical role in caspase-independent apoptosis (reviewed in 1,2). AIF is normally localized to the mitochondrial intermembrane space and released in response to apoptotic stimuli (3). Treatment of isolated nuclei with recombinant AIF leads to early apoptotic events, such as chromatin condensation and large-scale DNA fragmentation (3). Studies of AIF knockout mice have shown that the apoptotic activity of AIF is cell type and stimuli-dependent. Also noted was that AIF was required for embryoid body cavitation, representing the first wave of programmed cell death during embryonic morphogenesis (4). Structural analysis of AIF revealed two important regions, the first having oxidoreductase activity and the second being a potential DNA binding domain (3,5). While AIF is redox-active and can behave as an NADH oxidase, this activity is not required for inducing apoptosis (6). Instead, recent studies suggest that AIF has dual functions, a pro-apoptotic activity in the nucleus via its DNA binding and an anti-apoptotic activity via the scavenging of free radicals through its oxidoreductase activity (2,7).

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated S6 Ribosomal Protein (54D2) Mouse mAb #2317.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

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

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$364
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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-S6 Ribosomal Protein (Ser235/236) (D57.2.2E) XP® Rabbit mAb #4858.
APPLICATIONS
REACTIVITY
Human, Mink, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Flow Cytometry

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$364
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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb #4060.
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Hamster, Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Flow Cytometry

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).

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

Application Methods: Chromatin IP, Immunohistochemistry (Paraffin), Western Blotting

Background: RBPSUH (Recombining Binding Protein, SUppressor of Hairless), also termed RBP-J or CSL, is the DNA-binding component of the transcription complex regulated by canonical Notch signaling. In the absence of Notch activation, RBPSUH suppresses target gene expression through interactions with a co-repressor complex containing histone deacetylase. Upon activation of Notch receptors, the Notch intracellular domain (NICD) translocates to the nucleus and binds to RBPSUH. This displaces the co-repressor complex and replaces it with a transcription activation complex that includes Mastermind-like (MAML) proteins and histone acetylase p300, leading to transcriptional activation of Notch target genes (1-3). RBPSUH is also the DNA-binding partner for Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2), a protein critical for latent viral transcription and immortalization of EBV-infected B cells (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Protein-tyrosine phosphatase 1B (PTP1B) is the original member of the protein tyrosine phosphatase (PTP) family of proteins (1). PTP1B is highly expressed in insulin-responsive tissues and negatively regulates insulin, as well as integrin, through dephosphorylation of phosphotyrosine residues (2-4). PTP1B knockout mice show resistance to dietary weight gain and enhanced insulin sensitivity, suggesting a possible role in treatment of obesity as well as type 2 diabetes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The 25 kDa synaptosome-associated protein (SNAP25) is a target membrane soluble, N-ethylmaleimide-sensitive factor attachment protein receptor (t-SNARE) that is found on neuronal presynaptic membranes. SNAP25 forms a core complex with the SNARE proteins syntaxin and synaptobrevin to mediate synaptic vesicle fusion with the plasma membrane during Ca2+-dependent exocytosis (1). This complex is responsible for exocytosis of the neurotransmitter γ-aminobutyric acid (GABA). Neurotransmitter release is inhibited by proteolysis of SNAP25 by botulinum toxins A and E (2). SNAP25 plays a secondary role as a Q-SNARE involved in endosome fusion; the protein is associated with genetic susceptibility to attention-deficit hyperactivity disorder (ADHD) (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: GAP43 is a nervous system specific, growth-associated protein enriched in growth cones and areas of high plasticity (1). Phosphorylation of GAP43 at Ser41 by PKC is regulated by intracellular Ca2+ and affects the ability of GAP43 to bind calmodulin (2,3). GAP43 is integral to growth cone formation, neurite outgrowth, and the development of a functional cerebral cortex (4,5). Aberrant GAP43 expression can be seen in patients diagnosed with schizophrenia and Alzheimer's disease (6,7).