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Product listing: Cleaved Caspase-8 (Asp384) (11G10) Mouse mAb, UniProt ID Q14790 #9748 to Mitochondrial Membrane Potential Assay Kit (II) #13296

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: 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.

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Rab5 is a member of the Ras superfamily of small Rab GTPases. Rab5 is localized at the plasma membrane and early endosomes and functions as a key regulator of vesicular trafficking during early endocytosis (1). The conformational change between Rab5 GTP/GDP states is essential for its biological function as a rate limiting regulator at multiple steps during endocytosis (1,2). Rab5 exerts its function by interacting with several Rab5-specific effectors (1-3). These proteins form complexes with Rab5 on a specialized Rab domain of the endosome and promote recycling of Rab5-cargo targets between endosome and the plasma membrane.

The Neuronal Marker IF Antibody Sampler Kit provides an economical means for labeling neuronal structures by immunofluorescence (IF-F). This kit includes enough primary antibody to perform at least forty IF-F tests or two western blot experiments per primary antibody.
$489
96 assays
1 Kit
The PathScan® Phospho-eIF2α (Ser51) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of eIF2α phosphorylated at Ser51. A eIF2α rabbit antibody has been coated onto the microwells. After incubation with cell lysates, eIF2α protein is captured by the coated antibody. Following extensive washing, a phospho-eIF2α (Ser51) mouse detection antibody is added to detect captured phospho-eIF2α protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound mouse detection antibody. HRP substrate TMB is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of eIF2α phosphorylated at Ser51.Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

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, Mouse, Rat

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

Background: Alix, a phylogenetically conserved cytosolic scaffold protein, contains an N-terminal Bro1 domain, a coiled-coil region and a C-terminal proline-rich domain (1,2). Originally identified as an ALG-2 (apoptosis-linked gene 2)-interacting protein involved in programmed cell death (3,4), Alix also regulates many other cellular processes, such as endocytic membrane trafficking and cell adhesion through interactions with ESCRT (endosomal sorting complex required for transport) proteins, endophilins, and CIN85 (Cbl-interacting protein of 85 kDa) (5,6).

$61
500 ml
Ponceau S Staining Solution is supplied as ready to use. This product is recommended for rapid and reversible protein staining on nitrocellulose or PVDF membranes. This staining technique is often utilized to confirm protein electrotransfer in Western blotting assays prior to antibody-based detection.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, 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). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).

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

Application Methods: Western Blotting

Background: Caspase-6 (Mch2) is one of the major executioner caspases functioning in cellular apoptotic processes (1,2). Upon apoptotic stimulation, initiator caspases such as caspase-9 are cleaved and activated (3). The activated upstream caspases further process downstream executioner caspases, such as caspase-3 and caspase-6, by cleaving them into large and small subunits, thereby initiating a caspase cascade leading to apoptosis (4,5). One of the major targets for caspase-6 is the membrane associated protein lamin A (6). The cleavage of this protein causes cell membrane malfunction, membrane blebbing and eventual cell death.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Sphingosine kinases (SPHKs) catalyze the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), a lipid mediator with both intra- and extracellular functions. Together with other sphingolipid metabolizing enzymes, SPHKs regulate the balance of the lipid mediators, ceramide, sphingosine, and S1P (1-4). Two distinct SPHK isoforms, SPHK1 and SPHK2, have been cloned and characterized (5,6). SPHK1 and SPHK2 are highly conserved and diversely expressed (7,8). The SPHKs are activated by G protein-coupled receptors, receptor tyrosine kinases, immunoglobulin receptors, cytokines, and other stimuli (9-12). The molecular mechanisms by which SPHK1 and SPHK2 are specifically regulated are complex and only partially understood.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Bromodomain-containing protein 7 (BRD7, BP75, CELTIX-1) is a conserved bromodomain-containing protein that was first identified in a screen for proteins that interact with the PDZ domain of PSD95 (1). Subsequent studies identified BRD7 as a major component of SWI/SNF chromatin remodeling complexes, where it was shown to interact directly with acetylated histones to regulate gene transcription (2,3). BRD7 also interacts with p53, and was shown to participate directly in p53-dependent transcriptional regulation (4). Loss-of-function BRD7 mutations were identified in a subset of wild-type p53 breast cancer tumor samples, implicating BRD7 as a putative tumor-suppressor of potential clinical significance (5). BRD7 also associates with the BRCA1 protein, an interaction that facilitates recruitment of BRCA1 to the ERα gene promoter (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors critical for cellular differentiation, terminal functions and inflammatory response (1). Six members of the family have been characterized (C/EBPα, -β, -γ, -δ, -ε and -ζ) and are distributed in a variety of tissues (1). There are two forms of C/EBPβ, the 38 kDa liver activating protein (LAP) and the 20 kDa liver inhibitory protein (LIP) which may be products of alternative translation. The 38 kDa LAP protein is a transcriptional activator while LIP may act as an inhibitor of C/EBPβ transcriptional activity (2). Phosphorylation of C/EBPβ at distinct sites stimulates its transcriptional activity (3-5). Phosphorylation at serine 105 of rat C/EBPβ, a unique site only present in the rat sequence, seems essential for rat C/EBPβ activation (6).

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

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

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 Di-Methyl-Histone H3 Antibody Sampler Kit provides a fast and economical means of evaluating methylation sites on histone H3. The kit contains enough primary and secondary antibodies to perform two western blots.

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, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Flotillins belong to a family of lipid raft-associated integral membrane proteins that carry an evolutionarily conserved domain called the prohibitin homology domain (PHB) (1). Flotillin members are ubiquitously expressed and located in noncaveolar microdomains (lipid rafts) on the plasma membrane where they support signal transduction and regulate lipid raft motility and localization (2-5). Two flotillin members have been described, flotillin-1 and flotillin-2. In addition to its colocalization with lipid rafts on the plasma membrane, flotillin-1 also has been found in compartments of the endocytic and autophagosomal pathways, such as recycling/late endosomes, the Golgi complex, and the nucleus (6,7). Flotillin-2 is mainly localized to the plasma membrane and is prevalent in cell-cell contact sites. However, overexpressed flotillin-2 has also been found in the late endosome (4,8,9). Both flotillin-1 and flotillin-2 are commonly used as lipid raft-associated markers.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: IRG1 (Immune-responsive gene 1) is one of the most up-regulated genes in macrophages under proinflammatory conditions (1). It is also highly expressed in the pregnant uterus during implantation (2,3). IRG1 is a cis-aconitate decarboxylase that produces itaconic acid by decarboxylating cis-aconic acid, an intermediate of the tricarboxylic acid cycle (4). Itaconic acid is an endogenous inhibitor of succinate dehydrogenase, linking macrophage metabolic rewiring and regulation of inflammation (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The initiation of DNA replication in mammalian cells is a highly coordinated process that ensures duplication of the genome only once per cell division cycle. Origins of replication are dispersed throughout the genome, and their activities are regulated via the sequential binding of prereplication and replication factors. The origin recognition complex (ORC) is thought to be bound to chromatin throughout the cell cycle (1,2). The prereplication complex (Pre-RC) forms in late mitosis/early G1 phase beginning with the binding of CDT1 and cdc6 to the origin, which allows binding of the heterohexameric MCM2-7 complex. The MCM complex is thought to be the replicative helicase, and formation of the pre-RC is referred to as chromatin licensing. Subsequent initiation of DNA replication requires the activation of the S-phase promoting kinases CDK2 and cdc7. Cdc7, which is active only in complex with its regulatory subunit dbf4, phosphorylates MCM proteins bound to chromatin and allows binding of the replication factor cdc45 and DNA polymerase (3,4).Binding of CDT1 to geminin prevents pre-RC formation, and expression and degradation of geminin serve to regulate CDT1 activity (reviewed in 5). The interaction of CDT1 with MCM proteins is important in pre-RC formation and licensing (6,7). Both cdc6 and CDT1 are degraded by the ubiquitin proteasome pathway in response to DNA damage associated with rereplication (8).

The Malachite Green Phosphate Detection Kit is a convenient and sensitive, single-step free-phosphate determination kit that can be used for measuring phosphate released during enzymatic phosphatase assays.
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Tight junctions, or zona 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 (reviewed in 1). Zona occludens proteins ZO-1, -2, and -3 (also known as TJP1, 2, and 3) are peripheral membrane adaptor proteins that link junctional transmembrane proteins such as occludin and claudin to the actin cytoskeleton (reviewed in 2). ZO-1 and -2 are required for tight junction formation and function (3,4). In subconfluent proliferating cells, ZO-1 and ZO-2 have been shown to colocalize to the nucleus and play a role in transcriptional regulation, possibly through facilitating nuclear import/export of transcriptional regulators (5-7). The ZO-2 gene is transcribed from two promoters, generating the ZO-2A and ZO-2C isoforms. ZO-2C lacks a 23 amino acid amino-terminal sequence found in other ZO-2 isoforms. While both isoforms appear to be widely expressed, abnormal regulation of the ZO-2 gene may be correlated with development of ductal cancer (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: DPP4 (CD26) is a type II transmembrane glycoprotein expressed ubiquitously in most tissues and different cell types (1,2). The protein has a short cytoplasmic domain, transmembrane domain, a flexible stalk fragment and extracellular fragment (2). Both the catalytic peptide hydrolase domain and the beta-propeller ligand binding domain are located in the extracellular fragment (2). DPP4 is a multifunctional protein that exists in both a membrane bound form as well as an extracellular soluble form. As a peptidase, it removes N-terminal dipeptides sequentially from proteins with a proline or alanine as the penultimate P1 amino acid (3.4). DPP4 has been shown to cleave a wide range of substrates including GLP-1, BNP, substance P, etc. It is also involved in the regulation of related biological functions (5). In addition to it peptidase activity, DPP4 interacts with multiple important cell surface ligands, such as adenosine deaminase, fibronectin, and IGF2 receptor to influence processes like T cell activation, cell migration and proliferation (5). Several DPP4 inhibitors have been developed and their effects have been tested in the field of diabetes, cardiovascular disease and tumor immunity (2,5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TFAM (Transcription Factor A, Mitochondrial; aka TCF6) is a member of the high-mobility group (HMG) proteins because it contains two HMG boxes. TFAM is a transcription factor for mitochondrial DNA (mtDNA), and enhances mtDNA transcription in a promoter-specific fashion in the presence of mitochondrial RNA polymerase and transcription factor B (1). Because the majority of ATP production depends on the mitochondrial respiratory chain, maintenance of the mitochondrial genome is critical for normal health. TFAM plays an essential role in the maintenance of mtDNA and thus, ATP production (2). TFAM binds to mtDNA both nonspecifically and in a sequence-specific manner. It is known to have a dual effect on mtDNA: protection of mtDNA and initiation of transcription from mtDNA (3). TFAM attenuates age-dependent impairment of the brain by preventing oxidative stress and mitochondrial dysfunctions in microglia (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: 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).

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

Application Methods: Western Blotting

Background: β-Catenin is a key downstream effector in the Wnt signaling pathway (1). It is implicated in two major biological processes in vertebrates: early embryonic development (2) and tumorigenesis (3). CK1 phosphorylates β-catenin at Ser45. This phosphorylation event primes β-catenin for subsequent phosphorylation by GSK-3β (4-6). GSK-3β destabilizes β-catenin by phosphorylating it at Ser33, Ser37, and Thr41 (7). Mutations at these sites result in the stabilization of β-catenin protein levels and have been found in many tumor cell lines (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Troponin, working in conjunction with tropomyosin, functions as a molecular switch that regulates muscle contraction in response to changes in the intracellular Ca2+ concentration. Troponin consists of three subunits: the Ca2+-binding subunit troponin C (TnC), the tropomyosin-binding subunit troponin T (TnT), and the inhibitory subunit troponin I (TnI) (1). In response to β-adrenergic stimulation of the heart, Ser23 and Ser24 of TnI (cardiac) are phosphorylated by PKA and PKC. This phosphorylation stimulates a conformational change of the regulatory domain of TnC, reduces the association between TnI and TnC, and decreases myofilament Ca2+ sensitivity by reducing the Ca2+ binding affinity of TnC (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Thyroid Transcription Factor 1 (TTF-1, also known as NKX2-1), a member of the NKX homeobox transcription factor family, was initially discovered in the FRTL-5 rat thyroid cell line (1). Subsequent studies have shown that TTF-1 plays an important role in differentiation and morphogenesis of the developing thyroid, lung, and ventral forebrain (2). TTF-1 controls the expression of several genes, some of which are tissue specific, such as: thyroglobulin, thyroperoxidase, and the thyrotropin receptor in the thyroid; and surfactant proteins and clara cell secretory protein in the lung (2,3). Investigators have found that TTF-1 is expressed in malignant tumors of the thyroid and lung, and it is commonly used as a marker for both primary and malignant lung cancers (4-6).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric (mouse cells) and immunofluorescence (human cells) analysis. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Akt (Thr308) (D25E6) XP® Rabbit mAb #13038.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

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).

$115
40 immunoprecipitations
400 µl
Streptavidin (Magnetic Bead Conjugate) is useful for the precipitation of biotinylated proteins (1,2). Recombinant streptavidin is immobilized by the covalent binding of primary amino groups with formylbenzamide-modified magnetic bead.
APPLICATIONS

Application Methods: Immunoprecipitation

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

Application Methods: Western Blotting

Background: The Bcr gene was orginally identified by its presence in the chimeric Bcr-Abl oncogene (1). The amino-terminal region of Bcr contains an oligomerization domain, a serine/threonine kinase domain, and a region that binds SH2 domains. The middle of the protein has a PH domain and a region of sequence similarity to the guanine nucleotide exchange factors for the Rho family of GTP binding proteins. The carboxy-terminal region may be involved in a GTPase activating function for the small GTP-binding protein Rac (2,3). The function of wild type Bcr in cells remains unclear. PDGF receptor may use Bcr as a downstream signaling mediator (4). Research studies have shown that the Bcr-Abl fusion results in production of a constitutively active tyrosine kinase, which causes chronic myelogenous leukemia (CML) (5). Tyr177 of Bcr is phosphorylated in the Bcr-Abl fusion protein, which plays an important role in transforming the activity of Bcr-Abl (6). Phosphorylated Tyr177 provides a docking site for Gab2 and GRB2 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$271
500 assays (96 well format)
1 Kit
The Mitochondrial Membrane Potential Assay Kit (II) is a fluorescent assay that detects the mitochondrial membrane potential in living cells. The kit includes the cationic dye TMRE (tetramethylrhodamine ethyl ester perchlorate) and a mitochondrial membrane potential disruptor CCCP (carbonyl cyanide 3-chlorophenylhydrazone). TMRE is a cell membrane permeable, fluorescent dye that accumulates in intact mitochondria. Depolarized or inactive mitochondria exhibit decreased membrane potential, resulting in reduced TMRE accumulation.
APPLICATIONS

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)