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Product listing: CNPase (D83E10) XP® Rabbit mAb, UniProt ID P09543 #5664 to DPP4/CD26 (D6D8K) Rabbit mAb, UniProt ID P27487 #67138

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

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

Background: CNPase (2', 3’-cyclic nucleotide 3'-phosphodiesterase) catalyzes the in vitro hydrolysis of 2’, 3’-cyclic nucleotides to produce 2’-nucleotides. The in vivo molecular function and native substrate of this nucleotide phosphodiesterase remains under investigation (1). High CNPase expression is seen in oligodendrocytes and Schwann cells as CNPase accounts for roughly 4% of the total myelin protein in the central nervous system (2). CNPase binds to tubulin heterodimers and plays a role in tubulin polymerization, and oligodendrocyte process outgrowth (3). Typical myelination is seen in CNPase knock-out mice, but they suffer severe neurodegeneration from axonal loss and oligodendrocytes display abnormal paranodal loop structure prior to axonal degeneration. Paranodal loops typically contact the axolemma in axon-glial signaling; neurodegeneration in CNPase knock-out mice is a secondary consequence of impaired cell-cell communication (4).

$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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cas9 (7A9-3A3) Mouse mAb #14697.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The CRISPR associated protein 9 (Cas9) is an RNA-guided DNA nuclease and part of the Streptococcus pyogenes CRISPR antiviral immunity system that provides adaptive immunity against extra chromosomal genetic material (1). The CRISPR antiviral mechanism of action involves three steps: (i), acquisition of foreign DNA by host bacterium; (ii), synthesis and maturation of CRISPR RNA (crRNA) followed by the formation of RNA-Cas nuclease protein complexes; and (iii), target interference through recognition of foreign DNA by the complex and its cleavage by Cas nuclease activity (2). The type II CRISPR/Cas antiviral immunity system provides a powerful tool for precise genome editing and has potential for specific gene regulation and therapeutic applications (3). The Cas9 protein and a guide RNA consisting of a fusion between a crRNA and a trans-activating crRNA (tracrRNA) must be introduced or expressed in a cell. A 20-nucleotide sequence at the 5' end of the guide RNA directs Cas9 to a specific DNA target site. As a result, Cas9 can be "programmed" to cut various DNA sites both in vitro and in cells and organisms. CRISPR/Cas9 genome editing tools have been used in many organisms, including mouse and human cells (4,5). Research studies demonstrate that CRISPR can be used to generate mutant alleles or reporter genes in rodents and primate embryonic stem cells (6-8).

$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.

$327
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 analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cleaved Caspase-3 (Asp175) (D3E9) Rabbit mAb #9579.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Caspase-3 (CPP-32, Apoptain, Yama, SCA-1) is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP) (1). Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position (2).

$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).

$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.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Calcium/Calmodulin-dependent Protein Kinase Kinase 2 (CaMKK2) is a member of the CaMK family that contains a central Ser/Thr kinase domain followed by a regulatory domain consisting of overlapping autoinhibitory and CaM-binding regions (1). CaMKK2 can be distinguished from other CaMK family members by the presence of a unique Pro/Arg/Gly-rich insert following the ATP-binding domain (2). CaMKK2 phosphorylates CaMKI at Thr177 and CaMKIV at Thr200 (3). CaMKK2 also phosphorylates AMPKα in response to calcium (4). CaMKK2 has been implicated in long-term memory formation (5) and adipocyte development (6). CaMKK2 is phosphorylated at Ser511 by death-associated protein kinase (DAPK) in a signaling cascade thought to be involved in neuronal death (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey

Application Methods: Western Blotting

Background: PAI-1 is a secreted protein that belongs to the serine proteinase inhibitor (serpin) superfamily. It inhibits urokinase and tissue plasminogen activators (uPA and tPA) and thus, reduces the conversion of inactive plasminogen to plasmin (1). PAI-1 regulates fibrinolysis and plays an important role in vessel patency and tissue remodeling. Secreted PAI-1 interacts with the extracellular matrix (ECM) component vitronectin, thereby modulating cell-ECM interactions (2,3). PAI-1 is expressed in a variety of tissues with higher expression in liver, vascular endothelial cells, platelets, macrophages, and adipose tissue (1). Increased levels of PAI-1 are associated with deep vein thrombosis (4). Defects in PAI-1 cause plasminogen activator inhibitor-1 deficiency (PAI-1D), which is characterized by increased bleeding after injury or surgery (5). Research studies have shown that high levels of PAI-1 are associated with obesity, aging, insulin resistance, and type 2 diabetes (6-8). PAI-1 is transcriptionally regulated by TGF-β and mediates TGF-β-induced inhibition of cell migration and invasion in cancer cells (9). Studies have shown PAI-1 to be also involved in fibrosis (10).

$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).

$489
96 assays
1 Kit
CST's PathScan® Phospho-NF-KappaB p65 (Ser536) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Phospho-NF-KappaB p65 protein. A Phospho-NF-KappaB p65 (Ser 536) Mouse mAb has been coated onto the microwells. After incubation with cell lysates, phospho-NF-KappaB p65 protein is captured by the coated antibody. Following extensive washing, NF-KappaB p65 Rabbit mAb is added to detect the captured phospho-NF-KappaB p65 protein. Anti-rabbit IgG, HRP-linked Antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of optical density for this developed color is proportional to the quantity of phospho-NF-KappaB p65 (Ser536).Antibodies in kit are custom formulations specific to kit.
REACTIVITY
Human, Mouse

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$348
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 His-Tag (D3I1O) XP® Rabbit mAb #12698.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Flow Cytometry

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

$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: 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
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).

$147
1 ml
This Cell Signaling Technology product is useful for the detection of IgG. Conjugation of horseradish peroxidase (HRP) to protein A is obtained by cross-linking the amino groups on protein A with the carbohydrate groups on HRP.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

$305
100 µl
This Cell Signaling Technology 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 Ubiquitin (P4D1) Mouse mAb #3936.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

Background: Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7).

$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.

$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 ER and Golgi-Associated Marker Proteins Antibody Sampler Kit contains reagents to examine proteins that help regulate protein folding and vesicle trafficking. This kit includes enough antibody to perform two western blot experiments with each primary antibody.
$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).

$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: 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).

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

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

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: PARP, a 116 kDa nuclear poly (ADP-ribose) polymerase, appears to be involved in DNA repair in response to environmental stress (1). This protein can be cleaved by many ICE-like caspases in vitro (2,3) and is one of the main cleavage targets of caspase-3 in vivo (4,5). In human PARP, the cleavage occurs between Asp214 and Gly215, which separates the PARP amino-terminal DNA binding domain (24 kDa) from the carboxy-terminal catalytic domain (89 kDa) (2,4). PARP helps cells to maintain their viability; cleavage of PARP facilitates cellular disassembly and serves as a marker of cells undergoing apoptosis (6).

$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).

$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).

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

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

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$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).