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Product listing: USP15 (D1K6S) Rabbit mAb, UniProt ID Q9Y4E8 #66310 to GRB10 Antibody, UniProt ID Q13322 #3702

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs), respectively (1,2). DUBs are categorized into five subfamilies based on catalytic domain structure: USP, UCH, OTU, MJD, and JAMM. Ubiquitin carboxyl-terminal hydrolase 15 (USP15) is a USP subfamily deubiquitinating enzyme with similar domain structure to the paralogous DUBs, USP4, and USP11. The USP15 gene is amplified in glioblastoma and other solid tumors and its high expression correlates with a poor prognosis (3,4). Research studies demonstrate that USP15 is a positive regulator of oncogenic TGF-β signaling and that USP15 deubiquitinates monoubiquitinated R-SMADs to enhance target gene promoter binding (5). USP15 also promotes oncogenic TGF-β signaling by opposing SMURF2-mediated ubiquitination of the type I TGF-β receptor, which facilitates receptor stabilization (3,4). USP15 contributes to oncogenesis by negatively regulating T cell-mediated antitumor responses through the deubiquitination and stabilization of the E3 ubiquitin ligase MDM2. This observation supports USP15 as a potential target for cancer therapeutics (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Transcription factor EB (TFEB) is a member of the Myc-related, bHLH leucine-zipper family of transcription factors that drives the expression of a network of genes known as the Coordinated Lysosomal Expression and Regulation (CLEAR) network (1,2). TFEB specifically recognizes and binds regulatory sequences within the CLEAR box (GTCACGTGAC) of lysosomal and autophagy genes, resulting in the up-regulated expression of genes involved in lysosome biogenesis and function, and regulation of autophagy (1,2). TFEB is activated in response to nutrient deprivation, stimulating translocation to the nucleus where it forms homo- or heterooligomers with other members of the microphthalmia transcription factor (MiTF) subfamily and resulting in up-regulation of autophagosomes and lysosomes (3-5). Recently, it has been shown that TFEB is a component of mammalian target of rapamycin (mTOR) complex 1 (mTORC1), which regulates the phosphorylation and nuclear translocation of TFEB in response to cellular starvation and stress (6-9). During normal growth conditions, TFEB is phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation promotes association of TFEB with 14-3-3 family proteins and retention in the cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it increases transcription of CLEAR and autophagy genes (10). TFEB has also been shown to be activated in a nutrient-dependent manner by p42 MAP kinase (Erk2). TFEB is phosphorylated at Ser142 by Erk2 in response to nutrient deprivation, resulting in nuclear localization and activation, and indicating that pathways other than mTOR contribute to nutrient sensing via TFEB (3).

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

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

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. USP10 possesses amino acid sequences that match the consensus cysteine and histidine boxes representative of the USP family of deubiquitinating enzymes. At the posttranslational level, USP10 appears to be regulated through both protein-protein interactions and phosphorylation. Indeed, interaction of USP10 with Ras-GAP SH3 domain binding protein (G3BP) has been found to inhibit its ability to catalyze the disassembly of ubiquitin chains (3). Furthermore, ATM-mediated phosphorylation of USP10 at Thr42 and Ser337 was shown to promote USP10 stabilization and redistribution from the cytoplasm to the nucleus, where it functions in p53 deubiquitination, stabilization, and activation in response to genotoxic stress (4). Recently, it was shown that USP10 works in concert with USP13 and Vps34 complexes. USP10, along with USP13, appears to deubiquitinate Vps34 complexes to regulate the levels of this class III PI3K. Beclin-1, another component of these complexes, functions to regulate the stability of USP13, which can deubiquitinate and stabilize the levels of USP10. Therefore, Beclin-1, can indirectly regulate p53 stability by controlling the DUB activity of USP10 (5). USP10 also functions in the endosomal compartment, where it has been shown to deubiquitinate CFTR in order to enhance its endocytic recycling and cell surface expression (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription and replication of the eukaryotic genome. The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). CENP-A, also known as the chromatin-associated protein CSE4 (capping-enzyme suppressor 4-p), is an essential histone H3 variant that replaces canonical histone H3 in centromeric heterochromatin (2). The greatest divergence between CENP-A and canonical histone H3 occurs in the amino-terminal tail of the protein, which binds linker DNA between nucleosomes and facilitates proper folding of centromeric heterochromatin (3). The amino-terminal tail of CENP-A is also required for recruitment of other centromeric proteins (CENP-C, hSMC1, hZW10), proper kinetochore assembly and chromosome segregation during mitosis (4). Additional sequence divergence in the histone fold domain is responsible for correct targeting of CENP-A to the centromere (5). Many of the functions of CENP-A are regulated by phosphorylation (6,7). Aurora A-dependent phosphorylation of CENP-A on Ser7 during prophase is required for proper targeting of Aurora B to the inner centromere in prometaphase, proper kinetochore/microtubule attachment and proper alignment of chromosomes during mitosis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Inositol phospholipids have an important role in intracellular signaling in response to hormones, growth factors and neurotransmitters. Phosphatidylinositol 4-kinase phosphorylates phosphatidylinositol (PI) to phosphatidylinositol-4-phosphate (PIP). In a second step, PIP is further phosphorylated to phosphatidylinositol-4,5-bisphosphate (PIP2), and PIP2 is subsequently hydrolyzed by phospholipase C, producing the two intracellular second messengers, inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). PI4K230, PI4K92 and PI4K55 are three PI4 kinase isoforms that have been characterized and classified according to their molecular weights of 230, 92 and 55 kD. Previously, PI4 kinases were classified into type II and III enzymes (2). All isoforms are located on distinct membranes and cellular compartments suggesting various tasks. PI4K230 is located at the endoplasmatic reticulum and outer membranes of mitochondria, PI4K92 at the Golgi apparatus and endoplasmatic reticulum, and PI4K55 at the plasma membrane and endosomes (3-5). PI4K230 is predominantly expressed in brain and moderately sensitive to wortmannin as well as specifically and irreversibly inhibited by cyclitol derivatives (3, 6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway (1-3). The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses.

$262
50-100 transfections
300 µl
SignalSilence® NF-kappaB p65 siRNA from Cell Signaling Technology allows the researcher to specifically inhibit NF-kappaB p65 expression using RNA interference, a method in which gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce protein expression.
REACTIVITY
Human

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate (1). SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus (1,2). Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif (2), followed by tyrosine phosphorylation on the NPXY motif (2). The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1 (3-5). Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways (3-5). Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Disabled homologue 2 (Dab2) is a mitogen responsive phosphoprotein that exerts multiple functions through association with numerous proteins. Dab2 modulates signaling pathways through interactions with proteins such as Smads and TGF-β receptors (1,2), axin (3), GRB (4) and Src (5). Dab2 also serves as a cargo-specific adaptor of clathrin-mediated endocytosis via interaction with clathrin (6), AP2 (7), NPXY-containing cargo (8-10), and myosin VI (11,12). In addition, Dab2 regulates cell adhesion by directly binding integrins (13,14). The diverse functions of Dab2 enable it to coordinate cell adhesion, cell motility, membrane trafficking, and signaling. Research studies have shown Dab2 is down-regulated in a number of cancers, thereby suggesting a role as a tumor suppressor (15-17). Phosphorylation of Dab2 decreases its endocytotic function (18).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: FTO (fat mass and obesity-associated protein) is the first obesity gene product identified by genome-wide association studies and it is associated with the largest effect size for this class of proteins (1-4). Multiple single-nucleotide polymorphisms (SNPs) in the first intron of the FTO gene have been associated with increased body weight and obesity. Further studies reported that FTO risk alleles were associated with an increase in energy intake, a reduction of activity, and possibly an increased daily fat intake (4).FTO is a DNA and RNA demethylase that catalyzes the oxidative demethylation of thymidine and uracil. Among its targets is an mRNA subset involved in regulation of learning, reward behavior, motor functions, and feeding (5). Loss of the FTO gene in mice leads to postnatal growth retardation and a significant reduction in adipose tissue. Mice deficient in the FTO gene have lean body mass due to increased energy expenditure and systemic activation of sympathetic neurons, while overexpression of FTO in mice leads to increased food intake and results in obesity. These results demonstrate that FTO is functionally involved in energy homeostasis (6-8).

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

Application Methods: Western Blotting

Background: UBE3A, also commonly referred to as E6AP (E6 Associated Protein), is an E3 ubiquitin protein ligase and founding member of the HECT (Homologous to the E6 Carboxyl Terminus) family of E3 ligases (1). UBE3A has been shown to be hijacked by the oncogenic E6 protein of high-risk human papillomaviruses (HPV16 and HPV18) that causes the ubiquitination activity of UBE3A to be inappropriately directed toward several specific cellular proteins, the most notable of which, with respect to carcinogenesis, is p53 (2). Although the DNA-repair enzyme, HHR23A (human homolog A of Rad23), was the first described E6-independent substrate of UBE3A, very few E6-independent targets of UBE3A have been identified. This continues to be an active area of research, particularly because mutations or disruption in expression of UBE3A in the brain are the cause of Angelman syndrome (AS), a severe form of mental retardation (3-6). Although UBE3A is expressed in most human tissues from both parental alleles, it is expressed from the maternal allele in subregions of the brain, with the paternal allele being epigenetically silenced. AS is caused by disruptions in expression of the materal UBE3A allele, generally by large chromosomal deletion, but also by point mutations within the UBE3A coding sequence. This strongly suggests that lack of ubiquitination of one or more UBE3A substrates in neuronal tissue is responsible for the AS phenotype (7). Indeed, a recent study identified several new neuronal substrates of UBE3A including Arc and Ephexin-5 (8). The immediate early gene Arc (activity-regulated cytoskeleton-associated protein) is rapidly upregulated after robust neuronal stimulation and promotes internalization of AMPA-type glutamate receptors (AMPARs), resulting in reduction in synaptic strength. UBE3A ubiquitinates Arc and promotes its degradation by the 26S proteasome, thus preventing AMPAR internalization (8). Disruption in neuronal UBE3A function leads to an increase in Arc expression and a decrease in AMPARs at excitatory synapses, which may contribute to the neurological symptoms of AS.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cystathionine γ-lyase (CGL) is an enzyme in the transsulfuration pathway, a route in the metabolism of sulfur-containing amino acids (1). This enzyme regulates local vasodilation and blood pressure by generating hydrogen sulfide (H2S) as a physiological signaling molecule (2). A rodent model of sleep apnea showed that H2S production by cystathionine γ-lyase in the carotid body triggers hypertension in rodents during intermittent hypoxia, suggesting that inhibition of this enzyme may prevent the hypertension associated with sleep apnea (3). In addition, dietary restriction of sulfur-containing amino acids upregulates hepatic cystathionine γ-lyase expression in mice, leading to elevated production of H2S and protection from hepatic ischemia perfusion injury, indicating that this enzyme is critical for the benefits of dietary restriction (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Prospero homeobox protein 1 (PROX1) is a transcription factor known for its roles in organ development and lymphangiogenesis. It plays a critical role in the development of the CNS, lens, retina, liver, pancreas, and heart, and is considered to be the master regulator of the lymphatic system (1,2). PROX1 initiates the differentiation of lymphatic vasculature from the cardinal vein, where it is regulated by Sox18 (3,4). The PROX1 suppressor COUP-TFII represses the Notch pathway in venous endothelium, which prevents arterialization (4). HIF-1α and HIF-1β mediated hypoxia induces PROX1, which suggests a means of promoting lymphangiogenesis. Since the tumor microenvironment is typically hypoxic, regulation of PROX1 by hypoxia may also explain the up-regulation of this transcription factor in some cancers (2). PROX1 promotes colon cancer progression by down-regulating E-cadherin via miR-9, which promotes epithelial-mesenchymal transition (EMT) and metastasis (5). The PROX1 protein can act as a tumor suppressor in cases of hepatocellular carcinoma. PROX1 represses transcription of TWIST1, a transcription factor that promotes metastasis by binding the E-cadherin promoter. The function of PROX1 in other cancers is an area of active research (6).

$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 (COX IV (3E11) Rabbit mAb #4850).
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig, Rat, Zebrafish

Application Methods: Western Blotting

Background: Cytochrome c oxidase (COX) is a hetero-oligomeric enzyme consisting of 13 subunits localized to the inner mitochondrial membrane (1-3). It is the terminal enzyme complex in the respiratory chain, catalyzing the reduction of molecular oxygen to water coupled to the translocation of protons across the mitochondrial inner membrane to drive ATP synthesis. The 3 largest subunits forming the catalytic core are encoded by mitochondrial DNA, while the other smaller subunits, including COX IV, are nuclear-encoded. Research studies have shown that deficiency in COX activity correlates with a number of human diseases (4). The COX IV antibody can be used effectively as a mitochondrial loading control in cell-based research assays.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Correct segregation of sister chromatids prior to the onset of cell division is essential to the maintenance of genetic integrity and the avoidance of aneuploidy and chromosomal instability, characteristics of many cancer cells. The mitotic checkpoint, also known as the spindle assembly checkpoint, monitors accurate attachment of kinetochores to the spindle, inhibits mitosis and delays the onset of anaphase until all chromosomes are aligned at the metaphase plate (1). MAD2L1 is an essential participant in the mitotic checkpoint (2). It exists in two conformations, including the open and inactive O-MAD2 form and the closed, active C-MAD2 form. Prior to mitosis, MAD2L1 is localized to the cytosol and exists largely in the closed, inactive form. During the mitotic checkpoint, MAD2L1 switches to the open, active conformation (3). Together with other checkpoint proteins, MAD2L1 binds to and deactivates Cdc20, thereby inhibiting the anaphase promoting complex (4). When the kinetochores are correctly attached to the spindle, MAD2L1 releases Cdc20, which allows activation of the anaphase promoting complex and subsequent degradation of key mitotic substrates and the initiation of metaphase-anaphase transition (5).

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

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

Background: PHD finger protein 20 (PHF20) is a putative transcription factor protein. PHF20 contains a tudor domain, which facilitates binding to di-methylated histone H4 Lys20 (1). PHF20 may contribute to the development of cancers, including glioblastoma, lung cancer, colon cancer and ovarian cancer (2-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD14 is a leucine-rich repeat-containing pattern recognition receptor with expression largely restricted to the monocyte/macrophage cell lineage (1). Research studies have shown that CD14 is a bacterial lipopolysaccharide (LPS) binding glycoprotein, expressed as either a GPI-linked membrane protein or a soluble plasma protein (2). LPS induces an upregulation of GPI-linked CD14 expression, which facilitates TLR4 signaling and macrophage activation in response to bacterial infection (3-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Fer is a nonreceptor protein-tyrosine kinase of the Fes/Fps family. Like many other cytoplasmic tyrosine kinases, Fer contains a long amino-terminal domain, a central SH2 domain, and a carboxy-terminal kinase domain. Its amino-terminal domain is responsible for protein oligomerization as well as interaction with cytoskeletal proteins. Fer is ubiquitously expressed in a wide variety of cell and tissue types, and is localized to both cytoplasm and nucleus (1). Tyrosine kinase activity of Fer can be stimulated by growth factors and cytokines (2,3). After activation, Fer can further activate various downstream signaling components including Stat3 (3). Fer plays an important role in regulation of cell movement, oncogenesis and inflammation (4).

$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

Application Methods: Western Blotting

Background: Lymphocyte activation occurs in part through activation of the Ras signaling pathway following lymphocyte receptor stimulation. The RasGRP family of guanine nucleotide exchange factors (GEFs) catalyzes the exchange of GDP for GTP on Ras family small GTPases, promoting their active GTP-bound form. Diacylglycerol (DAG) or phorbol ester binding to RasGRP family members causes their translocation to the cell membrane and stimulates their activity (1,2). While T-Cells express RasGRP1, B-cells express both RasGRP1 and RasGRP3. RasGRP3 is important in linking B-cell receptor (BCR) activation to Ras signaling (3). In response to BCR stimulation, RasGRP3 is phosphorylated at Thr133 by PKC. This phosphorylation event further activates RasGRP3 in response to DAG, which stimulates PKC activity (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cyclin F is the founding member of the F-box protein family, present in all eukaryotic cells. F-box proteins are components of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. The substrate specificity of the SCF complex is determined by the interchangeable F-box proteins, which act as adaptors by associating with phosphorylated substrate proteins and recruiting them to the SCF core (1).Cyclin F contains a cyclin box domain in addition to an F-box domain, but does not regulate the activity of cyclin dependent kinases. Cyclin F expression does oscillate during the cell cycle, however, peaking in G2 phase (2).Cyclin F interacts with the centrosomal protein CP110, which plays critical roles centriole duplication and spindle formation. Cyclin F-mediated degradation of CP110 in G2 phase is required for normal progression into mitosis (3). In response to ionizing radiation, which causes DNA double strand breaks, Cyclin F interacts with B-Myb, preventing cyclin A-dependent phosphorylation of B-Myb, and delaying progression into mitosis. This G2 phase arrest allows the cell to respond to the DNA damage-induced G2/M phase checkpoint (4). Cyclin F also controls the stability of the ribonucleotide reductase M2 subunit, RRM2, which functions in maintaining the levels of dNTPs available in the cell for DNA synthesis and repair, in response to genotoxic stress (5). Researchers have implicated cyclin F as a prognostic marker in hepatocellular carcinoma (HCC) (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Frozen), 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bag1 belongs to the Bcl-2 associated athanogene (BAG) family of multifunctional proteins and was the first of six related proteins isolated from humans (1,2). This widely expressed protein interacts with a number of signaling molecules (including Bcl2, HGF receptor and Raf1) as it regulates signaling molecules in pathways involving cell survival, growth and differentiation. The most common role played by Bag1 protein is as an inhibitor of proteins favoring apoptosis (2-4). Bag1 also plays a role in Raf1 signaling and binds DNA as a transcription activator (4). Bag1 protein is a well-characterized inhibitor of its binding partner HSP70 (5). A conserved carboxy-terminal BAG domain within Bag1 interacts with the ATPase domain of HSP70 to negatively regulate heat shock protein chaperone activity (6,7). The multiple isoforms of Bag1 protein generated from a single transcript share a common ubiquitin homology domain and a carboxy-terminal Hsp70 binding region but differ in length and cellular localization. The 50 kDa long (Bag1-L) isoform also contains a nuclear localization signal and is often found in the nucleus where it activates transcription. The 46 kDa intermediate (Bag1-M) isoform is found mainly in the cytoplasm but can also translocate to the nucleus when associated with other proteins. The shorter 29-33 kDa isoforms (Bag1-S, Bag-1) isoforms are found primarily in the cytoplasm (8). High expression of the anti-apoptotic Bag1 protein correlates with increased survival in patients with particular forms of cancer, leading researchers to study possible therapeutic roles for Bag1 protein (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion that pair vesicular SNAREs (v-SNAREs) with cognate target SNARE (t-SNARE) proteins (reviewed in 1,2). Vesicle-associated membrane protein 7 (VAMP7), or tetanus neurotoxin-insensitive VAMP (TI-VAMP), is a widely expressed v-SNARE involved in exocytosis of granules and synaptic vesicles in various cell types, membrane remodeling, neurite outgrowth, lysosomal secretion, and autophagosome maturation (3). Activity of VAMP7 can be regulated by c-Src-mediated tyrosine phosphorylation, which activates VAMP7-mediated exocytosis (4). VAMP7 activity can also be regulated through interaction with the guanine nucleotide exchange factor Varp (5,6). Several research studies indicate that VAMP7 plays an important role in neurite outgrowth as well as potential neurological activities, including anxiety (7-9). VAMP7 also appears to have a key role in T-cell activation by facilitating the recruitment of vesicular Lat to the immunological synapse (10). The VAMP7 protein interacts with ATG16L, a component of the ATG5-ATG12 complex, and regulates autophagosome maturation through homotypic fusion of ATG16L1 vesicles (11).

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

Application Methods: Western Blotting

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

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CtBP2 (carboxy-terminal binding protein-2) and its homolog CtBP1 are transcriptional co-repressors originally identified as proteins that bind the carboxy-terminus of the human adenovirus E1A protein (1-3). CtBP proteins are thought to play important roles in regulating various developmental pathways because deletion of CtBP2 leads to embryonic lethality at E10.5 and is correlated with axial patterning defects (4). CtBP proteins regulate various oncogenic signaling pathways as promoters of epithelial-mesenchymal transition, apoptosis antagonists, and tumor suppressor genes repressors (1,5). The CtBP protein transcription co-repression activity results from interactions with numerous transcription factors and chromatin modulators, including the polycomb group proteins (1,6,7). Depending on the context, CtBP proteins interact with a short amino acid sequence motif (PXDLS) to mediate repression of target genes through both histone deacetylase-dependent and independent mechanisms (6,8,9). CtBP proteins display a high sequence homology to the bacterial D-isomer-specific 2-hydroxyacid dehydrogenase enzymes. Research studies indicate that nuclear NADH levels regulate CtBP transcription repression activities, as NADH binding is required for CtBP2 homodimerization and transcription co-repressor activity (6,9-11).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Presenilin 1 and presenilin 2 are transmembrane proteins belonging to the presenilin family. Mutation of presenilin genes has been linked to early onset of Alzheimer disease, probably due to presenilin's associated γ-secretase activity for amyloid-β protein processing (1,2). Endogenous presenilin mainly exists in a heterodimeric complex formed from the endoproteolytically processed amino-terminal (34 kDa) and carboxy-terminal (~20, 22, 23 kDa) fragments (CTF) (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: E4BP4/NFIL3 is a basic leucine zipper transcriptional regulator that plays a variety of roles in the immune system (1). For example, E4BP4/NFIL3 is required for bone marrow-derived NK cell development (2,3). In addition, it regulates IgE class switching in B cells by controlling IL-4 dependent induction of germ-line ε (GLε) transcription (4). In macrophages, E4BP4/NFIL3 is induced following exposure to bacteria and negatively regulates transcription of IL-12 p40. E4BP4/NFIL3 also controls cytokine production by T cells. Th2 cells from E4BP4/NFIL3(-/-) mice produced elevated levels of IL-5 an IL-13, but reduced levels of IL-4 ad IL-10 (5,6). Chronically stimulated Th1 cells, regulatory T cells, and NKT cells from E4BP4/NFIL3(-/-) mice all produce reduced levels of IL-10 and IL-13 (6). Finally, E4BP4/NFIL3 is also required for the development of conventional CD8α+ dendritic cells, as this subset is absent from E4BP4/NFIL3(-/-) mice (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Hemoglobin (Hb, Hgb) is a heme-containing transport protein found primarily in the red blood cells of humans and most other vertebrates. The primary function of hemoglobin is to transport oxygen from the external environment to the body tissues. Hemoglobin also facilitates metabolic waste removal by assisting in the transport of carbon dioxide from tissues back to the respiratory organs (1). Mature hemoglobin is a tetrameric protein complex, with each subunit containing an oxygen-binding heme group (2). Multiple isoforms of hemoglobin exist, which vary in relative abundance depending on developmental stage. Adult hemoglobin (HbA) is comprised of two α subunits and two β subunits and is the predominant hemoglobin found in red blood cells of children and adults. Fetal hemoglobin (HbF) contains two α subunits and two γ subunits and is the predominant isoform found during fetal and early postnatal development (2,3). Mutations that alter the structure or abundance of specific globin subunits can result in pathological conditions known as hemoglobinopathies (4). One such disorder is sickle cell disease, which is characterized by structural abnormalities that limit the oxygen carrying capacity of red blood cells. By contrast, thalassemia disorders are characterized by deficiencies in the abundance of specific hemoglobin subunits (4). Clinical treatments that are designed to alter the expression of specific hemoglobin subunits can be used to treat hemoglobinopathies (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The GRB7 family of adaptor proteins consist of GRB7, GRB10 and GRB14, which all contain an amino-terminal proline-rich SH3 binding domain, followed by PH, PBS, and SH2 domains. Each member of the family has several splice variants (1). It has been reported that GRB10 interacts with many receptor tyrosine kinases (RTKs) as well as downstream signal molecules including Raf, Akt, and Nedd4 (1,2). Although it was originally thought that GRB10 is exclusively phosphorylated at serine residues (3), Src kinase family members have been shown to phosphorylate GRB10 at Tyr67 (4).