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Product listing: CHD2 Antibody, UniProt ID O14647 #4170 to Atg2A Antibody, UniProt ID Q2TAZ0 #15011

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

Application Methods: Western Blotting

Background: Chromodomain-helicase-DNA-binding domain (CHD) proteins have been identified in a variety of organisms (1,2). This family of proteins, which consists of nine members, has been divided into three separate subfamilies: subfamily I (CHD1 and CHD2), subfamily II (CHD3 and CHD4), and subfamily III (CHD5, CHD6, CHD7, CHD8, and CHD9). All of the CHD proteins contain two tandem N-terminal chromodomains, a SWI/SNF-related ATPase domain, and a C-terminal DNA binding domain (1,2). The chromodomains facilitate binding to methylated lysine residues of histone proteins and confer interactions with specific regions of chromatin. The SWI/SNF-related ATPase domain utilizes the energy from ATP hydrolysis to modify chromatin structure. CHD1 is a euchromatic protein that associates with the promoters of active genes, and is required for the maintenance of open chromatin and pluripotency in embryonic stem cells (3-6). The two chromodomains of CHD1 facilitate its recruitment to active genes by binding to methyl-lysine 4 of histone H3, a mark associated with transcriptional activation (4-6). Yeast CHD1 is a component of the SAGA and SLIK histone acetyltransferase complexes, and is believed to link histone methylation with histone acetylation during transcriptional activation (6). The CHD2 protein is not well characterized; however, mouse knockout studies suggest important functions in development and tumor suppression. Homozygous CHD2 knockout mice exhibit delayed growth and perinatal lethality (7). Heterozygous knockout mice show increased mortality and gross organ abnormalities, in addition to increased extramedullary hematopoiesis and susceptibility to lymphomas (7,8). CHD2 mutant cells are defective in hematopoietic stem cell differentiation and exhibit aberrant DNA damage responses (8).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Myelin-oligodendrocyte glycoprotein (MOG) is a type I membrane bound glycoprotein of the immunoglobulin superfamily that is enriched in the in the outer lamella of the myelin sheath (1). The myelin sheath is a multi-layered membrane structure composed of oligodendrocytes that increases the conduction velocity of axonal impulses. The specific function of MOG is unknown, but MOG’s structure and expression during later stages of myelinogenesis suggests a role in myelin sheath maturation and maintenance (2). MOG may be an autoimmune target in central nervous system inflammatory diseases such as multiple sclerosis (MS) (3). Induction of MOG autoimmunity is also used as an experimental model for MS as injections of MOG peptide or recombinant protein in rodent models causes severe neurological disease that recapitulates several clinical features of MS (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Glutamatergic neurons release glutamate, the most common excitatory neurotransmitter. Their synaptic vesicles are filled with glutamate by vesicular glutamate transporters, VGLUTs (1). VGLUT1, also called solute carrier family 17 member 7 (SLC17A7), was first identified as an inorganic phosphate transporter (2). Despite the absence of homology with neurotransmitter transporters, VGLUT1 was later demonstrated to be a glutamate transporter (1) specific to glutamatergic neurons (3). Closely related to VGLUT1, VGLUT2 and VGLUT3 are also involved in glutamate uptake into synaptic vesicles, but define different neuronal subpopulations (4,5). VGLUT1 and VGLUT2 are the most abundant isoforms. VGLUT1 is expressed in the cortex, hippocampus, and cerebellar cortex, while VGLUT2 is mostly found in the thalamus (6,7). VGLUT3 is expressed in hair cells of the auditory system (8).

$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 VDAC (D73D12) Rabbit mAb #4661.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Voltage-dependent anion channel (VDAC), ubiquitously expressed and located in the outer mitochondrial membrane, is generally thought to be the primary means by which metabolites diffuse in and out of the mitochondria (1). In addition, this channel plays a role in apoptotic signaling. The change in mitochondrial permeability characteristic of apoptosis is mediated by Bcl-2 family proteins, which bind to VDAC, altering the channel kinetics (2). Homodimerization of VDAC may be a mechanism for changing mitochondrial permeability and supporting release of cytochrome c (3). In mammalian cells, there are three VDAC isoforms, VDAC1, which is the most widely expressed isoform, as well as VDAC2 and VDAC3 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: DOCK180 and its partner, ELMO1, interact directly with one another to form an atypical two-part guanine nucleotide exchange factor (GEF) for the small GTPase Rac (1). Rac activation occurs in association with p130 Cas and Crk, which form a complex with DOCK180 that is targeted to focal adhesions (2,3). DOCK180 is also recruited to the plasma membrane by binding to phosphoinositides (4). ELMO1 may function as an inhibitor of proteasome-dependent degradation of DOCK180 at the plasma membrane to regulate reorganization of the actin cytoskeleton (5). Localized Rac activation allows actin nucleation via WAVE family proteins, signaling to integrins, formation of lamellipodia and filopodia, and regulation of processes such as phagocytosis and cell migration (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Na(+)/glucose cotransporter 2 (SGLT2) is one of the two main glucose transporters in the kidney proximal convoluted tubule. It is activated by Protein Kinase A and Protein Kinase C, likely through phosphorylation of Ser624 (1,2). SGLT2 is responsible for the majority of glucose reabsorption in the kidney (3,4), and mutations in SGLT2 are known to cause familial renal glucosuria (5,6). SGLT2 is a therapeutic target for type 2 diabetes. Inhibitors of SGLT2 have been developed in order to treat people with type 2 diabetes (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: 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). SirT5, a mammalian homolog of Sir2, is localized to the mitochondria and has been implicated in the regulation of cell metabolism (2,3). SirT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1) in the mitochondrial matrix and increases its activity in response to fasting, allowing for adaptation to increased amino acid catabolism (4). SirT5 has also been shown to deacetylate cytochrome c in the mitochondrial intermembrane space (5). In addition to its deacetylase activity, SirT5 contains lysine desuccinylase and demalonylase activity (6,7). Succinyl-lysine and malonyl-lysine modifications occur in a variety of organisms and these post-translational modifications are found on many metabolic enzymes (6-8). Like phosphorylation of serine, threonine, and tyrosine residues, lysine succinylation and malonylation induces a change of two negative charges from a +1 to a -1 charge at physiological pH, and are thought to serve similar functions in the regulation of protein activity, protein-protein interactions, and protein stability. SirT5 knockout mice show increased levels of succinyl-lysine and malonyl-lysine protein modifications in the liver, including increased succinylation of CPS1, a known target of SirT5, suggesting that SirT5 functions to regulate metabolic enzymes through its deacetylase, desuccinylase, and demalonylase activities (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Keratins (cytokeratins) are intermediate filament proteins that are mainly expressed in epithelial cells. Keratin heterodimers composed of an acidic keratin (or type I keratin, keratins 9 to 23) and a basic keratin (or type II keratin, keratins 1 to 8) assemble to form filaments (1,2). Keratin isoforms demonstrate tissue- and differentiation-specific profiles that make them useful as research biomarkers (1). Research studies have shown that mutations in keratin genes are associated with skin disorders, liver and pancreatic diseases, and inflammatory intestinal diseases (3-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the Toll-like receptor (TLR) family, named for the closely related Toll receptor in Drosophila, play a pivotal role in innate immune responses (1-4). TLRs recognize conserved motifs found in various pathogens and mediate defense responses (5-7). Triggering of the TLR pathway leads to the activation of NF-κB and subsequent regulation of immune and inflammatory genes (4). The TLRs and members of the IL-1 receptor family share a conserved stretch of approximately 200 amino acids known as the Toll/Interleukin-1 receptor (TIR) domain (1). Upon activation, TLRs associate with a number of cytoplasmic adaptor proteins containing TIR domains, including myeloid differentiation factor 88 (MyD88), MyD88-adaptor-like/TIR-associated protein (MAL/TIRAP), Toll-receptor-associated activator of interferon (TRIF), and Toll-receptor-associated molecule (TRAM) (8-10). This association leads to the recruitment and activation of IRAK1 and IRAK4, which form a complex with TRAF6 to activate TAK1 and IKK (8,11-14). Activation of IKK leads to the degradation of IκB, which normally maintains NF-κB in an inactive state by sequestering it in the cytoplasm.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: HGK (MAP4K4 or mitogen-activated protein kinase kinase kinase kinase 4) is a serine/threonine kinase that belongs to the mammalian STE20/MAP4K kinase family involved in response to environmental stress and cytokines such as TNF-α (1-3). HGK specifically activates the c-Jun N-terminal kinase (JNK) signaling pathway and increases AP-1-mediated transcriptional activity in vivo (1). HGK is broadly expressed in many types of human cancer and cancer cell lines and plays an important role in cell transformation, invasiveness, adhesion and migration (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The mannose receptor (MR/CLEC13D/CD206/MMR/MRC1/Macrophage mannose receptor 1) is an endocytic receptor expressed by populations of dendritic cells, macrophages and nonvascular endothelium (1). The mannose receptor is a heavily glycosylated type I transmembrane protein with three types of extracellular domains and a short carboxy-terminal cytoplasmic domain with no apparent signaling motif (2-4). The extracellular portion of the protein is made up of a CR domain, which binds sulfated glycans, an FNII domain, which binds collagens, and eight C-type lectin domains, which bind carbohydrates containing mannose, fucose or GlcNAc (4-7). The receptor recycles between the plasma membrane and early endosomes (8). Functions include a role in antigen cross-presentation, clearance of endogenous proteins, pathogen detection and trafficking through lymphatic vessels (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Decay-accelerating factor (DAF/CD55) is a GPI-linked plasma membrane glycoprotein normally expressed on the surface of vascular endothelial and hematopoietic cells, which are continuously exposed to autologous complement components. In conjunction with other membrane complement regulatory proteins (CD35, CD46, and CD59), DAF/CD55 protects healthy cells from inappropriate complement-mediated lysis (1). DAF/CD55 inhibits activation of the complement cascade by promoting membrane dissociation and inactivation of C3 convertase, which inhibits amplification of the classical and alternative complement cascades (2). Research studies have demonstrated that DAF/CD55 is overexpressed in a variety of solid and liquid tumors, which functions to protect tumor cells from complement-mediated attack (3,4). Given its ability to disable the complement cascade and facilitate immune evasion by tumor cells, DAF/CD55 has received attention as a potential therapeutic target for the treatment of human malignancies. CD55 deficiency is also linked to human disease. The inability to express CD55 on the surface of erythrocytes renders them highly susceptible to complement-mediated lysis, which contributes to the development of paroxymal noctural hemoglobinuria (PNH). PNH is characterized by hemolytic anaemia, pancytopenia, and venous thrombosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Cancer/testis antigens (CTAs) are a family of more than 100 proteins whose normal expression is largely restricted to immune privileged germ cells of the testis, ovary, and trophoblast cells of the placenta. Although most normal somatic tissues are void of CTA expression, due to epigenetic silencing of gene expression, their expression is upregulated in a wide variety of human solid and liquid tumors (1,2). As such, CTAs have garnered much attention as attractive targets for a variety of immunotherapy-based approaches to selectively attack tumors (3).

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

Application Methods: Flow Cytometry, Western Blotting

Background: Protein phosphatase 5 (PP5) is a member of the serine/threonine phosphatase family that also includes PP1, PP2A and PP2B. PP5 uniquely contains an amino-terminal regulatory domain with three tetratricopeptide repeat (TPR) motifs and a carboxy-terminal catalytic domain (1-3). Through the TPR domain, PP5 interacts with a number of proteins and has been reported to be involved in diverse signal transduction pathways, including glucocorticoid receptor signaling, p53-mediated growth arrest, oxidative stress-mediated apoptosis and the response to ionizing radiation-induced DNA damage (4-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: 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 ubiquitin-activating enzyme (UBE1 or E1). The activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, and then from E2 to ubiquitin ligase E3 for final delivery to the ε-amino group of the target protein lysine residue (1-3). Combinatorial interactions of different E2 and E3 proteins result in substrate specificity (4). UBE1 has two isofoms: UBE1a is a nuclear protein of 117 kDa while UBE1b is a nuclear and cytoplasmic protein of 110 kDa (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Docking proteins are substrates of tyrosine kinases that function in the recruitment and assembly of specific signal transduction molecules. There are five members in the p62dok family, p62Dok (Dok-1), p56Dok-2 (Dok-2, or DoK-R), Dok-3, Dok-4 and Dok-5 (1-3), characterized by the presence of an amino-terminal PH domain, a central PTB domain and numerous potential sites of tyrosine phosphorylation. Tyrosine phosphorylation of p56Dok-2 occurs upon stimulation of cells with a variety of stimuli, or in cells transformed by oncogenic tyrosine kinases such as v-Src and Bcr-Abl (3-5). Based on the presence of several signaling domains (PH, PTB domain, tyrosine residue and proline-rich regions), it has been proposed that the p62dok family act as docking proteins that link RTKs to signal transduction pathways. p56Dok-2 has been proposed to be a negative regulator of cytokine-induced proliferation in T cells (5). Phosphorylated Tyr351 of p56Dok-2 mediates an association with the SH2 domain of Nck (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Pumilio 1 and Pumilio 2 (PUM1, PUM2, or Pumilio homolog 1 and 2, respectively) are evolutionarily conserved RNA binding proteins that are thought to repress translation and stability of mRNA targets by binding to the 3'-UTR of specific RNA sequences (1). Pumilio proteins have been implicated in the regulation of genes involved in embryogenesis and germline cell development (2). Research studies have shown that PUM2 may have a role in neural stem cell fate decisions (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Interferon regulatory factors (IRFs) comprise a family of transcription factors that function within the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in pathogen defense, autoimmunity, lymphocyte development, cell growth, and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, IRF-9/ISGF3γ, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7, and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA-binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA-binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS), and IFN regulatory elements (IRF-E) (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Uncoupling protein 3 (UCP3), a mitochondrial inner membrane transport protein, is highly expressed in skeletal muscle and activates glucose transport in muscle cells (2). UCP3 lowers the production of reactive oxygen species in mitochondria by reducing the mitochondrial inner membrane potential (3). UCP3 has been implicated in the protection against fat-induced insulin resistance in skeletal muscle (4) and fat gain induced by high-fat feeding (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The IL-17 family of cytokines consists of IL-17A-F, and their receptors include IL-17RA-RE (1). IL-17 cytokines are produced by a variety of cell types including the Th17 subset of CD4+ T cells, as well as subsets of γδ T cells, NK cells, and NKT cells (2). IL-17A and IL-17F, the most well-studied of the IL-17 cytokines, contribute to fungal and bacterial immunity by inducing expression of proinflammatory cytokines, chemokines, and antimicrobial peptides (2). In addition, IL-17A contributes to the pathogenesis of several autoimmune diseases (3). IL-17E promotes Th2 cell responses (4). The roles of IL-17B, IL-17C, and IL-17D are less clear, however these family members also appear to have the capacity to induce proinflammatory cytokines (1,5,6). IL-17 receptors have an extracellular domain, a transmembrane domain, and a SEFIR domain. They are believed to signal as homodimers, heterodimers, or multimers through their SEFIR domain by recruiting the SEFIR domain-containing adaptor Act1 (7). Unlike most cytokines that signal through Jak/STAT pathways, IL-17 signaling results in NF-κB activation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA polymerase γ (POLG, pol gamma) is a nuclear encoded protein that is responsible for mitochondrial genome replication in eukaryotic cells. The 140 kDa polymerase γ catalytic subunit forms a holoenzyme complex with a 55 kDa accessory protein (POLG2, pol γB) dimer, which confers processivity (1). In addition to polymerase activity, polymerase γ contains 3'-5' exonuclease activity for proofreading and 5′-deoxyribonucleic phosphate lyase activity that functions in DNA base excision repair (BER). The rate at which the catalytic subunit recognizes damaged DNA during DNA repair is enhanced by the pol γB accessory subunit (2). Mutations in the corresponding POLG gene are associated with several inherited neuropathies including progressive external ophthalmoplegia, myocerebrohepatopathy spectrum disorders and Alpers-Huttenlocher syndrome (3,4). Research studies indicate that mutations in the corresponding POLG gene may promote breast tumorigenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

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

Application Methods: Western Blotting

Background: Nicastrin is a transmembrane glycoprotein serving as an essential component of the γ-secretase complex (1,2). Nicastrin is physically associated with presenilin and plays an important role in the stabilization and correct localization of presenilin to the membrane-bound γ-secretase complex (3). Nicastrin also serves as a docking site for γ-secretase substrates such as APP and Notch, directly binding to them and properly presenting them to γ-secretase to ensure the correct cleavage process (2,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Synapse-associated protein 102 (SAP102, DLG3) belongs to the membrane-associated guanylate kinase (MAGUK) protein family and is a homolog of the Drosophila disc large (dlg) tumor suppressor protein. SAP102 consists of three PDZ domains, a Src homology 3 (SH3) domain, and a guanylate kinase (GK) domain (1). The SAP102 protein is more highly expressed in nonproliferating cells than in proliferating cells, indicating a role in the negative regulation of cell growth. SAP102 interacts with the carboxy terminus of the adenomatous polyposis coli (APC) tumor suppressor protein. Furthermore, SAP102 associates with PSD95 in the presence of calcium while the SH3 domain of SAP102 binds calmodulin (2,3). All three PDZ domains of SAP102 participate in binding to the NMDA receptor, interacting specifically with the carboxy-terminal domain of the N-methyl-D-aspartate receptor 2B (NR2B). This SAP102-NR2B interaction may facilitate AMPA receptor withdrawal from the postsynaptic membrane by inhibiting the Erk/MAPK pathway (1,4). Neuronal SAP102 is concentrated at dendritic shafts and spines, axons, and synaptic junctions. At excitatory synapses, SAP102 is involved in NMDA receptor clustering and immobilization and links NMDA receptors to the submembraneous cytomatrix (4). SAP102 and the NMDA receptor function together to mediate plasticity, behavior, and signal transduction (1). A nonsyndromic form of X-linked mental retardation is caused by loss-of-function mutations to the SAP102 gene. The SAP102 protein may be involved in autism since MAGUK proteins in the NMDA receptor complex bind directly to the autism susceptibility gene, neuroligin (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Activator protein 2γ (AP-2γ) is a member of the developmentally-regulated transcription factor activator protein 2 family (1). Overexpression of p53 in human breast cancer cells increases AP-2γ mRNA and protein (2). In addition, p53 binds to the AP-2γ promoter, suggesting that AP-2γ is a target of p53. AP-2γ therefore may contribute to p53-mediated growth inhibition (2). Studies also found that AP-2γ increases p21 mRNA and protein levels and induces cell-cycle arrest in G1 phase (3). Overexpression of AP-2γ inhibits the growth of human breast cancer cells (3). Taken together, these findings suggest that AP-2γ functions as a tumor suppressor (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Autophagy is a catabolic process that results in the degradation of bulk cytoplasmic contents within autophagosomes and lysosomes. The control of autophagy involves proteins encoded by a set of autophagy-related genes (Atg) that were originally characterized in yeast (1). Research studies in yeast indicate that Atg2 is essential for autophagy and the retrograde transport of Atg9 through an interaction with Atg18 (2-6). Two human Atg2 homologs (Atg2A, Atg2B) are critical for autophagosome formation as silencing of both results in the accumulation of unclosed autophagic structures (7). Starvation-induced autophagy targets Atg2A to the initiation site of autophagosome biogenesis, where it associates with DFCP1, WIPI-1, and other autophagy-related proteins (8).Atg2 proteins also function in lipid droplet metabolism as depletion of both Atg2A and AtgB results in changes in the size, number, and distribution of lipid droplets (7,8). These morphological changes in lipid droplets are not observed in Atg5-depleted cells, suggesting that this function is independent of the role of Atg2 in autophagy (7). Starvation-induced autophagy directs Atg2A (along with Atg14L) to localize to early autophagosomal membranes enriched in PI3P, while another subpopulation of Atg2A and Atg14L localizes to the lipid droplets independent of autophagic status (8). An increase in Atg2A expression during etoposide- and doxorubicin-induced apoptosis suggests that Atg2A may be a useful indicator of topoisomerase II inhibitor-mediated apoptosis (9). Mutations in the corresponding Atg2B gene are associated with gastric and colorectal carcinomas with high microsatellite instability (10).