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Product listing: Ape1 Antibody, UniProt ID P27695 #4128 to Atg5 Antibody, UniProt ID Q9H1Y0 #2630

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Ape1 (Apurinic/Apyrimidic eEndonuclease 1), also known as Ref1 (Redox effector factor 1), is a multifunctional protein with several biological activities. These include roles in DNA repair and in the cellular response to oxidative stress. Ape1 initiates the repair of abasic sites and is essential for the base excision repair (BER) pathway (1). Repair activities of Ape1 are stimulated by interaction with XRCC1 (2), another essential protein in BER. Ape1 functions as a redox factor that maintains transcription factors in an active, reduced state but can also function in a redox-independent manner as a transcriptional cofactor to control different cellular fates such as apoptosis, proliferation and differentiation (3). Increased expression of Ape1 is associated with many types of cancers including cervical, ovarian, prostate, rhabdomyosarcomas and germ cell tumors (4). Ape1 has been shown to stimulate DNA binding of several transcription factors known to be involved in tumor progression such as Fos, Jun, NF-κB, PAX, HIF-1, HLF and p53 (4). Mutation of the Ape1 gene has also been associated with amyotrophic lateral sclerosis (ALS) (5,6).

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

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Apoptosis related protein 3 (APR3), also known as C2orf28, is a membrane protein identified in HL-60 cells treated with all-trans retinoic acid (ATRA) and was later found to be induced by ATRA in other sensitive cell lines (1,2). APR3 is also up-regulated by NFAT and NF-κB activities (3). Regulation of APR3 by ATRA suggests a role in cell differentiation, but the mechanism of action is still unclear. Overexpression of APR3 can inhibit proliferation by inducing G1/S cell cycle arrest and decreasing expression of cyclin D1 (2). APR3 has also been shown to interact with NELL-1 to regulate osteoblast differentiation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: APS is an SH2 and PH domain-containing adaptor protein closely related to Lnk and SH2-B (1). APS was identified as a substrate for many receptor tyrosine kinases including TrkA, insulin receptor, c-Kit and PDGF receptor (2). Tyrosine phosphorylation of APS provides docking sites for downstrean signaling components, mediating diverse signaling pathways. APS plays quite different roles in RTK signaling. Overexpression of APS has been shown to inhibit PDGF-induced mitogenicity, which may result from APS/c-Cbl-mediated PDGF receptor degradation (3). However, APS promotes enhanced mitogenicity in response to insulin stimulation (4). The striking difference in APS-mediated signaling between the different RTKs could lie in the mode of interaction with the respective receptor.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Aquaporin 2 (AQP2) is a water transport protein that forms water channels in kidney tubules and plays a predominant role in controlling organism water homeostasis (1). Members of the aquaporin family are multiple pass transmembrane proteins that form homotetramers to facilitate the flow of water across the plasma membrane. At least thirteen aquaporins have been indentified to date (AQP0 through AQP12) and together this family of small, hydrophobic proteins plays a role in an array of biological processes that include urine formation, cell motility, fertilization, cell junction formation and regulation of overall water homeostasis (2). AQP2 tetramers form water channels that facilitate water transport and excretion in the kidney (3). This transport protein is localized to the plasma membrane is response to endocrine signaling. Posterior pituitary hormones arginine vasopressin (AVP) and ADH regulate osmotic water cell permeability by triggering phosphorylation and subsequent exocytosis of AQP2 (1,4). Mutations in the corresponding AQP2 gene cause a rare form of diabetes known as nephrogenic diabetes insipidus. This autosomal dominant disorder is characterized by abnormal water reabsorption by kidney tubules due, in part, to either nonfunctional or mislocalized AQP2 protein (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein acetylation is a common modification that occurs both at lysine residues within proteins (ε-amino acetylation) and multiple amino acid residues at the amino terminus of proteins (α-amino acetylation). The N-α-acetyltransferase ARD1 homolog A protein (ARD1A, also known as NAA10) and the highly homologous N-α-acetyltransferase ARD1 homolog B protein (ARD1B, also known as ARD2 or NAA11) are mutually exclusive catalytic subunits of the amino-terminal acetyltransferase complex (NatA) (1-3). This complex, which consists of either ARD1A or ARD1B and the N-α-acetyltransferase 15 (NAA15) auxiliary protein, localizes to ribosomes where it functions to acetylate Ser-, Ala-, Gly-, Thr-, Cys-, Pro-, and Val- amino termini after initiator methionine cleavage during protein translation (1-5). Like ε-amino acetylation, amino-terminal α-amino acetylation functions to regulate protein stability, activity, cellular localization, and protein-protein interactions (4,5). Defects in ARD1A have been shown to cause amino-terminal acetyltransferase deficiency (NATD), which results in severe delays and defects in postnatal growth (6).In addition to functioning as amino-terminal acetyltransferases in the NatA complex, free ARD1A and ARD1B proteins regulate cell growth and differentiation through ε-amino acetylation of lysine residues in multiple target proteins, including the HIF-1α, β-catenin, and AP-1 transcription factors (7-9). ARD1A-mediated acetylation of HIF-1α at Lys532 under normoxic conditions enhances binding of VHL, leading to increased ubiquitination and degradation of HIF-1α and down-regulation of HIF-1α target genes involved in angiogenesis, apoptosis, cellular proliferation, and glucose metabolism (7). Decreased expression of ARD1A under hypoxic conditions contributes to the stabilization of HIF-1α and upregulation of target genes (7). ARD1A also promotes cell proliferation and tumorigenesis by acetylating and activating β-catenin and AP-1 transcription factors, leading to the stimulation of cyclin D1 expression (8,9). Interestingly, the acetyltransferase activity of ARD1A is regulated by autoacetylation at Lys136, which is required for the ability of ARD1A to promote proliferation and tumorigenesis (9). Research studies have shown that ARD1 proteins are over-expressed in multiple cancers, including breast, prostate, lung, and colorectal cancers (10-13).

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

Application Methods: Western Blotting

Background: ADP-ribosylation factor (Arf) proteins are low molecular weight GTP binding proteins that belong to the Ras GTPase superfamily (1). Arf proteins are grouped into three distinct classes based on amino acid sequence and structural similarity, with Arf6 as the single class III protein to date. Arf6 is localized mainly to the plasma membrane and endosomes (1,2). This small GTPase interacts with PIP5K, PLD and Rac1, proteins important in lipid metabolism and actin regulation. Arf6 function depends upon its cycling between GDP- and GTP-bound states, which is regulated by associated GAP and GEF factors (3,4). Plasma membrane-associated Arf6 appears to play several functions during the many steps of membrane trafficking, including regulating membrane receptor internalization in both clathrin-dependent and independent pathways, endosomal recycling, and proximal actin reorganization and remodeling (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4, 6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4, 6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Arginase-2 is a mitochondrial enzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea (1). Research studies have shown that in acute myeloid leukemia (AML) patients, arginase-2 is released from AML blasts to the plasma, leading to the suppression of T-cell proliferation (2). It was also shown that arginase-2 is required for the immunosuppressive properties of neonatal CD71(+) erythroid cells, which inhibits neonatal host defense against infection (3). In addition, the expression of arginase-2 in dendritic cells is repressed by microRNA-155 during maturation (4). This repression is essential for T-cell activation and response (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Small non-coding RNAs are important regulators of gene expression in higher eukaryotes (1,2). Several classes of small RNAs, including short interfering RNAs (siRNAs) (3), microRNAs (miRNAs) (4), and Piwi-interacting RNAs (piRNAs) (5), have been identified. MicroRNAs are about 21 nucleotides in length and have been implicated in many cellular processes such as development, differentiation, and stress response (1,2). MicroRNAs regulate gene expression by modulating mRNA translation or stability (2). MicroRNAs function together with the protein components in the complexes called micro-ribonucleoproteins (miRNPs) (2). Among the most important components in these complexes are Argonaute proteins (1,2). There are four members in the mammalian Argonaute family and only Argonaute 2 (Ago2) possesses the Slicer endonuclease activity (1,2). Argonaute proteins participate in the various steps of microRNA-mediated gene silencing, such as repression of translation and mRNA turnover (1).

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

Application Methods: Western Blotting

Background: AMP-activated protein kinases (AMPKs) constitute a serine/threonine protein kinase family, which is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPKα1, AMPKα2, MELK and SNARK are the catalytic subunits in the family (2). Recently, AMPK-related protein kinase ARK5 was identified, which shares 84% similarity with the sequence of the catalytic domain of SNARK (2). In vitro, Akt phosphorylates ARK5 at Ser600. This phosphorylation activates ARK5, which in turn results in the increased phosphorylation of the SAMS peptide, an AMPK consensus substrate (2). In vivo experiments showed that Akt-activated ARK5 is critical for the survival of cells under glucose starvation (2). Furthermore, studies also linked ARK5 to tumor invasion (3, 4). Overexpressed ARK5 leads to higher tumor growth rate (3). For example, the overexpression of ARK5 in pancreatic tumor cell line PANC-1 significantly elevates its metastasis in the liver (4).

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

Application Methods: Western Blotting

Background: Actin nucleation, the formation of new actin filaments from existing filaments, affects actin filament structure during cell motility, division, and intracellular trafficking. An important actin nucleation protein complex is the highly conserved ARP2/3 complex, consisting of ARP2, ARP3, and ARPC1-5. The ARP2/3 complex promotes branching of an existing actin filament and formation of a daughter filament following activation by nucleation-promoting factors, such as WASP/WAVE or cortactin (1). The formation of podosomes, small cellular projections that degrade the extracellular matrix, is enhanced by ARP2/3 complex action. ARP2/3 competes with caldesmon, an actin binding protein shown to negatively affect podosome formation (2). Along with N-WASP, the ARP2/3 complex regulates nuclear actin filament nucleation and controls actin polymerization during transcription (3).

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

Application Methods: Western Blotting

Background: Actin nucleation, the formation of new actin filaments from existing filaments, affects actin filament structure during cell motility, division, and intracellular trafficking. An important actin nucleation protein complex is the highly conserved ARP2/3 complex, consisting of ARP2, ARP3, and ARPC1-5. The ARP2/3 complex promotes branching of an existing actin filament and formation of a daughter filament following activation by nucleation-promoting factors, such as WASP/WAVE or cortactin (1). The formation of podosomes, small cellular projections that degrade the extracellular matrix, is enhanced by ARP2/3 complex action. ARP2/3 competes with caldesmon, an actin binding protein shown to negatively affect podosome formation (2). Along with N-WASP, the ARP2/3 complex regulates nuclear actin filament nucleation and controls actin polymerization during transcription (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Arrestin proteins function as negative regulators of G protein-coupled receptor (GPCR) signaling. Cognate ligand binding stimulates GPCR phosphorylation, which is followed by binding of arrestin to the phosphorylated GPCR and the eventual internalization of the receptor and desensitization of GPCR signaling (1). Four distinct mammalian arrestin proteins are known. Arrestin 1 (also known as S-arrestin) and arrestin 4 (X-arrestin) are localized to retinal rods and cones, respectively. Arrestin 2 (also known as β-arrestin 1) and arrestin 3 (β-arrestin 2) are ubiquitously expressed and bind to most GPCRs (2). β-arrestins function as adaptor and scaffold proteins and play important roles in other processes, such as recruiting c-Src family proteins to GPCRs in Erk activation pathways (3,4). β-arrestins are also involved in some receptor tyrosine kinase signaling pathways (5-8). Additional evidence suggests that β-arrestins translocate to the nucleus and help regulate transcription by binding transcriptional cofactors (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin is a major hormone controlling critical energy functions, such as glucose and lipid metabolism. Insulin binds to and activates the insulin receptor (IR) tyrosine kinase, which phosphorylates and recruits adaptor proteins. The signaling pathway initiated by insulin and its receptor stimulates glucose uptake in muscle cells and adipocytes through translocation of the Glut4 glucose transporter from the cytoplasm to the plasma membrane (1). A 160 kDa substrate of the Akt Ser/Thr kinase (AS160, TBC1D4) is a Rab GTPase-activating protein that regulates insulin-stimulated Glut4 trafficking. AS160 is expressed in many tissues including brain, kidney, liver, and brown and white fat (2). Multiple Akt phosphorylation sites have been identified on AS160 in vivo, with five sites (Ser318, Ser570, Ser588, Thr642, and Thr751) showing increased phosphorylation following insulin treatment (2,3). Studies using recombinant AS160 demonstrate that insulin-stimulated phosphorylation of AS160 is a crucial step in Glut4 translocation (3) and is reduced in some patients with type 2 diabetes (4). The interaction of 14-3-3 regulatory proteins with AS160 phosphorylated at Thr642 is a necessary step for Glut4 translocation (5). Phosphorylation of AS160 by AMPK is involved in the regulation of contraction-stimulated Glut4 translocation (6).

$260
100 µl
APPLICATIONS

Application Methods: Western Blotting

Background: CRISPR-Cas (clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins) are RNA-guided nuclease effectors that are utilized for precise genome editing in mammalian systems (1). Cpf1 (CRISPR from Prevotella and Francisella) are members of the Class 2 CRISPR system (2). Class 2 CRISPR systems, such as the well characterized Cas9, rely on single-component effector proteins to mediate DNA interference (3). Cpf1 endonucleases, compared to Cas9 systems, have several unique features that increase the utility of CRISPR-based genome editing techniques: 1) Cpf1-mediated cleavage relies on a single and short CRISPR RNA (crRNA) without the requirement of a trans-activating crRNA (tracrRNA), 2) Cpf1 utilizes T-Rich protospacer adjacent motif (PAM) sequences rather than a G-Rich PAM, and 3) Cpf1 generates a staggered, rather than a blunt-ended, DNA double-stranded break (2). These features broaden the utility of using CRISPR-Cas systems for specific gene regulation and therapeutic applications. Several Cpf1 bacterial orthologs have been characterized for CRISPR-mediated mammalian genome editing (2, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: ASF1 was first identified in S. cerevisiae based on its ability to de-repress transcriptional silencing when overexpressed (1). While only one gene exists in yeast and Drosophila, mammalian cells contain the two highly homologous ASF1A and ASF1B genes (2). ASF1A and ASF1B function as histone chaperones, delivering histone H3/H4 dimers to CAF-1 or HIRA histone deposition complexes to facilitate replication-coupled and replication-independent nucleosome assembly on DNA (2-5). Both ASF1A and ASF1B bind to CAF-1, but only ASF1A binds to HIRA (5). In addition to playing a role in DNA replication and gene silencing, ASF1 functions in DNA damage repair, genome stability and cellular senescence. Deletion of ASF1 in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint (6-8). Depletion of both ASF1A and ASF1B in mammalian cells results in the accumulation of cells in S phase, increased phosphorylation of H2A.X, centrosome amplification and apoptosis (9,10). ASF1A is required for the formation of senescence-associated heterochromatin foci (SAHF), with overexpression of ASF1A inducing senescence in primary cells (4). Both ASF1A and ASF1B are phosphorylated in S phase by the Tousled-like kinases TLK1 and TLK2, and are dephosphorylated when TLK1 and TLK2 are inactivated by Chk1 kinase in response to replicative stress (11,12). The function of ASF1 phosphorylation is not yet understood.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Apoptosis signal-regulating kinase 1 (ASK1), a MAP kinase kinase kinase, plays essential roles in stress-induced apoptosis (1,2). ASK1 is activated in response to a variety of stress-related stimuli through distinct mechanisms and activates MKK4 and MKK3, which in turn activate JNK and p38 (3). Overexpression of ASK1 activates JNK and p38 and induces apoptosis in several cell types through signals involving the mitochondrial cell death pathway. Embryonic fibroblasts or primary neurons derived from ASK1-/- mice are resistant to stress-induced JNK and p38 activation as well as cell death (4,5). Phosphorylation at Ser967 is essential for ASK1 association with 14-3-3 proteins and suppression of cell death (6). Oxidative stress induces dephosphorylation of Ser967 and phosphorylation of Thr845 in the activation loop of ASK1, both of which are correlated with ASK1 activity and ASK1-dependent apoptosis (7,8). Akt phosphorylates ASK1 at Ser83, which attenuates ASK1 activity and promotes cell survival (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to produce ceramide and phosphocholine (1). Ceramide is an important bioactive lipid triggering signal transduction involved in cell proliferation, apoptosis and differentiation (1,2). A number of SMases have been described and categorized based on their optimum pH activity, cation dependence, tissue distribution, and subcellular localization (1). These include a lysosomal acid SMase, a Zn++-dependent secreted acid SMase, a membrane-bound Mg++-dependent neutral SMase, a Mg++-independent neutral SMase, and an alkaline SMase.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Astrin/SPAG5 was identified as a microtubule-associated protein in a mitotic extract (1). It is essential for cells to assemble biploar spindle structures and progress through mitosis (1, 2). Astrin/SPAG5 was also identified to be a component associated with outer dense fibers in the sperm tail (3). In addition, this protein negatively regulates mTORC1 activity during the cell stress response (4). Under stress conditions, Astrin/SPAG5 interacts with the mTORC1 component raptor and recruits raptor to stress granules, thereby suppressing mTORC1 formation (4). The inhibition of mTORC1 prevents its hyperactivation and thus keeps cells from undergoing apoptosis during stresses (4). Furthermore, Astrin/SPAG5 has been implicated to be a prognostic marker in breast cancer (5).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Mouse, Rat

Application Methods: Western Blotting

Background: Spinocerebellar ataxia 1 (SCA1), an autosomal dominant neurodegenerative disorder, is characterized by slurred speech, loss of limb coordination, and gait abnormalities resulting from the degeneration of cerebellar Purkinje cells and of a subset of brainstem neurons (1). Individuals with SCA1 have a highly polymorphic CAG repeat expansion encoding a polyglutamine tract in ataxin-1 (2). Akt phosphorylates ataxin-1 at Ser776, which regulates an association with 14-3-3. This interaction increases ataxin-1 stabilization and accumulation resulting in enhanced neurodegeneration (3). In addition, HSP70 controls the effect that phosphorylation has on ataxin-1 stability (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but is also associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, which are cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vps34, including p105/Vps15, Beclin-1, UVRAG, Atg14, and Rubicon (6-12). Atg14 and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14 localizes to autophagosomes, isolation membranes, and ER and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).

$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).

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

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related genes (Atg). Formation of the autophagic vesicles involves two ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are essential for autophagy and widely conserved in eukaryotes (2). There are at least three Atg8 homologs in mammalian cells, GATE-16, GABARAP, and LC3, that are conjugated by lipids (3,4). Lipid conjugation of Atg8 and its mammalian homologs requires Atg3 (Apg3p/Aut1p in yeast), an ubiquitously expressed E2-like enzyme (5-7). Following C-terminal cleavage by the cysteine protease Atg4, the exposed glycine residue of Atg8 binds to the E1-like enzyme Atg7, is transferred to Atg3, and then conjugated to phophatidylethanolamine. Atg3-deficient mice die within 1 day after birth and are completely defective for the conjugation of Atg8 homlogs and autophagome formation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. Control of autophagy was largely discovered in yeast and involves proteins encoded by a set of autophagy-related genes (Atg) (1). Formation of autophagic vesicles requires a pair of essential ubiquitin-like conjugation systems, Atg12-Atg5 and Atg8-phosphatidylethanolamine (Atg8-PE), which are widely conserved in eukaryotes (2). Numerous mammalian counterparts to yeast Atg proteins have been described, including three Atg8 proteins (GATE-16, GABARAP, and LC3) and four Atg4 homologs (Atg4A/autophagin-2, Atg4B/autophagin-1, Atg4C/autophagin-3, and Atg4D/autophagin-4) (3-5). The cysteine protease Atg4 is pivotal to autophagosome membrane generation and regulation. Atg4 primes the Atg8 homolog for lipidation by cleaving its carboxy terminus and exposing its glycine residue for E1-like enzyme Atg7. The Atg8 homolog is transferred to the E2-like enzyme Atg3 before forming the Atg8-PE conjugate. During later stages of autophagy, Atg4 can reverse this lipidation event by cleaving PE, thereby recycling the Atg8 homolog (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation but has also been associated with a number of physiological processes including development, differentiation, neurodegeneration, infection, and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and referred to as autophagy-related (Atg) genes. Formation of the autophagosome involves a ubiquitin-like conjugation system in which Atg12 is covalently bound to Atg5 and targeted to autophagosome vesicles (4-6). This conjugation reaction is mediated by the ubiquitin E1-like enzyme Atg7 and the E2-like enzyme Atg10 (7,8).