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Product listing: Atg12 (D88H11) Rabbit mAb, UniProt ID O94817 #4180 to Aurora A/AIK (1G4) Rabbit mAb, UniProt ID O14965 #4718

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

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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.Atg13/Apg13 was originally identified in yeast as a constitutively expressed protein that was genetically linked to Atg1/Apg1, a protein kinase required for autophagy (4). Overexpression of Atg1 suppresses the defects in autophagy observed in Atg13 mutants (4). Autophagy requires a direct association between Atg1 and Atg13, and is inhibited by TOR-dependent phosphorylation of Atg13 under high-nutrient conditions (5). Similarly, mammalian Atg13 forms a complex with the Atg1 homologues ULK1/2, along with FIP200, which localizes to autophagic isolation membranes and regulates autophagosome biogenesis (6-8). mTOR phosphorylates both Atg13 and ULK1, suppressing ULK1 kinase activity and autophagy (7-9). ULK1 can directly phosphorylate Atg13 at a yet unidentified site, presumably to promote autophagy (7,8). Additional studies suggest that Atg13 and FIP200 can function independently of ULK1 and ULK2 to induce autophagy through an unknown mechanism (10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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.Atg13/Apg13 was originally identified in yeast as a constitutively expressed protein that was genetically linked to Atg1/Apg1, a protein kinase required for autophagy (4). Overexpression of Atg1 suppresses the defects in autophagy observed in Atg13 mutants (4). Autophagy requires a direct association between Atg1 and Atg13, and is inhibited by TOR-dependent phosphorylation of Atg13 under high-nutrient conditions (5). Similarly, mammalian Atg13 forms a complex with the Atg1 homologues ULK1/2, along with FIP200, which localizes to autophagic isolation membranes and regulates autophagosome biogenesis (6-8). mTOR phosphorylates both Atg13 and ULK1, suppressing ULK1 kinase activity and autophagy (7-9). ULK1 can directly phosphorylate Atg13 at a yet unidentified site, presumably to promote autophagy (7,8). Additional studies suggest that Atg13 and FIP200 can function independently of ULK1 and ULK2 to induce autophagy through an unknown mechanism (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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 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, 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 Vsp34, including p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, to determine Vsp34 function (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).

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

Application Methods: Immunofluorescence (Immunocytochemistry), 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 (LC3)-phosphatidylethanolamine (LC3-PE), which are widely conserved in eukaryotes (2).Mammalian Atg16L1, containing an amino-terminal coiled coil domain and carboxyl-terminal WD-repeats, has multiple isoforms produced by alternative splicing (3,4). Atg16L1 provides a functional link between the two crucial ubiquitin-like conjugation systems of autophagy. Atg16L1 binds Atg5 of the Atg12-Atg5 conjugate forming an 800 kDa multimeric complex (3). The Atg12-Atg-5-Atg16L1 complex localizes to pre-autophagosomal membranes where it determines the site of LC3 lipidation and catalyzes the reaction required for the formation of mature autophagosomes (3,5). Genome-wide association scanning revealed variations in the Atg16L1 gene associated with Crohn's disease (6,7). Mice lacking the coiled coil domain of Atg16L1 have impaired autophagosome formation and elevated inflammatory cytokines, consistent with its role in inflammatory disease pathogenesis (8). Hypomorphic Atg16L1 mice also show defects in autophagy and abnormalities in intestinal Paneth cell function similar to that found in Crohn's disease (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

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, Mouse, Rat

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).

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

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).

$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).

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

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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). It 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 (4).Atg9, one of the Atg proteins identified in yeast, is essential for autophagosome formation (5). There are two human functional orthologues based on the yeast homolog Atg9p: Atg9A, which has also been identified as Atg9L1 and mAtg9, and Atg9L2, which was first reported as nitric-oxide synthase 3 antisense (NOS3AS) (6,7). Atg9A is an integral membrane protein that is required for both the initiation and the expansion of the autophagosome (6,7). Recruitment of Atg9A to the autophagosomal membrane is dynamic and transient as Atg9A also cycles between autophagy-related structures known as omegasomes, the trans-Golgi network (TGN), and endosomes, and at no point becomes a stable component of the autophagosomal membrane (6,8). The precise regulation of Atg9A trafficking is not fully clarified, yet it is suggested to involve p38 mitogen-activated protein kinase (MAPK)-binding protein p38IP and the Beclin-1-binding protein Bif-1 (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Triglycerides form an important energy store in many living organisms. Adipose tissue serves as the primary storage depot for triglycerides in mammals. Lipolytic enzymes mobilize triglycerides during periods of starvation to provide organisms with necessary energy. Hormone-sensitive lipase (HSL), the first identified lipolytic enzyme, hydrolyzes triglycerides in mammalian adipose tissues (1-3). Additional lipolytic enzymes, including adipose triglyceride lipase (ATGL), have also been discovered. The primary function of ATGL is to catalyze the hydrolysis of the first ester bond of lipid molecules. This enzyme may provide diglyceride substrates for HSL hydrolysis. ATGL is abundantly expressed in murine white and brown adipose tissue, and is highly substrate specific (4). ATGL was independently identified as desnutrin (5) and the TG-hydrolace inducible phospholipase-A2-ζ (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Atlastin proteins are highly conserved members of the dynamin superfamily of membrane GTPases that are involved in the formation of vesicles for the endocytotic and secretory processes (1). Atlastins are required to establish and maintain the morphology of the tubular endoplasmic reticulum (ER) and are therefore important in ER function (2). GTP hydrolysis and dimerization are required for atlastin-dependent ER membrane fusion (3).Atlastin GTPase 1 (ATL1) is primarily expressed in brain, while the related atlastin 2 and atlastin 3 proteins are ubiquitously expressed (4). Mutations in the atlastin 1 gene SPG3A and the ER defects that result are thought to cause one form of hereditary spastic paraplegia (HSP), a group of heterogeneous neurological disorders characterized by severe progressive spasticity of the lower limbs (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

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

Application Methods: Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) is a serine/threonine kinase that regulates cell cycle checkpoints and DNA repair (1). Activation of ATM by autophosphorylation on Ser1981 occurs in response to exposed DNA double stranded breaks. ATM kinase regulates a number of proteins involved in cell cycle checkpoint control, apoptosis, and DNA repair. Known substrates include p53, Chk2, Chk1, CtIP, 4E-BP1, BRCA1, RPA3, H2A.X, SMC1, FANCD2, Rad17, Artemis, Nbs1, and the I-2 regulatory subunit of PP1 (1,2). Mutations in the corresponding ATM gene result in ataxia telangiectasia (AT), an autosomal recessive disease characterized by uncoordinated muscle movement and neurodegeneration. Cells from AT patients display defective DNA damage-induced checkpoint activation, sensitivity to radiation, and a higher frequency of chromosome breakage (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: ATP-citrate lyase (ACL) is a homotetramer that catalyzes the formation of acetyl-CoA and oxaloacetate (OAA) in the cytosol, which is the key step for the biosynthesis of fatty acids, cholesterol and acetylcholine, as well as for glucogenesis (1). Nutrients and hormones regulate the expression level and phosphorylation of ATP-citrate lyase (1,2). It is phosphorylated by GSK-3 on Thr446 and Ser450 (3). Ser455 of ATP-citrate lyase has been reported to be phosphorylated by PKA and Akt (4,5). Phosphorylation on Ser455 abolishes the homotropic allosteric regulation by citrate and enhances the catalytic activity of the enzyme (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Sarcoplasmic and endoplasmic reticulum Ca2+ ATPases (SERCA) are members of a highly conserved family of Ca2+ pumps (1). SERCA pumps transport Ca2+ from the cytosol to the sarcoplasmic and endoplasmic reticulum lumen against a large concentration gradient (1). ATP2A1 (SERCA1) is a fast-twitch, skeletal muscle sarcoplasmic reticulum Ca2+ ATPase (2). Research studies have shown that mutations in the ATP2A1 gene cause an autosomal recessive muscle disorder known as Brody myopathy, which is characterized by muscle cramping and impaired muscle relaxation associated with exercise (1-3).

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

Application Methods: Western Blotting

Background: The ATP2A2 (SERCA2) calcium pump is one of several sarcoplasmic and endoplasmic reticulum Ca2+-ATPases responsible for regulating calcium transport across intracellular membranes (1). Multiple isoforms have been isolated, with ATP2A2a (SERCA2a) found predominantly in the sarcoplasmic reticulum of muscle cells and ATP2A2b (SERCA2b) more ubiquitously expressed in the endoplasmic reticulum of most cell types (2). An isoform containing a truncated carboxy region (ATP2A2c) is expressed in epithelial and hematopoietic cell lines and may be involved in monocyte differentiation (3). Post-translational modification of ATP2A2 (SERCA2), including phosphorylation and tyrosine nitration, modify Ca2+ -ATPase activity and calcium transport (4,5). Mutation in the corresponding ATP2A2 (SERCA2) gene results in Darier disease, a skin disorder characterized by the presence of dark, keratotic papules or rash found on the head and torso (6).

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

Application Methods: Western Blotting

Background: Eukaryotic cells contain ATP-driven proton pumps known as vacuolar H+-ATPases (V-ATPases) that acidify intracellular compartments and translocate protons across the plasma membrane (1,2). Intracellular v-ATPases play an important role in endocytosis and intracellular membrane trafficking, while plasma membrane v-ATPases are important in processes such as urinary acidification and bone resorption (1,2). Vacuolar ATPase enzymes are large, heteromultimeric protein complexes with component proteins found in either the V1 peripheral domain or the V0 integral domain (2). The cytoplasmic V1 domain contains a hexamer of A and B catalytic subunits, as well as a number of other protein subunits required for ATPase assembly and ATP hydrolysis. The integral V0 v-ATPase domain exhibits protein translocase activity and is responsible for transport of protons across the membrane (2). Research studies show that the v-ATPases ATP6V0c, ATP6V0d1, ATP6V1A, ATP6V1B2, and ATP6V1D interact with the Ragulator protein complex and are essential for amino acid induced activation of mTORC1 on the surface of lysosomes (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Eukaryotic cells contain ATP-driven proton pumps known as vacuolar H+-ATPases (V-ATPases) that acidify intracellular compartments and translocate protons across the plasma membrane (1,2). Intracellular v-ATPases play an important role in endocytosis and intracellular membrane trafficking, while plasma membrane v-ATPases are important in processes such as urinary acidification and bone resorption (1,2). Vacuolar ATPase enzymes are large, heteromultimeric protein complexes with component proteins found in either the V1 peripheral domain or the V0 integral domain (2). The cytoplasmic V1 domain contains a hexamer of A and B catalytic subunits, as well as a number of other protein subunits required for ATPase assembly and ATP hydrolysis. The integral V0 v-ATPase domain exhibits protein translocase activity and is responsible for transport of protons across the membrane (2). Research studies show that the v-ATPases ATP6V0c, ATP6V0d1, ATP6V1A, ATP6V1B2, and ATP6V1D interact with the Ragulator protein complex and are essential for amino acid induced activation of mTORC1 on the surface of lysosomes (3).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The ATPase inhibitor factor 1 (ATPIF1) gene encodes a mitochondrial ATPase inhibitor that limits ATP depletion when mitochondrial respiration is impaired (1). ATPIF1 becomes activated following a drop in pH, binding to β-F1-ATPase, thereby inhibiting the hydrolase activity of the H+-ATP synthase (1,2). In addition to its role as an ATP hydrolase, ATPIF1 has also been shown to play a regulatory role in cellular energy metabolism by triggering the induction of aerobic glycolysis in cancer cells resulting in their Warburg phenotype (3,4). Research studies demonstrate that the overexpression of ATPIF1 in several human carcinomas further supports its participation in oncogenesis and provides insight into the altered metabolism of cancer cells, which includes the reprogramming of energetic metabolism toward glycolysis (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ataxia telangiectasia mutated kinase (ATM) and ataxia telangiectasia and Rad3-related kinase (ATR) are PI3 kinase-related kinase (PIKK) family members that phosphorylate multiple substrates on serine or threonine residues that are followed by a glutamine in response to DNA damage or replication blocks (1-3). Despite the essential role of ATR in cell cycle signaling and DNA repair processes, little is known about its activation. ATR was long thought to exist in a constitutively active state in cells, with DNA damage-induced signaling occurring via recruitment of ATR to single stranded DNA and sites of replication stress. Phosphorylation of ATR at serine 428 in response to UV-induced DNA damage has been suggested as a means of activating ATR (4,5). Recent work has shown autophosphorylation of ATR at threonine 1989. Like ATM Ser1981, phosphorylation of ATR Thr1989 occurs in response to DNA damage, indicating that phosphorylation at this site is important in ATR-mediated signaling (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: α-thalassemia/mental retardation X-linked (ATRX) is transcriptional regulator and helicase that belongs to the SNF2 family of chromatin remodeling proteins (1,2). Together with its binding partner death-associated protein 6 (DAXX), ATRX acts as histone chaperone to deposit histone variant H3.3 at repetitive DNA sequences such as telomeric, pericentric, and ribosomal gene repeats (3-6). ATRX is involved in many nuclear functions that ensure proper sister chromatid cohesion during mitosis and chromosome alignment during meiosis (7,8). The ATRX transcriptional regulator also plays a role in the maintenance of telomere integrity and the regulation of gene expression during mammalian development by influencing DNA methylation patterns at high DNA repeat sequences (9,10). Mutations in the corresponding ATRX gene results in ATR-X syndrome, an X-linked disorder characterized by intellectual disabilities, craniofacial abnormalities, and mild α-thalassemia (11,12). Research studies indicate that the loss of ATRX protein occurs in numerous cancers, including pancreatic neuroendocrine tumors (PanNETs) and pediatric glioblastoma, where telomere maintenance occurs independently of telomerase (13-16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: AU-rich element RNA binding protein 1 (AUF1) is also known as heterogeneous ribonucleoprotein D (hnRNP D). AUF1 binds to the AU rich element (ARE) of target mRNA and regulates mRNA decay (1,2). It has a broad range of target genes including IL-1, IL-2, IL-3, Myc, TNF-α, and cyclin D1 (2). Binding of AUF1 to Myc mRNA also affects translation of Myc (3). Recent studies have provided evidence that AUF1 is also involved in the regulation of transcription. AUF1 binds to the promoters of various genes including complement receptor 2 (4), enkephalin (5), and α-fetoprotein (6). AUF1 also binds to the telomerase catalytic subunit Tert promoter and the G-rich telomeric repeat, thus regulating telomere maintenance and normal aging (7,8). AUF1 has four isoforms produced by alternative splicing of a single transcript: p37, p40, p42, and p45 (9,10). All AUF1 isoforms shuttle between the nucleus and cytoplasm (11, 12). These isoforms have distinct localization and bind to different target mRNAs that contribute to the diversity of AUF1 function (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ancient ubiquitous protein 1 (AUP1) is a component of the ER-associated protein degradation (ERAD) machinery responsible for the ubiquitin-mediated degradation of misfolded proteins (1). AUP1 protein contains four conserved domains, with a long, amino-terminal stretch of hydrophobic amino acids followed by an acyltransferase domain (2). Amino-terminal protein sequences direct localization of AUP1 to both the ER and to cytosolic lipid droplets (3). The AUP1 CUE domain binds ubiquitin (4), while the G2BR domain allows for association between AUP1 and E2 conjugating enzyme UBE2G2 (5,6). The presence of these binding domains suggests a central role for AUP1 in the ubiquitination-mediated protein degradation (2). Research studies indicate that AUP1 recruits UBE2G2 to cytosolic lipid droplets, ER-derived organelles that are sites for storage and hydrolysis of neutral lipids. Inhibition of AUP1 protein function results in decreased ubiquitin-mediated degradation of several proteins, including the cholesterol biosynthetic enzyme HMG-CoA-reductase and the cholesterol synthesis regulator INSIG1 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Aurora A (D3E4Q) Rabbit mAb #14475.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Aurora kinases belong to a highly conserved family of mitotic serine/threonine kinases with three members identified among mammals: Aurora A, B, and C (1,2). Studies on the temporal expression pattern and subcellular localization of Aurora kinases in mitotic cells suggest an association with mitotic structure. Aurora kinase functional influences span from G2 phase to cytokinesis and may be involved in key cell cycle events such as centrosome duplication, chromosome bi-orientation and segregation, cleavage furrow positioning, and ingression (3). Aurora A is detected at the centrosomes, along mitotic spindle microtubules, and in the cytoplasm of mitotically proliferating cells. Aurora A protein levels are low during G1 and S phases and peak during the G2/M phase of the cell cycle. Phosphorylation of Aurora A at Thr288 in its catalytic domain increases kinase activity. Aurora A is involved in centrosome separation, maturation, and spindle assembly and stability. Expression of Aurora B protein also peaks during the G2/M phase of the cell cycle; Aurora B kinase activity peaks at the transition from metaphase to the end of mitosis. Aurora B associates with chromosomes during prophase prior to relocalizing to the spindle at anaphase. Aurora B regulates chromosome segregation through the control of microtubule-kinetochore attachment and cytokinesis. Expression of both Aurora A and Aurora B during the G2/M phase transition is tightly coordinated with histone H3 phosphorylation (4,5); research investigators have observed overexpression of these kinases in a variety of human cancers (2,4). Aurora C localizes to the centrosome from anaphase to cytokinesis and both mRNA and protein levels peak during G2/M phase. Although typical Aurora C expression is limited to the testis, research studies report overexpression of Aurora C is detected in various cancer cell lines (6).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Aurora A (AIK) is a cell cycle-regulated Ser/Thr protein kinase that is overexpressed in many tumor cell lines (1-3). Phosphorylation of Aurora A at Thr288 within the kinase activation loop results in a significant increase in its activity and may target the protein for proteasomal degradation during mitosis (4). The closely-related kinase Aurora B (AIM1) has been implicated in multiple mitotic events (5), and siRNA silencing of Aurora B expression results in reduced histone H3 phosphorylation, aberrant chromosome alignment/segregation, and altered survivin localization (6).