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Product listing: MPC1 (D2L9I) Rabbit mAb, UniProt ID Q9Y5U8 #14462 to PANK4 (D6J4R) Rabbit mAb, UniProt ID Q9NVE7 #12665

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The transport of the glycolytic end product pyruvate into mitochondria and the decarboxylation of pyruvate in the citric acid cycle generate energy through oxidative phosphorylation under aerobic conditions (1,2). Two inner mitochondrial membrane proteins, mitochondrial pyruvate carrier 1 (MPC1) and mitochondrial pyruvate carrier 2 (MPC2), form a 150 kDa complex and are essential proteins in the facilitated transport of pyruvate into mitochondria (1,2). Mutations in the corresponding MPC1 gene are associated with deficient pyruvate transport and may result in lactic acidosis, developmental delay, and premature death (2,3). Altered MPC1/MPC2 expression or activity may result in significant metabolic disorders and contribute to the increase in aerobic glycolysis in cancer cells (a.k.a., the Warburg effect) (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The transport of the glycolytic end product pyruvate into mitochondria and the decarboxylation of pyruvate in the citric acid cycle generate energy through oxidative phosphorylation under aerobic conditions (1,2). Two inner mitochondrial membrane proteins, mitochondrial pyruvate carrier 1 (MPC1) and mitochondrial pyruvate carrier 2 (MPC2), form a 150 kDa complex and are essential proteins in the facilitated transport of pyruvate into mitochondria (1,2). Mutations in the corresponding MPC1 gene are associated with deficient pyruvate transport and may result in lactic acidosis, developmental delay, and premature death (2,3). Altered MPC1/MPC2 expression or activity may result in significant metabolic disorders and contribute to the increase in aerobic glycolysis in cancer cells (a.k.a., the Warburg effect) (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Multidrug resistance-associated protein 1 (MRP1/ABCC1) is a member of the MRP subfamily of ATP-binding cassette (ABC) transporters (1). MRP1/ABCC1 protein functions as an organic anion transporter. It has a broad range of substrates, including antineoplastic or therapeutic agents and the glutathione (GSH) conjugates of these compounds. MRP1/ABCC1 also transports physiological substrates such as folates, GSH and GSH disulfide (GSSG) conjugates of steroids, leukotrienes, and prostaglandins (2,3).Although MRP1/ABCC1 is generally expressed in normal tissue, upregulation of MRP1/ABCC1 has been found in a variety of solid tumors, including small cell lung cancer, breast cancer, and prostate cancer (1,4,5). Research studies show that overexpression of MRP1/ABCC1 facilitates the elimination of therapeutic agents from cancer cells and confers drug resistance in those patients. Research studies also show that elevated expression of MRP1/ABCC1 is a negative prognostic marker for breast cancer and small cell lung cancer, as the level of MRP1/ABCC1 is predictive of the response and toxicity of chemotherapeutic agents in those patients (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Multidrug resistance-associated protein 1 (MRP1/ABCC1) is a member of the MRP subfamily of ATP-binding cassette (ABC) transporters (1). MRP1/ABCC1 protein functions as an organic anion transporter. It has a broad range of substrates, including antineoplastic or therapeutic agents and the glutathione (GSH) conjugates of these compounds. MRP1/ABCC1 also transports physiological substrates such as folates, GSH and GSH disulfide (GSSG) conjugates of steroids, leukotrienes, and prostaglandins (2,3).Although MRP1/ABCC1 is generally expressed in normal tissue, upregulation of MRP1/ABCC1 has been found in a variety of solid tumors, including small cell lung cancer, breast cancer, and prostate cancer (1,4,5). Research studies show that overexpression of MRP1/ABCC1 facilitates the elimination of therapeutic agents from cancer cells and confers drug resistance in those patients. Research studies also show that elevated expression of MRP1/ABCC1 is a negative prognostic marker for breast cancer and small cell lung cancer, as the level of MRP1/ABCC1 is predictive of the response and toxicity of chemotherapeutic agents in those patients (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Multi-drug resistance protein 2 (MRP2), also known as cMRP, cMOAT, and ABCC2, is an ATP binding cassette (ABC) transporter and part of the multi-drug resistance (MRP) family (1,2). The MRP proteins are membrane proteins that function as organic anion pumps involved in the cellular removal of cancer drugs (2). MRP2 is associated with resistance to a number of cancer drugs, such as cisplatin, etoposide, doxorubicin, and methotrexate (3-5). MRP2 is predominately expressed on the apical membranes in the liver (6-9) and kidney proximal tubules (10). It is responsible for the ATP-dependent secretion of bilirubin glucuronides and other organic anions from hepatocytes into the bile, a process important for the excretion of endogenous and xenobiotic substances. Loss of MRP2 activity is the cause of Dubin-Johnson syndrome, an autosomal recessive disorder characterized by defects in the secretion of anionic conjugates and the presence of melanin like pigments in hepatocytes (11-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MRP3/ABCC3 belongs to the super family of ATP-binding cassette (ABC) transporters. It is a member of the MRP subfamily that is expressed in various organs including liver, gallbladder, small intestine, colon, kidney, and adrenal gland (1-3). MRP3 is involved in multi-drug resistance (1). It facilitates the efflux of organic anions including monoanionic bile acid and anti-cancer reagents such as etoposide and paclitaxel from liver and small intestine into blood (4-7). Expression of MRP3 is increased in the cholestatic human and rat liver, suggesting its role in cholehepatic and enterohepatic bile circulation and in protecting liver from toxic bile salts (2,8). MRP3 expression is also upregulated in people with Dubin-Johnson Syndrome (DJS) who lack functional MRP2 in the liver, which implicates the compensatory role of MRP3 in the absence of functional MRP2 (4).Elevated expression of MRP3 has been detected in various cancer types such as hepatocellular carcinomas, primary ovarian cancer, and adult acute lymphoblastic leukemia (ALL) (9-11). Overexpression of MRP3 was reported to be a prognostic factor in ALL and adult acute myeloid leukemia (AML) (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: ABCC4 is a member of the ATP-binding Cassette (ABC) transporter family. ABC proteins transport various molecules across cellular membranes by utilizing the energy generated from ATP hydrolysis. There are seven subfamilies of ABC proteins: ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White (1). ABCC4 belongs to the MRP subfamily, which is involved in multi-drug resistance, hence it is also named MRP4. ABCC4 is widely expressed in tissues including prostate, kidney proximal tubules, astrocytes and capillary endothelial cells of the brain, platelets, and many cancer cell lines (2-4). ABCC4 mediates efflux transport of a wide variety of endogenous and xenobiotic organic anionic compounds (5). The diversity of substrates determines the biological functions of ABCC4. It regulates cAMP levels in human leukemia cells, thereby controlling the proliferation and differentiation of leukemia cells (6). ABCC4 also enables COX deficient pancreatic cancer cells to obtain exogenous prostaglandins (7). Research studies have shown that ABCC4 expression is elevated in drug resistant cancer cells, which makes it a potential target for cancer therapy (8,9). ABCC4 localizes to both plasma membrane and intracellular membranous structures (10). Investigators have also implicated ABCC4 in the pathogenesis of Kawasaki disease, a childhood genetic disorder characterized by vasculitis (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: ABCC4 is a member of the ATP-binding Cassette (ABC) transporter family. ABC proteins transport various molecules across cellular membranes by utilizing the energy generated from ATP hydrolysis. There are seven subfamilies of ABC proteins: ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, and White (1). ABCC4 belongs to the MRP subfamily, which is involved in multi-drug resistance, hence it is also named MRP4. ABCC4 is widely expressed in tissues including prostate, kidney proximal tubules, astrocytes and capillary endothelial cells of the brain, platelets, and many cancer cell lines (2-4). ABCC4 mediates efflux transport of a wide variety of endogenous and xenobiotic organic anionic compounds (5). The diversity of substrates determines the biological functions of ABCC4. It regulates cAMP levels in human leukemia cells, thereby controlling the proliferation and differentiation of leukemia cells (6). ABCC4 also enables COX deficient pancreatic cancer cells to obtain exogenous prostaglandins (7). Research studies have shown that ABCC4 expression is elevated in drug resistant cancer cells, which makes it a potential target for cancer therapy (8,9). ABCC4 localizes to both plasma membrane and intracellular membranous structures (10). Investigators have also implicated ABCC4 in the pathogenesis of Kawasaki disease, a childhood genetic disorder characterized by vasculitis (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: MTAP is an enzyme that is essential for the salvage pathway for both adenine and methionine synthesis. MTAP catalyzes the cleavage of 5’-methylthioadenosine into adenine and 5-methylthio-D-ribose-1-phosphate. Adenine is then used to generate AMP whereas 5-methylthio-D-ribose-1-phosphate is converted into methionine (1,2). MTAP is expressed in all normal cells and tissues, although frequently lost in different human tumors including pancreatic adenocarcinoma, neuroendocrine tumors, non-small cell lung carcinoma and breast carcinoma. MTAP is usually codeleted with p16 (cdkN2a/ARF) (3-5). MTAP overexpression in breast cancer cells inhibits their ability to form colonies in soft agar, thereby implicating its function as a tumor suppressor (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Methylenetetrahydrofolate reductase (MTHFR), a key enzyme in one-carbon metabolism, catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. 5-methyltetrahydrofolate donates its methyl group for remethylation of homocysteine to methionine. Methionine is further converted to S-adenosylmethionine (SAM), a major reactive methyl carrier. DNA methyltransferases and histone methyltransferases use SAM to methylate DNA and histones with concomitant conversion of SAM to S-adenosylhomocysteine (SAH) (1, 2). In addition, MTHFR is inhibited by SAM and this feedback inhibition is partially reduced by SAH (3). Metabolically regulated levels of SAM and SAM/SAH ratio are shown to predict histone methylation levels, indicating the important role of enzymes in one-carbon metabolism including MTHFR in determining histone methylation status (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Myoglobin (MB) is an oxygen-binding protein that contains one polypeptide chain and one heme group. It is expressed in vertebrate skeletal and cardiac muscles where it plays an essential role in the storage and transport of oxygen to mitochondria. Reversible oxygen binding occurs by a linkage with the imidazole nitrogen of the 91st histidine residue in the myoglobin chain. Research studies indicate that the blockade of myoglobin in isolated cardiac myocytes mimics hypoxia when electrically stimulated for paced contractions (1). During fetal development, myoglobin is required to support cardiac function (2). Diving mammals are known to have high concentrations of myoglobin in their blood, which may contribute to their ability to endure long periods of oxygen deprivation during deep dives (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The sodium-dependent phosphate transport protein 2B (NaPi-2b, SLC34A2) is a sodium dependent inorganic phosphate (Pi) transporter that regulates phosphate homeostasis in various organs, including the small intestine, lung, liver, and testis (1). In the small intestine, NaPi-2b localizes to the intestinal brush border membrane to mediate Pi reabsorption (2). In the lung, NaPi-2b is expressed in the apical membrane of type II alveolar cells and is involved in the synthesis of surfactant (3). Mutations in the corresponding SLC34A2 gene causes pulmonary alveolar microlithiasis, a rare autosomal recessive disorder characterized by the deposition of calcium phosphate microliths throughout the lungs (4). Research studies show aberrant expression of NaPi-2b in various type of cancer, including ovarian, breast, and lung cancer (5). Chromosomal rearrangements involving SLC34A2-ROS1 are seen in gastric carcinoma and non-small cell lung cancer and result in the formation of a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase activity (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The sodium-dependent phosphate transport protein 2B (NaPi-2b, SLC34A2) is a sodium dependent inorganic phosphate (Pi) transporter that regulates phosphate homeostasis in various organs, including the small intestine, lung, liver, and testis (1). In the small intestine, NaPi-2b localizes to the intestinal brush border membrane to mediate Pi reabsorption (2). In the lung, NaPi-2b is expressed in the apical membrane of type II alveolar cells and is involved in the synthesis of surfactant (3). Mutations in the corresponding SLC34A2 gene causes pulmonary alveolar microlithiasis, a rare autosomal recessive disorder characterized by the deposition of calcium phosphate microliths throughout the lungs (4). Research studies show aberrant expression of NaPi-2b in various type of cancer, including ovarian, breast, and lung cancer (5). Chromosomal rearrangements involving SLC34A2-ROS1 are seen in gastric carcinoma and non-small cell lung cancer and result in the formation of a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase activity (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The homeodomain protein NKX6.1 is a transcription factor that regulates pancreatic β-cell development (1). Overexpressed NKX6.1 stimulates rat pancreatic β-cell proliferation and increases glucose-stimulated insulin secretion (GSIS) (2). The effect on GSIS was shown to be mediated by the up-regulation of prohormone VGF expression and the subsequent potentiation by TLQP-21, a peptide derived from VGF (3). Both nuclear receptors Nr4a1 and Nr4a3 are essential for pancreatic β-cell proliferation driven by overexpressed NKX6.1 (4). In addition, studies suggest that NKX6.1 is a suppressor for epithelial-to-mesenchymal transition (EMT), leading to inhibition of tumor metastasis (5).

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

Application Methods: Western Blotting

Background: The NDK/NME/NM23 kinase family (encoded by the NME gene family) consists of at least eight distinct proteins that exhibit different cellular localization (1). Members of this group inhibit metastasis in a variety of tumor cell types (2). All NDK/NME/NM23 proteins possess nucleoside diphosphatase kinase (NDK) activity and catalyze the phosphorylation of nucleoside diphosphate to the corresponding nucleoside triphosphate to regulate a diverse array of cellular events (3). At least four classes of NDK biochemical activities have been described, including protein-protein interactions (4-6), regulation of GTP-binding protein function (7-9), DNA-associated activities (10,11), and histidine-dependent protein phosphotransferase activity (12). NDK/NME proteins participate in the regulation of a broad spectrum of cellular responses, including development, differentiation, proliferation, endocytosis, and apoptosis (13). Because of its role in metastasis suppression and oncogenesis, NDKA (NME1/NM23-H1) has been widely studied (14). NDKA (NM23-H1) and NDKB (NM23-H2) are encoded by adjacent NME1 and NME2 genes and share 90% sequence identity. Two serine residues (Ser122 and Ser144) on NDKA/NM23-H1 can be phosphorylated by AMPKα1, but only phosphorylation at Ser122 determines whether NDKA channels ATP to AMPKα1. This regulates AMPKα1 activity towards ACC1, an important regulator of fatty acid metabolism (15). Mutation of NDKB/NM23-H2 at Ser122 (S122P) in melanoma cells results in altered phosphoryl transfer activity (16).

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

Application Methods: Western Blotting

Background: The NDK/NME/NM23 kinase family (encoded by the NME gene family) consists of at least eight distinct proteins that exhibit different cellular localization (1). Members of this group inhibit metastasis in a variety of tumor cell types (2). All NDK/NME/NM23 proteins possess nucleoside diphosphatase kinase (NDK) activity and catalyze the phosphorylation of nucleoside diphosphate to the corresponding nucleoside triphosphate to regulate a diverse array of cellular events (3). At least four classes of NDK biochemical activities have been described, including protein-protein interactions (4-6), regulation of GTP-binding protein function (7-9), DNA-associated activities (10,11), and histidine-dependent protein phosphotransferase activity (12). NDK/NME proteins participate in the regulation of a broad spectrum of cellular responses, including development, differentiation, proliferation, endocytosis, and apoptosis (13). Because of its role in metastasis suppression and oncogenesis, NDKA (NME1/NM23-H1) has been widely studied (14). NDKA (NM23-H1) and NDKB (NM23-H2) are encoded by adjacent NME1 and NME2 genes and share 90% sequence identity. Two serine residues (Ser122 and Ser144) on NDKA/NM23-H1 can be phosphorylated by AMPKα1, but only phosphorylation at Ser122 determines whether NDKA channels ATP to AMPKα1. This regulates AMPKα1 activity towards ACC1, an important regulator of fatty acid metabolism (15). Mutation of NDKB/NM23-H2 at Ser122 (S122P) in melanoma cells results in altered phosphoryl transfer activity (16).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: NAD(P)H:quinone oxidoreductase 1 (NQO1) is a flavoprotein that catalyzes the two-electron reduction of quinones and their derivatives (1,2). This enzyme protects cells against redox cycling and oxidative stress (1,3). The expression of NQO1 is increased in liver, colon and breast tumors and non-small cell lung cancer (NSCLC) compared with the normal tissues (1,2). Moreover, expression levels are also elevated in developing tumors, suggesting a role for NQO1 in the prevention of tumor development (1). Studies on NQO1 knockout mice suggest that the lack of NQO1 enzymatic activity changes intracellular redox states resulting in a reduction in apoptosis, which in turn leads to myeloid hyperplasia of bone marrow (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: NAD(P)H:quinone oxidoreductase 1 (NQO1) is a flavoprotein that catalyzes the two-electron reduction of quinones and their derivatives (1,2). This enzyme protects cells against redox cycling and oxidative stress (1,3). The expression of NQO1 is increased in liver, colon and breast tumors and non-small cell lung cancer (NSCLC) compared with the normal tissues (1,2). Moreover, expression levels are also elevated in developing tumors, suggesting a role for NQO1 in the prevention of tumor development (1). Studies on NQO1 knockout mice suggest that the lack of NQO1 enzymatic activity changes intracellular redox states resulting in a reduction in apoptosis, which in turn leads to myeloid hyperplasia of bone marrow (2).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Nuclear respiratory factor 1 (NRF1) was identified as a transcription activator for the gene encoding cytochrome c (1). It was later found to play a role in the nuclear control of mitochondrial function (1). PGC-1 induces the expression of NRF1 and NRF2 (2). NRF1, along with the coactivator PGC-1, stimulates the promoter of mitochondrial transcription factor A, which regulates mitochondrial biogenensis and function (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear respiratory factor 1 (NRF1) was identified as a transcription activator for the gene encoding cytochrome c (1). It was later found to play a role in the nuclear control of mitochondrial function (1). PGC-1 induces the expression of NRF1 and NRF2 (2). NRF1, along with the coactivator PGC-1, stimulates the promoter of mitochondrial transcription factor A, which regulates mitochondrial biogenensis and function (2).

$283
100 µl
APPLICATIONS
REACTIVITY
All Species Expected, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: A distinct form of protein glycosylation, beta-linked N-acetyl-glucosamine (GlcNAc) moieties can be added to serine or threonine residues of proteins (1,2). This differs from other forms of glycosylation, as it typically is a single moiety rather than the complex branched sugars that are more commonly studied. It is thought that these modifications happen in a much more dynamic cycle more reminiscent of phosphorylation modifications (3). GlcNAc modified proteins are found in the cytoplasm and nucleus and are modulated by means of specific O-GlcNAc transferases (OGT) as well as GlcNAcase activity that can be inhibited using the Thiamet-G (TMG) inhibitor. Mass spectrometry analysis of this modification has been complicated due to the loss of the GlcNAc group during ionization and fragmentation, but methods and technologies such as electron transfer dissociation (ETD) are opening up new avenues to study these modifications. O-GlcNAc could play an important role in many cellular processes, including metabolism, growth, morphogenesis, apoptosis, transcription, and it may play a critical role in cancer.(4)

$303
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 O-GlcNAc (CTD110.6) Mouse mAb #9875.
APPLICATIONS
REACTIVITY
All Species Expected, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: A distinct form of protein glycosylation, beta-linked N-acetyl-glucosamine (GlcNAc) moieties can be added to serine or threonine residues of proteins (1,2). This differs from other forms of glycosylation, as it typically is a single moiety rather than the complex branched sugars that are more commonly studied. It is thought that these modifications happen in a much more dynamic cycle more reminiscent of phosphorylation modifications (3). GlcNAc modified proteins are found in the cytoplasm and nucleus and are modulated by means of specific O-GlcNAc transferases (OGT) as well as GlcNAcase activity that can be inhibited using the Thiamet-G (TMG) inhibitor. Mass spectrometry analysis of this modification has been complicated due to the loss of the GlcNAc group during ionization and fragmentation, but methods and technologies such as electron transfer dissociation (ETD) are opening up new avenues to study these modifications. O-GlcNAc could play an important role in many cellular processes, including metabolism, growth, morphogenesis, apoptosis, transcription, and it may play a critical role in cancer.(4)

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

Application Methods: Immunoprecipitation, Western Blotting

Background: 2-oxoglutarate dehydrogenase (OGDH) is one of three enzymes in the α ketoglutarate dehydrogenase complex (OGDC) that is responsible for catalyzing a rate-regulating step of the tricarboxylic acid (Krebs) cycle. Together with dihydrolipoamide S-succinyltransferase (DLST) and dihydrolipoamide dehydrogenase (DLD), OGDH helps to convert 2-oxoglutarate to succinyl-CoA and CO2 within eukaryotic mitochondria (1). Regulation of this enzyme complex is important for mitochondrial energy metabolism within cells (2). Research studies indicate that OGDH activity within the mitochondrial matrix is regulated by multiple factors, including calcium, the adenine nucleotides ATP and ADP, and NADH (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: O-GlcNAcylation is a post-translational modification where β-D-N-acetylglucosamine (GlcNAc) is covalently linked to cytoplasmic and nuclear proteins at serine or threonine residues (1,2). This modification is important in many cellular processes including metabolism, cell growth and morphogenesis, apoptosis, and transcription (2,3), and research studies have implicated this modification in cancer (1). The reversible protein modification by O-GlcNAc, which has been suggested to be a nutrient and stress sensor, is catalyzed by two highly conserved enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) (4).

$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 OGT (D1D8Q) Rabbit mAb #24083.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: O-GlcNAcylation is a post-translational modification where β-D-N-acetylglucosamine (GlcNAc) is covalently linked to cytoplasmic and nuclear proteins at serine or threonine residues (1,2). This modification is important in many cellular processes including metabolism, cell growth and morphogenesis, apoptosis, and transcription (2,3), and research studies have implicated this modification in cancer (1). The reversible protein modification by O-GlcNAc, which has been suggested to be a nutrient and stress sensor, is catalyzed by two highly conserved enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Changes in mitochondrial dynamics regulated by environmental cues affect mitochondrial size and shape and have been shown to dramatically impact mitochondrial metabolism, apoptosis, and autophagy (1). These processes are largely controlled by mitochondrial dynamin-related GTPases, including mitofusin-1, mitofusin-2, OPA1, and DRP1. DRP1 regulates mitochondrial fission, while the mitofusins and OPA1 control fusion at the outer and inner mitochondrial membrane, respectively.OPA1, or Optic Atrophy 1, was originally identified as a genetic cause for Autosomal Dominant Optic Atrophy, a neuropathy resulting in progressive visual loss (2,3). OPA1 is a widely expressed protein localized to the inner mitochondrial membrane, which regulates mitochondrial fusion and cristae morphology and protects against apoptosis (4-6). OPA1 activity is tightly regulated through alternative splicing and post-translational modifications including complex proteolytic processing by multiple proteases (7-12). In addition, OPA1 expression can be induced under conditions of metabolic demand through a pathway involving Parkin induced NF-κB activation (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Changes in mitochondrial dynamics regulated by environmental cues affect mitochondrial size and shape and have been shown to dramatically impact mitochondrial metabolism, apoptosis, and autophagy (1). These processes are largely controlled by mitochondrial dynamin-related GTPases, including mitofusin-1, mitofusin-2, OPA1, and DRP1. DRP1 regulates mitochondrial fission, while the mitofusins and OPA1 control fusion at the outer and inner mitochondrial membrane, respectively.OPA1, or Optic Atrophy 1, was originally identified as a genetic cause for Autosomal Dominant Optic Atrophy, a neuropathy resulting in progressive visual loss (2,3). OPA1 is a widely expressed protein localized to the inner mitochondrial membrane, which regulates mitochondrial fusion and cristae morphology and protects against apoptosis (4-6). OPA1 activity is tightly regulated through alternative splicing and post-translational modifications including complex proteolytic processing by multiple proteases (7-12). In addition, OPA1 expression can be induced under conditions of metabolic demand through a pathway involving Parkin induced NF-κB activation (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Pantothenate kinase 1 (PANK1) is the rate-limiting enzyme in coenzyme A (CoA) synthesis (1,2). PPARα -mediated transcriptional regulation of PANK1 plays an important role in controlling CoA levels in hepatocytes (1). Research studies indicate that PANK1 expression, along with microRNA-107, decreases in a murine macrophage model upon lipopolysaccharide (LPS) exposure in a PPARα-dependent manner (3). Additional studies show that the corresponding PANK1 gene is a direct target of tumor suppressor p53 and that p53 regulates energy homeostasis through control of PANK1 expression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: PANK2, pantothenate kinase 2, catalyzes the first step in CoA biosynthesis (1,2). Human PANK2 is located in the mitochondria, and research studies have shown some mutations in human PANK2 are linked to neurodegeneration (2). Alternatively, mouse PANK2 localizes in the cytosol, and defective PANK2 in mice leads to retinal degeneration (1,3).

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

Application Methods: Western Blotting

Background: Panthothenate kinase (PANK) is an enzyme that is responsible for catalyzing the first step in coenzyme A (CoA) synthesis (1-4). There are four human PANK genes (PANK1-4) (1-4). PANK4 is ubiquitously expressed, but higher expression levels are observed in muscle (1,2). PANK4 expression is elevated in rat skeletal muscle under high glucose conditions (2). There is evidence that rat PANK4 colocalizes with pyruvate kinase M2 (PKM2) in vitro (2). PANK4 may also play a protective role in beta-cell apoptosis by lowering the levels of pro-caspase-9 (3). Research studies have shown that mutations in the PANK2 gene are associated with Neurodegeneration with Brain Iron Accumulation (NBIA), formerly known as Hallervorden-Spatz syndrome (1,4). Expression of hPANK4 in a Drosophila model of NBIA rescues the phenotype with the exception of infertility (4).