1814 Results for: "peptide synthesis"

Supplier: Enzo Life Sciences

EIF-2α, also known as eukaryotic translation initiation factor 2α, promotes the binding of the initiator tRNA to the 40S ribosomal subunits and controls translational rates via phosphorylation/dephosphorylation mechanisms. The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides an important control in the regulation of protein synthesis initiation through the phosphorylation of eIF-2α. Phosphorylated eIF-2α inhibits cell growth and induces apoptosis. Phosphorylation of eIF-2α occurs under a variety of conditions including viral infection, apoptosis, nutrient deprivation, heme-deprivation, and certain stresses. EIF-2 exists as a heterotrimeric protein composed of 3 nonidentical subunits, alpha (36 kDa), beta (38 kDa), and gamma (52 kDa).

Supplier: Rockland Immunochemical

TNFAIP3, also known as A20, is located in chromosome band 6q23, a region that is often deleted in B cell lymphomas. Recently, it was identified as a tumor suppressor gene in Hodgkin lymphoma and several subtypes of non-Hodgkin lymphomas. TNFAIP3 was initially identified as a zinc-finger protein that is rapidly and transiently induced by TNF-a, inhibiting NF-kB-dependent gene expression, and protecting cells from TNF-a-cytotoxicity. Overexpression of TNFAIP3 also inhibits the TLR2- and TLR4-mediated interleukin-8 synthesis in airway epithelial cells, suggesting that TNFAIP3 also acts as a negative regulator of TLR-mediated inflammatory responses, thereby protecting the host against harmful over-responses to pathogens. At least two isoforms of TNFAIP3 are known to exist.

Supplier: Rockland Immunochemical

TNFAIP3, also known as A20, is located in chromosome band 6q23, a region that is often deleted in B cell lymphomas. Recently, it was identified as a tumor suppressor gene in Hodgkin lymphoma and several subtypes of non-Hodgkin lymphomas. TNFAIP3 was initially identified as a zinc-finger protein that is rapidly and transiently induced by TNF-a, inhibiting NF-kB-dependent gene expression, and protecting cells from TNF-a-cytotoxicity. Overexpression of TNFAIP3 also inhibits the TLR2- and TLR4-mediated interleukin-8 synthesis in airway epithelial cells, suggesting that TNFAIP3 also acts as a negative regulator of TLR-mediated inflammatory responses, thereby protecting the host against harmful over-responses to pathogens. At least two isoforms of TNFAIP3 are known to exist.

Supplier: Prosci

ELOVL6 Antibody: Lipogenesis is a key event in the energy storage system and is controlled by the transcription factor sterol regulatory element-binding protein (SREBP)-1. Elongation of very long chain fatty acids protein 6 (ELOVL6) is a member of fatty acyl-CoA elongase gene family that converts palmitic to stearic acid and it has been shown to be a target of SREBP-1, playing an important role in de novo synthesis of long-chain saturated and monosaturated fatty acids in conjunction with fatty acid synthase and stearoyl-CoA desaturase ELOVL6 was predicted to be important for tissue fatty acid composition. Recent studies suggest that inhibition of this elongase could be a new therapeutic approach for ameliorating insulin resistance, diabetes and cardiovascular risks, even in the presence of a continuing state of obesity.

Supplier: Prosci

eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis

Supplier: Bioss

Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.

Supplier: Bioss

Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum.

Supplier: Prosci

SCO2 Antibody: Synthesis of cytochrome c oxidase 2 was initially identified in yeast as one of two cytochrome c oxidase (COX) assembly proteins that enable the assembly of cytochrome c holoenzyme, a complex that catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. Like their yeast homologs, the function of both SCO2 and SCO1 are dependent on copper ion binding. Recent studies suggest that SCO2 expression is regulated by p53, so that a decrease in p53 expression, such as in numerous tumors and cells lines, the drop in SCO2 expression leads to a shift from normal aerobic respiration towards the production of glycolytic ATP. Defects in the SCO2 protein are also associated with fatal infantile cardioencephalomyopathy and COX deficiency.

Supplier: Prosci

Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells.

Supplier: Bioss

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Supplier: Prosci

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. The ribosomal protein is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Prosci

HAAO Antibody: HAAO (3-Hydroxyanthranilate 3, 4-dioxygenase) is a monomeric cytosolic protein of the family of intramolecular dioxygenases containing non-heme ferrous iron. It is widely distributed in peripheral organs, such as liver and kidney, and is present in low amounts in the central nervous system. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron. HAAO catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is mediated by its ability to activate glutamate N-methyl-D-aspartate receptors. Increased cerebral levels of QUIN may participate in the pathogenesis of neurological and inflammatory disorders. HAAO has been suggested to play a role in disorders associated with altered tissue levels of QUIN. Furthermore, recent study shows that HAAO are excellent candidate biomarkers for detecting ovarian cancer.

Supplier: Prosci

This gene, CYP2B6, encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and its expression is induced by phenobarbital. The enzyme is known to metabolize some xenobiotics, such as the anti-cancer drugs cyclophosphamide and ifosphamide. Transcript variants for this gene have been described; however, it has not been resolved whether these transcripts are in fact produced by this gene or by a closely related pseudogene, CYP2B7. Both the gene and the pseudogene are located in the middle of a CYP2A pseudogene found in a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.

Supplier: Prosci

This gene encodes two proteins: sterol carrier protein X (SCPx) and sterol carrier protein 2 (SCP2), as a result of transcription initiation from 2 independently regulated promoters. The transcript initiated from the proximal promoter encodes the longer SCPx protein, and the transcript initiated from the distal promoter encodes the shorter SCP2 protein, with the 2 proteins sharing a common C-terminus. Evidence suggests that the SCPx protein is a peroxisome-associated thiolase that is involved in the oxidation of branched chain fatty acids, while the SCP2 protein is thought to be an intracellular lipid transfer protein. This gene is highly expressed in organs involved in lipid metabolism, and may play a role in Zellweger syndrome, in which cells are deficient in peroxisomes and have impaired bile acid synthesis. Alternative splicing of this gene produces multiple transcript variants, some encoding different isoforms.

Supplier: Prosci

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX50 is a DEAD box enzyme that may be involved in ribosomal RNA synthesis or processing. DDX50 and DDX21, also called RH-II/GuA, have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. DDX50 gene has pseudogenes on chromosomes 2, 3 and 4. Alternative splicing of this gene generates multiple transcript variants, but the full length nature of all the other variants but one has not been defined.

Supplier: Prosci

MAGEA9 is a member of the MAGEA gene family. The members of this family encode proteins with 50 to 80% sequence identity to each other. The promoters and first exons of the MAGEA genes show considerable variability, suggesting that the existence of this gene family enables the same function to be expressed under different transcriptional controls. The MAGEA genes are clustered at chromosomal location Xq28. They have been implicated in some hereditary disorders, such as dyskeratosis congenita. This pseudogene is a member of the cytochrome P450 gene superfamily. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. It is possible that, in rare cases, a combination of two SNPs in this gene may result in an open reading frame encoding a functional enzyme which metabolizes codeine to morphine. This locus is part of a cluster of cytochrome P450 genes on chromosome 22q13.1.

Supplier: Prosci

ATP5B is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). ATP5B is the beta subunit of the catalytic core.This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Prosci

ACSL1 Antibody: Long-chain acyl coenzyme A synthetase 1 (ACSL1) catalyzes the synthesis of acyl-CoA from long-chain fatty acids in an ATP-dependent manner. ACSL1 is a member of a family of long-chain acyl-CoA synthetases which differ in substrate preference, tissue expression, and subcellular localization. In mouse, ASCL1 is the major acyl-CoA enzyme in the heart, providing 60-90% of heart ATP. Loss of ASCL1 either globally or in heart ventricles resulted in impaired fatty acid oxidation, activation of the mammalian target of rapamycin (mTOR), and cardiac hypertrophy.

Supplier: Prosci

SLC35D2 Antibody: The solute carrier family SLC35 consists of at least 17 proteins that act as nucleotide sugar transporters localized to the Golgi apparatus and endoplasmic reticulum. The role of the ER-resident SLC family member SLC35D2 is to transport both UDP-glucuronic acid and UDP-N-acetylgalactosamine. Its overexpression in transfected cells modulated cell surface heparin sulfate expression, suggesting that SLC35D2 is involved in heparin sulfate synthesis. SLC35D2-overexpressing cells also showed increased constitutive and hypotonic stress-stimulated release of UDP-GlcNAc, suggesting that SLC35D2 may be involved in UDP-sugar release and cell signaling.

Supplier: Prosci

The Cpt1 family of proteins are outer mitochondrial membrane proteins that regulate the entry into, and oxidation of fatty acids by, mitochondria. Malonyl-CoA, an intermediate in fatty acid synthesis, has been implicated as a regulatory component of the energy sensing system that feeds into hypothalmic neurons to impart energy homeostasis. Malonyl-CoA levels in the hypothalamus are dynamically regulated by fasting and feeding, altering subsequent feeding behaviour. Cpt1c, the brain-specific carnitine O-palmitoyltransferase 1, is thought to relay information about malonyl-CoA levels in hypothalamic neurons that express orexigenic and anorexigenic neuropeptides that regulate food intake and peripheral energy expenditure. Unlike other Cpt1 proteins, Cpt1c binds Malonyl-CoA but does not catalyse the transfer of the malonyl group from CoA to carnitine.

Supplier: Prosci

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the d subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.

Supplier: Rockland Immunochemical

Synthesis of cytochrome c oxidase 2 was initially identified in yeast as one of two cytochrome c oxidase (COX) assembly proteins that enable the assembly of cytochrome c holoenzyme, a complex that catalyzes the transfer of reducing equivalents from cytochrome c to molecular oxygen and pumps protons across the inner mitochondrial membrane. Like their yeast homologs, the function of both SCO2 and SCO1 are dependent on copper ion binding. Recent studies suggest that SCO2 expression is regulated by p53, so that a decrease in p53 expression, such as in numerous tumors and cells lines, the drop in SCO2 expression leads to a shift from normal aerobic respiration towards the production of glycolytic ATP. Defects in the SCO2 protein are also associated with fatal infantile cardioencephalomyopathy and COX deficiency.

Supplier: Rockland Immunochemical

The sterol regulatory element binding transcription factor 1 (SREBF1) is a transcription factor that binds to the sterol regulatory element-1 (SRE1), which is a decamer flanking the low density lipoprotein receptor gene and some genes involved in sterol biosynthesis (1). The related protein SREBF2 also binds SRE1 and activates transcription in an additive fashion to SREBF1 (2). SREBF1 is synthesized as a precursor that is attached to the nuclear membrane and endoplasmic reticulum. Following cleavage, the mature protein translocates to the nucleus and activates transcription by binding to the SRE1 (3). The SREBF1 proteins are important in the regulation of genes involved in lipid metabolism, while SREBF2 has been more closely associated with cholesterol synthesis and accumulation (4).

Supplier: Bioss

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Supplier: Prosci

PKR Antibody: The interferon-inducible, double-stranded RNA (dsRNA)-dependent protein kinase PKR is a member of the eukaryotic initiation factor-2 alpha (eIF2-alpha) kinase family, possessing serine-threonine kinase activity and two dsRNA-binding motifs that acts as part of the innate immune system. Upon binding dsRNA, PKR undergoes a conformational change leading to its activation and its phosphorylation of the translation factor eIF2, resulting in a general shutdown of protein synthesis and induction of apoptosis through upregulation of caspase-8 and capsase-9 activity in order to prevent the production of more viruses. To evade the antiviral effects of PKR, viruses have evolved multiple mechanisms, such as the inhibition of PKR by the non-structural protein (NS1) of the influenza virus. More recently, PKR has been implicated in several neurodegenerative diseases including Alzheimer, Huntington, and amyotrophic lateral sclerosis.

Supplier: Prosci

Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is a 28S subunit protein that belongs to the ribosomal protein S15P family. The protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the protein is the least conserved among small subunit ribosomal proteins.Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a 28S subunit protein that belongs to the ribosomal protein S15P family. The encoded protein is more than two times the size of its E. coli counterpart, with the 12S rRNA binding sites conserved. Between human and mouse, the encoded protein is the least conserved among small subunit ribosomal proteins. Pseudogenes corresponding to this gene are found on chromosomes 15q and 19q.

Supplier: Prosci

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. They have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. Another difference between mammalian mitoribosomes and prokaryotic ribosomes is that the latter contain a 5S rRNA. Among different species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology. This gene encodes a putative 39S subunit protein and belongs to the L47P ribosomal protein family. Pseudogenes corresponding to this gene are found on chromosomes 2p, 2q, 5p, and 10q.

Supplier: Prosci

Cytoplasmic ribosomes, organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes ribosomal protein S4, a component of the 40S subunit. Ribosomal protein S4 is the only ribosomal protein known to be encoded by more than one gene, namely this gene and ribosomal protein S4, X-linked (RPS4X). The 2 isoforms encoded by these genes are not identical, but are functionally equivalent. Ribosomal protein S4 belongs to the S4E family of ribosomal proteins. It has been suggested that haploinsufficiency of the ribosomal protein S4 genes plays a role in Turner syndrome; however, this hypothesis is controversial. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Rockland Immunochemical

HAAO (3-Hydroxyanthranilate 3, 4-dioxygenase) is a monomeric cytosolic protein of the family of intramolecular dioxygenases containing non-heme ferrous iron. It is widely distributed in peripheral organs, such as liver and kidney, and is present in low amounts in the central nervous system. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron. HAAO catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is mediated by its ability to activate glutamate N-methyl-D-aspartate receptors. Increased cerebral levels of QUIN may participate in the pathogenesis of neurological and inflammatory disorders. HAAO has been suggested to play a role in disorders associated with altered tissue levels of QUIN. Furthermore, recent study shows that HAAO are excellent candidate biomarkers for detecting ovarian cancer.

Supplier: Prosci

ATP5B is a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). ATP5B is the beta subunit of the catalytic core.This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.