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Aluminium+oxide+acidic
Catalog Number:
(10427-826)
Supplier:
Bioss
Description:
AARE (Acylamino-acid-releasing enzyme) is also known as Acyl-peptide hydrolase. It catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus corresponding to the protein are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma.
Catalog Number:
(10464-122)
Supplier:
Bioss
Description:
Lipin 1 is a member of the Lipin family of nuclear proteins. This family contains three members: Lipin 1, Lipin 2 and Lipin 3, all of which contain a nuclear signal sequence, a highly conserved amino-terminal (NLIP) domain and a carboxy-terminal (CLIP) domain. LPIN1 (Lipin 1) is crucial for normal adipose tissue development and metabolism. LPIN1 selectively activates a subset of PGC1 alpha target pathways, including fatty acid oxidation and mitochondrial oxidative phosphorylation by inducing expression of the nuclear receptor PPARalpha. LPIN1 also inactivates the lipogenic program and suppresses circulating lipid levels. An abundance of LPIN1 promotes fat accumulation and insulin sensitivity, whereas a deficiency in LPIN1 may deter normal adipose tissue development, resulting in insulin resistance and lipodystrophy, a heterogeneous group of disorders characterized by loss of body fat, fatty liver, hypertriglyceridemia and insulin resistance.
Catalog Number:
(10332-148)
Supplier:
Bioss
Description:
Cytochromes P45 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase.
Catalog Number:
(10103-406)
Supplier:
Prosci
Description:
APEH is the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma.This gene encodes the enzyme acylpeptide hydrolase, which catalyzes the hydrolysis of the terminal acetylated amino acid preferentially from small acetylated peptides. The acetyl amino acid formed by this hydrolase is further processed to acetate and a free amino acid by an aminoacylase. This gene is located within the same region of chromosome 3 (3p21) as the aminoacylase gene, and deletions at this locus are also associated with a decrease in aminoacylase activity. The acylpeptide hydrolase is a homotetrameric protein of 300 kDa with each subunit consisting of 732 amino acid residues. It can play an important role in destroying oxidatively damaged proteins in living cells. Deletions of this gene locus are found in various types of carcinomas, including small cell lung carcinoma and renal cell carcinoma. 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.
Catalog Number:
(10395-184)
Supplier:
Bioss
Description:
12 Lipoxygenase is a non heme iron containing dioxygenase which stereospecifically incorporates molecular oxygen into cis,cis-1,4-pentadiene containing polyunsaturated fatty acids. Murine leukocyte 12 Lipoxygenase oxidizes arachidonic acid to 12(S)-HpETE and 15(S)-HpETE in a ratio of 3:1. Murine leukocyte 12 Lipoxygenase is a 75 kDa protein which is 58% homologous to murine platelet 12 Lipoxygenase, and 70% homologous to porcine leukocyte 12 Lipoxygenase.
Catalog Number:
(10408-588)
Supplier:
Bioss
Description:
Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation.
Catalog Number:
(75832-010)
Supplier:
GLOBAL LIFE SCIENCES SOLUTIONS
Description:
A universal, ultra pure water for your most sensitive research applications.
Catalog Number:
(10752-180)
Supplier:
Prosci
Description:
ME2 is a homotetrameric, mitochondrial NAD-dependent malic enzyme that catalyzes the oxidative decarboxylation of malate to pyruvate. It is related to malic enzyme 1 (ME1), a cytoplasmic NADP-dependent enzyme that generates NADPH for fatty acid biosynthesis. The expression of both malic enzymes is reciprocally regulated by p53; this regulation has been shown to modulate metabolism and senescence. Certain single-nucleotide polymorphism haplotypes of the ME2 gene have been shown to increase the risk for idiopathic generalized epilepsy.
Catalog Number:
(10282-042)
Supplier:
Bioss
Description:
The alcohol dehydrogenase family of proteins metabolize a wide variety of substrates, including retinol, hydroxysteroids, ethanol, aliphatic alcohols and lipid peroxidation products. ADH5 (alcohol dehydrogenase 5 (class III)), also known as FDH (formaldehyde dehydrogenase), ADHX, ADH-3 or GSNOR, is a 374 amino acid cytoplasmic protein that belongs to the class III subfamily of alcohol dehydrogenases. Expressed ubiquitously, ADH5 uses iron as a cofactor to catalytically oxidize both long-chain primary alcohols and S-hydroxymethyl-glutathione, a product formed spontaneously between formaldehyde and glutathione. ADH5 exists as a homodimer and, via its ability to oxidize S-hydroxymethyl-glutathione and, thus, eliminate formaldehyde, functions as an important component of cellular metabolism. Genetic variations in the gene encoding ADH5 may affect drug and alcohol dependence in humans.
Supplier:
Shenandoah Biotechnology
Description:
Leptin is a hormone that is produced by adipose tissue and plays critical roles in the physiologic regulation of body weight. Leptin acts through the leptin receptor (LEPR) to regulate adipose mass by inhibiting hunger and balancing energy usage. Leptin mutations cause severe hereditary obesity and hypogonadism in rodents and humans. Leptin also has thermogenic actions, regulates enzymes of fatty acid oxidation, and is involved in hematopoiesis, angiogenesis, wound healing, inflammation, and immune responses.
Catalog Number:
(10464-126)
Supplier:
Bioss
Description:
Lipin 1 is a member of the Lipin family of nuclear proteins. This family contains three members: Lipin 1, Lipin 2 and Lipin 3, all of which contain a nuclear signal sequence, a highly conserved amino-terminal (NLIP) domain and a carboxy-terminal (CLIP) domain. LPIN1 (Lipin 1) is crucial for normal adipose tissue development and metabolism. LPIN1 selectively activates a subset of PGC1 alpha target pathways, including fatty acid oxidation and mitochondrial oxidative phosphorylation by inducing expression of the nuclear receptor PPARalpha. LPIN1 also inactivates the lipogenic program and suppresses circulating lipid levels. An abundance of LPIN1 promotes fat accumulation and insulin sensitivity, whereas a deficiency in LPIN1 may deter normal adipose tissue development, resulting in insulin resistance and lipodystrophy, a heterogeneous group of disorders characterized by loss of body fat, fatty liver, hypertriglyceridemia and insulin resistance.
Catalog Number:
(76079-638)
Supplier:
Bioss
Description:
ECHS1 (Enoyl Coenzyme A hydratase, short chain, 1) catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs, in the second step of the mitochondrial fatty acid beta-oxidation pathway.
Supplier:
Thermo Scientific Chemicals
Description:
In phosphors for color TV tubes, in microwave filters, and as a stabilizer for high-temperature service materials
Catalog Number:
(10407-316)
Supplier:
Bioss
Description:
The protein encoded by this gene, a member of the carnitine/choline acetyltransferase family, is the rate-controlling enzyme of the long-chain fatty acid beta-oxidation pathway in muscle mitochondria. This enzyme is required for the net transport of long-chain fatty acyl-CoAs from the cytoplasm into the mitochondria. Multiple transcript variants encoding different isoforms have been found for this gene, and read-through transcripts are expressed from the upstream locus that include exons from this gene. [provided by RefSeq, Jun 2009].
Supplier:
MP Biomedicals
Description:
Storage: -20°C, desiccate
This is an ultrapure NAD, chromatographically purified to remove trace inhibitors. β-NAD, a pyridine nucleotide and biologically active form of nicotinic acid, is a coenzyme necessary for the catalytic reaction of certain enzymes. It occurs in living cells primarily in the oxidized state. Serves as a coenzyme of the dehydrogenases, especially in the dehydrogenation of primary and secondary alcohols. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain. Many metabolites and enzymes of biological interest are present in tissues at low concentrations. With the use of β-NAD as a catalyst intermediate and several enzymes in a multistep system, known as enzyme cycling, much greater sensitivity for detection of these components is achieved. The reduced form, β-NADH, is fluorescent whereas β-NAD is not. This difference in fluorescence provides a sensitive fluorescent measurement of the oxidized or reduced pyridine nucleotides at concentrations down to 10-7 M. Electron acceptor. β-NAD is a carrier for hydride ion, forming b-NADH. Hydride ion is enzymatically removed from a substrate molecule by the action of dehydrogenases such as malic dehydrogenase and lactic dehydrogenase. Such enzymes catalyze the reversible transfer of a hydride ion from malate or lactate to b-NAD to form the reduced product, b-NADH. Unlike b-NAD which has no absorbance at 340 nm, b-NADH absorbs at 340 nm (EmM = 6.22). The increase in absorbance at 340 nm with the formation of b-NADH is the basis for measurement of activity of many enzymes.
Catalog Number:
(10297-632)
Supplier:
Bioss
Description:
Glucose Oxidase is a dimeric enzyme that binds to β-D-glucose and aids in its oxidation into D-glucono-1,5-lactone which then hydrolyzes to gluconic acid. Flavin adenine dinucleotide (FAD) is a cofactor to Glucose Oxidase that acts as the initial electron acceptor and is required for this oxidation to occur. Glucose Oxidase is a natural preservative found in honey, where it reduces atmospheric oxygen into hydrogen peroxide which acts as an antibacterial barrier. Glucose Oxidase is also commonly used in biosensors in which it conveys levels of glucose by keeping track of the number of electrons passed through the enzyme. In this application, Glucose Oxidase is connected to an electrode and the resulting charge is measured.
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