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Beschreibung:
IDO catalyses the first and rate-limiting step in the main pathway of human tryptophan catabolism, the kynurenine pathway. Proinflammatory mediators, such as endotoxin and IFN-gamma induce the expression of IDO in several tissues. IDO-dependent suppression of T cell responses might function as natural immunoregulatory mechanism. Physiological IDO activity has been implicated in T cell tolerance to tumours, dysfunctional selftolerance in non-obese diabetic (NOD) mice, and as a protective negative regulator in autoimmune disorders.
Beschreibung:
IRF5 is a member of the interferon regulatory factor (IRF) family, a group of transcription factors with diverse roles, including virus-mediated activation of interferon, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Alternative splice variants encoding different isoforms exist.
Beschreibung:
Nicotinate-Nucleotide Pyrophosphorylase (QPRT) belongs to the nadC/modD family. QPRT plays an improtant role in catabolism of quinolinate which acts as a potent endogenous exitotoxin to neurons. In addition, QPRT serves as an an intermediate in the Tryptophan-Nicotinamide Adenine Dinucleotide pathway. QPRT participates in some pathways including Cofactor biosynthesis, NAD(+) biosynthesis and the Nicotinate D-Ribonucleotide from Quinolinate. In addition, QPRT is involved in the catabolism of Quinolinic Acid (QA). The activity toward QA is slightly repressed by phosphoribosylpyrophosphate (PRPP) in both a competitive and a non-competitive manner.
Beschreibung:
IDO catalyzes the first and rate-limiting step in the main pathway of human tryptophan catabolism, the kynurenine pathway. Proinflammatory mediators, such as endotoxin and IFN-gamma induce the expression of IDO in several tissues. IDO-dependent suppression of T-cell responses might function as natural immunoregulatory mechanism. Physiological IDO activity has been implicated in T-cell tolerance to tumors, dysfunctional selftolerance in non-obese diabetic (NOD) mice, and as a protective negative regulator in autoimmune disorders.
Beschreibung:
Anti-Tryptophan Hydroxylase (Sheep) antibody is suitable for use in Western Blotting and IHC. Specific conditions for reactivity should be optimized by the end user. Expect a band of approximately 55 kDa in size.
Beschreibung:
Preparation Method Produced from 3× crystallised chymotrypsinogen α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology. Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.
Beschreibung:
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA (trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family.Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA (trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. Four transcript variants encoding two different isoforms have been found for this gene.
Beschreibung:
Interferon Regulatory Factor 5 (IRF5) is a member of the IRF family. It contains one IRF tryptophan pentad repeat DNA-binding domain. IRF5 shuttles between the nucleus and the cytoplasm. IRF5 can form homodimer when it is phosphorylated. IRF5 functions as a transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. Genetic variations in IRF5 are associated with susceptibility to systemic lupus erythematosus type 10. In addition, the genetic variations wil result in susceptibility to rheumatoid arthritis.
Beschreibung:
Cysteine-Rich with EGF-Like Domain Protein 2 (CRELD2) is a secreted protein that is a member of the CRELD family. Human CRELD2 is synthesized as a 353 amino acid precursor protein with a signal peptide, a highly conserved domain rich in glutamic acid and tryptophan (WE) and EGF-like repeats. CRELD2 is ubiquitously expressed in many tissues. CRELD2 may interact with CHRNA4 and regulate transport of alpha4- beta 2 neuronal acetylcholine receptor. In addition, CRELD2 could be a novel mediator in regulating the onset and progression of various ER stress-associated diseases.
Beschreibung:
α-Chymotrypsin is a serine peptidase and has 241 amino acid residues contained in three polypeptide chains (A chain-13 residues, B chain-131 residues, and C chain-97 residues) linked by disulfide bridges. Molecular weight of this enzyme is found to be 25 kDa. Its pI is 8,75. It selectively hydrolyses peptide bonds on the C-terminal side of tyrosine, phenylalanine, tryptophan, and leucine. Ca²⁺ activates and stabilizes the enzyme. The enzyme is inhibited by diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), N-p-tosyl-L-phenylalanine chloromethyl ketone (TPCK), chymostatin, aprotinin, α1-antitrypsin, α2-macroglobulin, 10 mM Cu²⁺ and Hg²⁺.A serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met, Leu) on the carboxyl end of the bond.
Beschreibung:
Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. This protein is normally expressed in the dendritic cells, macrophages, microglia, eosinophils, fibroblasts, endothelial cells, and most tumour cells. IDO activity is associated with immunosuppression and immune attenuation. Several studies showed that IDO can contribute to immune escape when expressed directly in tumour cells or when expressed in immunosuppressive antigen presenting cells such as tolerogenic dendritic cells or tumour associated macrophages. IDO also is a promising therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterised by pathological immune suppression.
Beschreibung:
Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.
Beschreibung:
Die BCA-Methode ist ein sehr empfindlicher Proteinnachweis. Peptidbindungen und die vier Aminosäuren Cystein, Cystin, Tryptophan und Tyrosin sollen für die Bestimmung bedeutsam sein. Die Bildung von Cu(I)-Ionen durch Proteine unter alkalischen Bedingungen entspricht dabei der Biuret Bestimmungsmethode. Ein Cu(I)-Ion wird dann durch zwei Moleküle BCA zu einem roten Farbkomplex gebunden. Dieser Komplex kann sehr empfindlich nachgewiesen werden.
Beschreibung:
Glutaryl-CoA Dehydrogenase Mitochondrial (GCDH) is an enzyme that acts upon glutaryl-coenzyme A, creating crotonyl-coenzyme A. It plays a role in the metabolism of lysine, hydroxylysine and tryptophan. It uses electron transfer flavoprotein as its electron acceptor. Isoform Short is inactive Glutaryl-CoA and electron-transfer flavoprotein to (E)-but-2-enoyl-CoA, CO2 and reduced electron-transfer flavoprotein. A defect in this enzyme is associated with neurological condition glutaric acidemia type 1 and cause a progressive form of early-onset generalised dystonia.
Beschreibung:
Indoleamine 2,3-dioxygenase (IDO) is a heme enzyme that initiates the oxidative degradation of the least abundant, essential amino acid, l-tryptophan, along the kynurenine pathway. This protein is normally expressed in the dendritic cells, macrophages, microglia, eosinophils, fibroblasts, endothelial cells, and most tumour cells. IDO activity is associated with immunosuppression and immune attenuation. Several studies showed that IDO can contribute to immune escape when expressed directly in tumour cells or when expressed in immunosuppressive antigen presenting cells such as tolerogenic dendritic cells or tumour associated macrophages. IDO also is a promising therapeutic target for the treatment of cancer, chronic viral infections, and other diseases characterized by pathological immune suppression.
Beschreibung:
Sodium thioglycolate is a commonly used reagent for bacteriological research to maintain reducing conditions in media. Thioglycolate can also protect enzymes against inactivation by maintaining protein thiol groups in the reduced state. Thioglycolate medium is frequently used in inflammation research to elicit a neutrophil and macrophage response in vivo.
Thioglycolic acid protects tryptophan in amino acid analysis,and also mediates formation of ATP from ADP. It lowers the oxidation-reduction potential and neutralises mercurial preservatives. An inhibitor of fatty acid oxidation. An agent that prevents the metabolism of fatty acids and stimulates feeding. The sodium salt form is typically used in production of bacteriological culture media.
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