IDO2 recombinant protein
Recombinant Human IDO2 Protein (C-His)
Purity
>95% as determined by reducing SDS-PAGE.
Synonyms
IDO2; Recombinant Human IDO2 Protein (C-His); INDOL1; IDO2 recombinant protein
Host
E Coli
Purity/Purification
>95% as determined by reducing SDS-PAGE.
Form/Format
Supplied as a 0.2 mum filtered solution of 20mM Tris, 10% Glycerol, 1mMEDTA, 250mM NaCl, pH8.0.
Sequence
Met14-Gly420
Sequence Length
407
Species
Human
Endotoxin
< 1.0 EU per mug as determined by the LAL method.
Fusion Tag
C-His
Preparation and Storage
Store at < -20 degree C, stable for 6 months. Please minimize freeze-thaw cycles.
Related Product Information for IDO2 recombinant protein
Protein Construction: Recombinant Human IDO2 is produced by our E Coli expression system and the target gene encoding Met14-Gly420 is expressed with a 6His tag at the C-terminus.
Background: Indoleamine 2,3-dioxygenase-like protein 1(IDO2) belongs to the indoleamine 2,3-dioxygenase family. IDO2 can be detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. It also expressed at low level in testis and thyroid but not expressed in the majority of human tumor samples. IDO2 catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. It involved in immune regulation. IDO1 and IDO2 are 2 distinct enzymes which catalyze the same reaction. IDO2 affinity for tryptophan is much lower than that of IDO1. 50 % of Caucasians harbor polymorphisms which abolish IDO2 enzymatic activity. IDO2 is expressed in human tumors in an inactive form: tryptophan degradation is entirely provided by IDO1 in these cells. IDO2 may play a role as a negative regulator of IDO1 by competing for heme-binding with IDO1. Low efficiency IDO2 enzymes have been conserved throughout vertebrate evolution, whereas higher efficiency IDO1 enzymes are dispensable in many lower vertebrate lineages. IDO1 may have arisen by gene duplication of a more ancient proto-IDO gene before the divergence of marsupial and eutherian (placental) mammals.
Background: Indoleamine 2,3-dioxygenase-like protein 1(IDO2) belongs to the indoleamine 2,3-dioxygenase family. IDO2 can be detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. It also expressed at low level in testis and thyroid but not expressed in the majority of human tumor samples. IDO2 catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. It involved in immune regulation. IDO1 and IDO2 are 2 distinct enzymes which catalyze the same reaction. IDO2 affinity for tryptophan is much lower than that of IDO1. 50 % of Caucasians harbor polymorphisms which abolish IDO2 enzymatic activity. IDO2 is expressed in human tumors in an inactive form: tryptophan degradation is entirely provided by IDO1 in these cells. IDO2 may play a role as a negative regulator of IDO1 by competing for heme-binding with IDO1. Low efficiency IDO2 enzymes have been conserved throughout vertebrate evolution, whereas higher efficiency IDO1 enzymes are dispensable in many lower vertebrate lineages. IDO1 may have arisen by gene duplication of a more ancient proto-IDO gene before the divergence of marsupial and eutherian (placental) mammals.
NCBI and Uniprot Product Information
NCBI GI #
UniProt Accession #
Molecular Weight
Molecular Mass: 46.5kDa
Actual Protein Molecular Mass: 45kDa
Actual Protein Molecular Mass: 45kDa
NCBI Official Full Name
Indoleamine 2,3-dioxygenase 2
UniProt Protein Name
Indoleamine 2,3-dioxygenase 2
Protein Family
UniProt Gene Name
IDO2
UniProt Synonym Gene Names
INDOL1; IDO-2
UniProt Entry Name
I23O2_HUMAN
Uniprot Description
INDOL1: Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism. Belongs to the indoleamine 2,3-dioxygenase family. 2 isoforms of the human protein are produced by alternative splicing.
Protein type: Amino Acid Metabolism - tryptophan; Oxidoreductase; EC 1.13.11.-
Chromosomal Location of Human Ortholog: 8p11.21
Cellular Component: cytoplasm; cytosol
Molecular Function: metal ion binding; heme binding; indoleamine 2,3-dioxygenase activity; tryptophan 2,3-dioxygenase activity
Biological Process: tryptophan catabolic process to kynurenine; tryptophan catabolic process
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Product Notes
The IDO2 ido2 (Catalog #AAA2557255) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The amino acid sequence is listed below: Met14-Gly4 20. It is sometimes possible for the material contained within the vial of "IDO2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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