Recombinant Human IDO2 Protein (C-6His)

Name: Recombinant Human IDO2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1640NP
Availability: InStock

BL-1640NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Featured immune checkpoint protein molecules, Immune checkpoint proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Indoleamine 2,3-dioxygenase 2 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.
Accession	Q6ZQW0
Synonym	Indoleamine 2,3-dioxygenase 2; Indoleamine 2,3-dioxygenase-like protein 1; Indoleamine-pyrrole 2,3-dioxygenase-like protein 1; IDO2; INDOL1
Gene 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.
Molecular Mass	46.5 KDa
Apmol Mass	45 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 10% Glycerol, 1mM EDTA, 250mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway. Involved in immune regulation. May not play a significant role in tryptophan-related tumoral resistance.
Protein Families	Indoleamine 2,3-dioxygenase family
Database References	HGNC: 27269 OMIM: 612129 KEGG: hsa:169355 STRING: 9606.ENSP00000443432 UniGene: Hs.676257
Tissue Specificity	Detected in liver, small intestine, spleen, placenta, thymus, lung, brain, kidney, and colon. Also expressed at low level in testis and thyroid. Not expressed in the majority of human tumor samples (>99%).

Gene Functions References

This study demonstrated that IDO2 rs10109853 and rs4503083 polymorphisms are not associated with MS risk, age at onset and disease progression in Italian MS patients. PMID: 28477703
High IDO2 expression is associated with Colorectal Cancer. PMID: 27578919
High IDO2 expression is associated with cervical cancer. PMID: 27106797
functional importance of IDO enzymes in human Crohn's disease PMID: 25541686
Human indoleamine 2,3-dioxygenase-2 has substrate specificity and inhibition characteristics distinct from those of indoleamine 2,3-dioxygenase-1 PMID: 24875753
These results demonstrate that IDO2 plays a novel role as a negative regulator of IDO1 by competing for heme-binding with IDO1. PMID: 25394548
The IDO2 is now known to catalyze the first and rate-limiting step in the catabolism of tryptophan along a relative newcomer to the kynurenine pathway field. PMID: 24105077
Multiple-scattering (MS) analysis of EXAFS data on met-indoleamine 2,3-dioxygenase-2 (IDO2) and analysis of XANES have provided the first direct structural information about the axial donor ligands of the iron center for this recently discovered protein. PMID: 24858687
IDO2 is expressed in both mDCs and plasmacytoid DCs and is not modulated by PGE2. IDO2 expression is constitutively, stably expressed in steady-state conditions and may contribute to the homeostatic tolerogenic capacity of DCs. PMID: 24391212
Indoleamine2,3-dioxygenase and tryptophanyl-tRNA synthetase may play critical roles in the immune pathogenesis of chronic kidney disease. PMID: 23651343
Purification and kinetic characterization of human indoleamine 2,3-dioxygenases 1 and 2 (IDO1 and IDO2) and discovery of selective IDO1 inhibitors. PMID: 21835273
Data show that IDO2-specific T cells are cytotoxic effector cells that recognize and kill tumor cells. PMID: 21406395
Tryptophan supplementation was able to completely restore hepatitis b virus replication in IFN-gamma- but not IFN-alpha-treated cells, which strongly argues that IDO is the primary mediator of IFN-gamma-elicited antiviral response in human hepatocytes. PMID: 21084489
High activity of indoleamine 2,3 dioxygenase enzyme predicts disease severity and case fatality in bacteremic patients. PMID: 19487973
The pro-apoptotic activity of indoleamine 2, 3-dioxygenase is responsible for its transcriptional regulation and the modulation of its pro-apoptotic activity during death receptor activation in melanoma cells. PMID: 19799997
First study to report IDO2 expression in pancreatic ductal adenocarcinoma indicating that IDO2 genetic polymorphisms do not negate interferon-gamma-inducible protein expression. PMID: 19476837
IDO2 encodes a novel IDO-related tryptophan catabolic enzyme that is preferentially inhibited by D-1-methyl-tryptophan (D-1MT). IDO2 may have a distinct role in immune tolerance. Two common human genetic polymorphisms ablate IDO2 enzyme activity. PMID: 17671174
This article describes the evolutionary relationships between the INDO and INDOL1 genes. The INDOL1 protein has a distinct expression pattern compared to INDO and both have the ability to catabolise tryptophan. PMID: 17499941

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.