Recombinant Human Indoleamine 2,3-Dioxygenase 2 (IDO2) Protein (His)

Name: Recombinant Human Indoleamine 2,3-Dioxygenase 2 (IDO2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-11050P
Availability: InStock

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 (IDO2) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q6ZQW0
Target Symbol	IDO2
Synonyms	3-dioxygenase 2; 3-dioxygenase-like protein 1; EC 1.13.11.; I23O2_HUMAN; IDO 2; IDO-2; Ido2; INDOL 1; Indoleamine 2; Indoleamine 2,3 dioxygenase 2; Indoleamine 2,3 dioxygenase like 1 protein ; Indoleamine 2,3 dioxygenase like protein 1; Indoleamine pyrrole 2,3 dioxygenase like 1; Indoleamine pyrrole 2,3 dioxygenase like protein 1; Indoleamine-pyrrole 2
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQAHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSRNLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVPGIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSGWKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYMPPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAAKAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG
Expression Range	14-420aa
Protein Length	Partial
Mol. Weight	46.6
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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.