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Rat Anti-IDO1 Recombinant Antibody (mIDO-48) (CBMAB-I0872-YY)

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Basic Information

Host Animal
Rat
Clone
mIDO-48
Application
WB, IHC-P, IHC-Fr
Specificity
Human, Mouse
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

Target

Full Name
Indoleamine 2,3-Dioxygenase 1
Introduction
This gene encodes indoleamine 2,3-dioxygenase (IDO) - a heme enzyme that catalyzes the first and rate-limiting step in tryptophan catabolism to N-formyl-kynurenine. This enzyme acts on multiple tryptophan substrates including D-tryptophan, L-tryptophan, 5-hydroxy-tryptophan, tryptamine, and serotonin. This enzyme is thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation, and antioxidant activity. Through its expression in dendritic cells, monocytes, and macrophages this enzyme modulates T-cell behavior by its peri-cellular catabolization of the essential amino acid tryptophan.
Entrez Gene ID
Human3620
Mouse15930
UniProt ID
HumanP14902
MouseP28776
Alternative Names
Indoleamine 2,3-Dioxygenase 1
Function
Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174).

Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses (PubMed:25691885).

Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells (PubMed:25691885).

Acts as a suppressor of anti-tumor immunity (PubMed:23103127, PubMed:25157255, PubMed:14502282, PubMed:25691885).

Limits the growth of intracellular pathogens by depriving tryptophan (PubMed:25691885).

Protects the fetus from maternal immune rejection (PubMed:25691885).
Biological Process
de novo' NAD biosynthetic process from tryptophan Source: GO_Central
Female pregnancy Source: ProtInc
Immune system process Source: UniProtKB-KW
Inflammatory response Source: Ensembl
Kynurenic acid biosynthetic process Source: Ensembl
Multicellular organismal response to stress Source: Ensembl
Negative regulation of interleukin-10 production Source: Ensembl
Negative regulation of T cell apoptotic process Source: Ensembl
Negative regulation of T cell proliferation Source: Ensembl
Positive regulation of chronic inflammatory response Source: Ensembl
Positive regulation of interleukin-12 production Source: Ensembl
Positive regulation of T cell apoptotic process Source: UniProtKB
Positive regulation of T cell tolerance induction Source: Ensembl
Positive regulation of type 2 immune response Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Swimming behavior Source: Ensembl
Tryptophan catabolic process Source: ProtInc
Tryptophan catabolic process to kynurenine Source: GO_Central
Cellular Location
Cytosol

Salminen, A. (2022). Role of indoleamine 2, 3-dioxygenase 1 (IDO1) and kynurenine pathway in the regulation of the aging process. Ageing Research Reviews, 75, 101573.

Pallotta, M. T., Rossini, S., Suvieri, C., Coletti, A., Orabona, C., Macchiarulo, A., ... & Grohmann, U. (2022). Indoleamine 2, 3‐dioxygenase 1 (IDO1): an up‐to‐date overview of an eclectic immunoregulatory enzyme. The FEBS journal, 289(20), 6099-6118.

Fujiwara, Y., Kato, S., Nesline, M. K., Conroy, J. M., DePietro, P., Pabla, S., & Kurzrock, R. (2022). Indoleamine 2, 3-dioxygenase (IDO) inhibitors and cancer immunotherapy. Cancer Treatment Reviews, 102461.

Zhang, Y., Hu, Z., Zhang, J., Ren, C., & Wang, Y. (2022). Dual-target inhibitors of indoleamine 2, 3 dioxygenase 1 (Ido1): A promising direction in cancer immunotherapy. European Journal of Medicinal Chemistry, 238, 114524.

Tang, K., Wu, Y. H., Song, Y., & Yu, B. (2021). Indoleamine 2, 3-dioxygenase 1 (IDO1) inhibitors in clinical trials for cancer immunotherapy. Journal of Hematology & Oncology, 14, 1-21.

Röhrig, U. F., Michielin, O., & Zoete, V. (2021). Structure and plasticity of indoleamine 2, 3-dioxygenase 1 (IDO1). Journal of Medicinal Chemistry, 64(24), 17690-17705.

Wang, X. X., Sun, S. Y., Dong, Q. Q., Wu, X. X., Tang, W., & Xing, Y. Q. (2019). Recent advances in the discovery of indoleamine 2, 3-dioxygenase 1 (IDO1) inhibitors. MedChemComm, 10(10), 1740-1754.

Röhrig, U. F., Reynaud, A., Majjigapu, S. R., Vogel, P., Pojer, F., & Zoete, V. (2019). Inhibition mechanisms of indoleamine 2, 3-dioxygenase 1 (IDO1). Journal of medicinal chemistry, 62(19), 8784-8795.

Nayak-Kapoor, A., Hao, Z., Sadek, R., Dobbins, R., Marshall, L., Vahanian, N. N., ... & Khleif, S. N. (2018). Phase Ia study of the indoleamine 2, 3-dioxygenase 1 (IDO1) inhibitor navoximod (GDC-0919) in patients with recurrent advanced solid tumors. Journal for immunotherapy of cancer, 6(1), 1-12.

Komiya, T., & Huang, C. H. (2018). Updates in the clinical development of epacadostat and other indoleamine 2, 3-dioxygenase 1 inhibitors (IDO1) for human cancers. Frontiers in oncology, 8, 423.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Antibody Pairs

IDO1 Matched Antibody Pair (585) (CAT#: APMAB-585LY)

IDO1 Matched Antibody Pair (586) (CAT#: APMAB-586LY)

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For research use only. Not intended for any clinical use.

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