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IDO (human) (rec.) (His) (highly active)

Replaces AG-40A-0028
AG-40B-0161-C050 50 µg INQ
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Additional Information

Product Data
Synonyms Indoleamine 2,3-dioxygenase; INDO; IDO1; IDO-1
Properties
Source/Host E. coli
Sequence Human IDO (aa 1-403) is fused at the N-terminus to a His-tag.
Crossreactivity Human
Biological Activity Specific Activity: >100’000U/mg protein with L-tryptophan as substrate (activity assay with catalase). One unit is defined as the amount of enzyme that produces 1nmol of N-formylkynurenine (NFK) per hour. For more information see Activity Test Protocol.
MW ~47kDa (SDS-PAGE)
Purity ≥90% (SDS-PAGE)
Endotoxin Content <0.1EU/μg purified protein (LAL test; Lonza).
Concentration Lot dependent
Formulation Liquid. 0.2μm-filtered solution in 10mM Tris, pH 7.5, containing 100mM NaCl and 20% glycerol.
Other Product Data UniProt link P14902: Indoleamine 2,3-dioxygenase (human)
Product Type Protein
Shipping and Handling
Shipping DRY ICE
Short Term Storage -20°C
Long Term Storage -80°C
Handling Advice After opening, prepare aliquots and store at -80°C. Avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -80°C.
Documents
Protocols Download Document Download
MSDS Download Document Download
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Product Description

IDO is a heme enzyme that catalyzes the first and rate-limiting step in the main pathway of human tryptophan catabolism, the kynurenine pathway, causing depletion of tryptophan which can lead to halted growth of microbes as well as T cells. IDO is an immune checkpoint protein, thought to play a role in a variety of pathophysiological processes such as antimicrobial and antitumor defense, neuropathology, immunoregulation and antioxidant activity. Cancer cells are able to evade the immune system is by hijacking the checkpoint proteins. Increased IDO protein levels drive growth arrest and apoptosis of the effector T cells, a group of immune cells that mediate the immune system’s ability to destroy pathogens. By reducing the number of effector T cells, IDO overexpression prevents the immune system from effectively destroying cancer cells. IDO overexpression has been observed in a wide range of human cancers such as prostatic, colorectal, pancreatic, cervical, gastric, ovarian, head or lung cancer. 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. Biological active IDO enzyme can be used for screening of IDO inhibitors, which have shown promising antitumor activity and appear to be synergistic in combination with chemotherapy and other forms of immunotherapy.
Activity assay figure of IDO (human) (rec.) (His) (highly active) (AG-40B-0161). IDO (human) has been tested with a protocol using catalase (see our website). The specific activity has been calculated to be >100’000U/mg protein with L-tryptophan as substrate (one unit is defined as the amount of enzyme that produces 1nmol of N-formylkynurenine (NFK) per hour).
Activity assay figure of IDO (human) (rec.) (His) (highly active) (AG-40B-0161). IDO (human) has been tested with a protocol using catalase (see our website). The specific activity has been calculated to be >100’000U/mg protein with L-tryptophan as substrate (one unit is defined as the amount of enzyme that produces 1nmol of N-formylkynurenine (NFK) per hour).
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