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Human IFI30 Protein (His Tag)

GILT,IFI-30,IFI30,IP-30,IP30

Catalog Number P12623-H08H
Organism Species Human
Host Human Cells
Synonyms GILT,IFI-30,IFI30,IP-30,IP30
Molecular Weight The recombinant human IFI30 is a disulfide-linked homodimer. The reduced monomer comprises 217 amino acids and has a predicted molecular mass of 24.7 kDa. The apparent molecular mass of the protein is approximately 31-34 kDa in SDS-PAGE under reducing conditions.
predicted N Ser 27
SDS-PAGE
Purity > 96 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human IFI30 (P13284) (Met1-Lys243) with a C-terminal polyhistidine tag was expressed.
Bio-activity
Research Area Cancer |Signal transduction |Metabolism |Pathways and Processes |Redox metabolism |Oxidative stress |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background IFI30 belongs to the GILT family. This family includes the two characterised human gamma-interferon-inducible lysosomal thiol reductase (GILT) sequences: P13284 and Q9UL08. It also contains several other eukaryotic putative proteins with similarity to GILT. The aligned region contains three conserved cysteine residues. In addition, the two GILT sequences possess a C-X(2)-C motif that is shared by some of the other sequences in the family. This motif is thought to be associated with disulphide bond reduction. IFI30 is a lysosomal thiol reductase that can reduce protein disulfide bonds. It facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds. It also facilitates MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation. IFI30 may facilitate the complete unfolding of proteins destined for lysosomal degradation and plays an important role in antigen processing.
Reference
  • Haque MA, et al. (2002) Absence of gamma-Interferon-inducible Lysosomal Thiol Reductase in Melanomas Disrupts T Cell Recognition of Select Immunodominant Epitopes. J Exp Med. 195(10):1267-77.
  • Phan UT, et al. (2000) Gamma-interferon-inducible lysosomal thiol reductase (GILT). Maturation, activity, and mechanism of action. J Biol Chem. 275(34):25907-14.
  • Phan UT, et al. (2001) Multiple species express thiol oxidoreductases related to GILT. Immunogenetics. 53(4):342-6.