Recombinant Human IFI30 Protein (His Tag)

Name: Recombinant Human IFI30 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2519
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P13284
Synonym	GILT, IFI-30, IFI30, IP-30, IP30
Background	IFI3 belongs to the GILT family. This family includes the two characterised human gamma-interferon-inducible lysosomal thiol reductase (GILT) sequences: P13284 and Q9UL8. 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. IFI3 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. IFI3 may facilitate the complete unfolding of proteins destined for lysosomal degradation and plays an important role in antigen processing.
Description	A DNA sequence encoding the human IFI30 (P13284) (Met1-Lys243) with a C-terminal His tag was expressed.
Source	HEK293
Predicted N Terminal	Ser 27
AA Sequence	Met1-Lys243
Molecular Weight	The recombinant human IFI30 is a disulfide-linked homodimer. The reduced monomer comprises 217 a.a. 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.
Purity	>96% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the endocytic reduction of disulfide bonds. Facilitates also MHC class I-restricted recognition of exogenous antigens containing disulfide bonds by CD8+ T-cells or crosspresentation.
Subcellular Location	Secreted. Lysosome.
Protein Families	GILT family
Database References	HGNC: 5398 OMIM: 604664 KEGG: hsa:10437 STRING: 9606.ENSP00000384886 UniGene: Hs.14623

Gene Functions References

Results shows that GILT expression is required for downregulation of PAX-3 proteins in late stage human melanoma cells. GILT co-localizes with PAX-3 proteins regulating its expression through the autophagy and lysosomal degradation pathway in human melanoma cells. PMID: 28857256
GILT functions as a host restriction factor against the retroviruses. PMID: 27655726
GILT expression is anticipated to result in improved presentation of melanoma antigens and more effective antimelanoma T-cell responses. PMID: 26930048
The lysosomal thiol reductase GILT expressed by antigen-presenting cells has diverse cellular and organismal functions. (Review) PMID: 26116226
this review discusses recent studies that have advanced our understanding of the role of GILT in antigen processing and revealed surprising new functions for the enzyme.[review] PMID: 23246037
Single nucleotide polymorphism of the interferon-gamma-inducible protein 30 gene is associated with hyperglycemia in severely obese individuals. PMID: 21701784
GILT is required for efficient histocompatiblity class II-restricted processing of melanoma antigen tyrosinase-related protein 1 epitope in vitro and accelerates the onset of vitiligo in TRP1-specific T-cell receptor transgenic mice. PMID: 20668223
Absence of gamma-interferon-inducible lysosomal thiol reductase in melanomas disrupts T cell recognition of select immunodominant epitopes. PMID: 12021307
Role of the C-terminal propeptide in the activity and maturation of gamma -interferon-inducible lysosomal thiol reductase (GILT). PMID: 12198183
GILT-expressing melanoma cells could prove to be very promising for direct antigen presentation and CD4+ T cell recognition PMID: 18343923
studied gene expression profile of brain lesions of a patient with Neuromyelitis optica by using DNA microarray; found marked up-regulation of interferon gamma-inducible protein 30 (IFI30), CD163, and secreted phosphoprotein 1 (SPP1, osteopontin) PMID: 18410276

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.