Purity
Greater than 85% as determined by SDS-PAGE.
Species
Homo sapiens (Human)
Expression Region
28-207aa
Target Protein Sequence
LDCNLLNVHLRRVTWQNLRHLSSMSNSFPVECLRENIAFELPQEFLQYTQPMKRDIKKAFYEMSLQAFNIFSQHTFKYWKERHLKQIQIGLDQQAEYLNQCLEEDKNENEDMKEMKENEMKPSEARVPQLSSLELRRYFHRIDNFLKEKKYSDCAWEIVRVEIRRCLYYFYKFTALFRRK
Note: The complete sequence including tag
sequence, target protein sequence and linker sequence could be provided upon request.
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 6xHis-SUMO-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that
we have in stock, however, if you have any special requirement for the format, please remark your
requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description
This recombinant Human IFNK protein is typically achieved by the manipulation of IFNK gene expression in E.coli cells so that it expresses large amounts of a recombinant IFNK gene. In order to get enough amount of the IFNK protein, strain selection, codon optimization, fusion systems, co-expression, mutagenesis, and isotope labeling techniques are used. Finally, the IFNK protein is isolated from the samples such as cell lysates or medium. Protein refolding, cleavage of fusion moieties and chromatography techniques are involved in the protein purification process.
IFNK is a multifunctional type I IFN that elicits autoimmunity when transgenically expressed in the β cells of the pancreatic islets in mice. IFNK is induced after viral infection or treatment of cells with double-stranded RNA (dsRNA). IFNK signaling stimulates a collection of genes, including IRF1, STAT1, MXA, PKR, and OAS1, which are common to signaling via the type I interferon receptor, and modulates the release of cytokines from monocytes. Different from other members of the type I IFN family, IFNK is constitutively and highly expressed in human keratinocytes. IFNK plays an important role in keratinocyte host defense against herpes simplex virus-1 (HSV-1).
