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Recombinant Human Interferon-alpha2a
Accession P01563
GeneID 3440
Source Yeast
Molecular Weight Approximately 19.2 kDa, a single non-glycosylated polypeptide chain containing 165 amino acids.
Quantity 20µg/100µg/1mg
AA Sequence CDLPQTHSLG SRRTLMLLAQ MRKISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE
Purity > 97 % by SDS-PAGE and HPLC analyses.
Biological Activity Fully biologically active when compared to standard. The specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation Lyophilized from a 0.2 µm filtered solution in PBS, pH 7.4.
Endotoxin Less than 1 EU/µg of rHuIFN-α2a as determined by LAL method.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.
SDS-PAGE
Reference 1. Tarhini AA, Gogas H, Kirkwood JM. 2012. J Immunol, 189: 3789-93.
2. Zarogoulidis P, Kioumis I, Papanas N, et al. 2012. J Chemother, 24: 173-7.
3. Tohyama M, Yang L, Hanakawa Y, et al. 2012. J Invest Dermatol, 132: 1933-5.
4. Corssmit EP, Heijligenberg R, Hack CE, et al. 1997. Clin Exp Immunol, 107: 359-63.
Background IFN-αs are proteins secreted by leukocyte. They are mainly involved in innate immune response against viral infection. The IFN-α family has 13 subtypes and 23 different variants. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.
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