名称：重组人IFN-α1b
Species：9
Accession：P01562
GeneID：3439
Source：Escherichia coli.
Molecular Weight：Approximately 19.5 kDa, a single non-glycosylated polypeptide chain containing 167 amino acids.
Quantity：2µg/10µg/1000µg
AA Sequence：MCDLPETHSL DNRRTLMLLA QMSRISPSSC LMDRHDFGFP QEEFDGNQFQ KAPAISVLHE LIQQIFNLFT TKDSSAAWDE DLLDKFCTEL YQQLNDLEAC VMQEERVGET PLMNVDSILA VKKYFRRITL YLTEKKYSPC AWEVVRAEIM RSLSLSTNLQ ERLRRKE
Purity：> 96 % 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, containing 4 % mannitol and 1 % HSA.
Endotoxin：Less than 1 EU/µg of rHuIFN-α1b 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.
Reference：1. Tarhini AA, Gogas H, Kirkwood JM. 2012. J Immunol, 189: 3789-93.
2. Tohyama M, Yang L, Hanakawa Y, et al. 2012. J Invest Dermatol, 132: 1933-5.
3. Corssmit EP, Heijligenberg R, Hack CE, et al. 1997. Clin Exp Immunol, 107: 359-63.
4. Corssmit EP, de Metz J, Sauerwein HP, et al. 2000. J Interferon Cytokine Res, 20: 1039-47.
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.
SDS-PAGE：
