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: