Catalog Number:  C22-106-04Y
Source:  Saccharomyces cerevisiae
Molecular Weight:  Approximately 19.4 kDa, a single non-glycosylated polypeptide chain containing 166 amino acids
Quantity:  20μg/100μg/1000μg
AA Sequence:  MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM
 IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV
 RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Purity:  >98% 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 1.6 × 108 IU/mg.
Physical Appearance:  Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation:  Lyophilized from a 0.2μm filtered solution in PBS, pH 7.4.
Endotoxin:  Less than 1EU/μg of rHuIFN-α2b 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.
Storage:  This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage,
 preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For
 maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to
 -70°C. Avoid repeated freeze/thaw cycles.
Usage:  This material is offered by Shanghai Corning Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

Human Interferon-α2b
At least 23 different variants of IFN-α are known. 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-α 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.