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.
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.
Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.4.
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.
Approximately 19.2 kDa, a single non-glycosylated polypeptide chain containing 165 amino acids.
Less than 1 EU/μg of IFN-α2a as determined by LAL method.
This material is offered by Cyagen Biosciences for research, laboratory or further evaluation purposes. FOR RESEARCH USE ONLY. NOT INTENDED FOR ANY ANIMAL OR HUMAN THERAP EUTIC OR DIAGNOSTIC USE.
The specific activity determined by an anti-viral assay is no less than 1.0 × 108 IU/mg.
Sterile filtered white lyophilized (freeze-dried) powder.
CDLPQTHSLG SRRTLMLLAQ MRKISLFSCL KDRHDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE
> 97% by SDS-PAGE and HPLC analyses.