Interferon Alpha Human 2a Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 165 amino acids and having a molecular mass of 19241 Dalton.The Interferon-a 2a gene was obtained from human leukocytes.The IFN-A 2a is purified by proprietary chromatographic techniques.
IFN-alpha is produced by macrophages and has antiviral activities. Interferon stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.
Leukocyte interferon, B cell interferon, Type I interferon, IFNA2, IFN-a 2a.
Sterile Filtered White lyophilized (freeze-dried) powder.
Lyophilized without additives.
It is recommended to reconstitute the lyophilized Interferon-alpha 2a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Lyophilized Interferon alpha 2a althoµgh stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-alpha 2a should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Cys-Asp-Leu-Pro-Gln, conforming to the sequence of native human IFN-a.N-terminal methionine has been completely removed enzymatically.
Greater than 98.0% as determined by both:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 270,000,000 IU/mg.
NeoScientific's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals.
Title:Gender specificity of altered human immune cytokine profiles in aging.Publication:Published online before print May 7, 2010, doi: 10.1096/fj.10-160911 September 2010 The FASEB Journal vol. 24 no. 9 3580-3589 Link:http://www.fasebj.org/content/24/9/3580.full