Recombinant human IFN-a 2b produced in
E. coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19.4 kDa. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.
Synonyms: IFN Alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Formulation: lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Purity: Greater than 98% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Source:Escherichia coli. Amino acid sequence: MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Uniprot ACC number: Q86UP4
Transportation method: Shipped at room temperature.
Stability: Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN Alpha 2b 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.
Biological Activity: The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.
Solubility: It is recommended to reconstitute the lyophilized IFN-alpha 2b in sterile 18MΩ-cm H
2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
References: Title:IFN-β induces apoptosis in human SH-SY5Y neuroblastoma cells through activation of JAK–STAT signaling and down-regulation of PI3K/Akt pathway. Publication:Article first published online: 11 NOV 2010 DOI:10.1111/j.1471-4159.2010.07046. x © 2010 The Authors. Journal of Neurochemistry © 2010 International Society for Neurochemistry. Link:http://onlinelibrary. wiley. com/doi/10.1111/j.1471-4159.2010.07046. x/full
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