IFNA2C Human
Saccharomyces cerevisiae.
Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Description
Interferon-alpha 2c Recombinant Human produced in yeast is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 19.3kDa. The IFNA2C is purified by proprietary chromatographic techniques.
Product Specs
Macrophages produce IFN-alpha, which possesses antiviral properties. This interferon stimulates the production of two key enzymes: protein kinase and oligoadenylate synthetase.
Recombinant Human Interferon-alpha 2c, produced in yeast, is a single, glycosylated polypeptide chain consisting of 165 amino acids with a molecular weight of 19.3kDa. The purification of IFNA2C is achieved through proprietary chromatographic techniques.
Sterile Filtered White lyophilized (freeze-dried) powder.
The product is lyophilized from a 0.2µm filtered solution concentrated in PBS with a pH of 7.4 and containing 0.02% Tween-20.
For reconstitution of the lyophilized Interferon-alpha 2c, it is recommended to use sterile 18 MΩ-cm H2O to achieve a concentration of at least 100µg/ml. This solution can then be further diluted into other aqueous solutions as needed.
While Lyophilized IFNA2C remains stable at room temperature for up to 3 weeks, it is recommended to store it desiccated below -18°C for optimal long-term preservation. Once reconstituted, Interferon-alpha 2c should be stored at 4°C for a period of 2-7 days. For extended storage, it should be kept below -18°C. It is crucial to avoid repeated freeze-thaw cycles.
The purity is determined to be greater than 97.0% using the following methods:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Activity is determined by measuring the inhibition of the cytopathic effect using a standardized assay.
Interferon alpha-2, IFN-alpha-2, Interferon alpha-A, LeIF A, IFNA2, IFNA2A, IFNA2B, IFNA2C.
Saccharomyces cerevisiae.
CDLPQTHSLG SRRTLMLLAQ MRRISLFSCL KDRRDFGFPQ EEFGNQFQKA ETIPVLHEMI QQIFNLFSTK DSSAAWDETL LDKFYTELYQ QLNDLEACVI QGVGVTETPL MKEDSILAVR KYFQRITLYL KEKKYSPCAW EVVRAEIMRS FSLSTNLQES LRSKE.
Product Science Overview
Interferon-alpha 2c (IFN-α2c) is a member of the type I interferon family, which plays a crucial role in the innate immune response against viral infections. Interferons are cytokines, proteins that are secreted by cells in response to various stimuli, including viral infections, and they have antiviral, antitumor, and immunomodulatory effects .
Interferons were first discovered in 1957 by Isaacs and Lindenmann, who observed that cells infected with a virus produced a substance that could inhibit viral replication in other cells . Interferons are classified into three types based on their receptor specificity: type I, type II, and type III. Type I interferons include multiple subtypes, such as IFN-α and IFN-β, with IFN-α being the most extensively studied .
IFN-α2c is one of the three acid-stable forms of IFN-α2, the others being IFN-α2a and IFN-α2b. These forms share a high degree of sequence identity, with IFN-α2b sharing 99.4% amino acid sequence identity with both IFN-α2a and IFN-α2c . IFN-α2c contains four highly conserved cysteine residues that form two disulfide bonds, which are essential for its biological activity .
Recombinant DNA technology has enabled the production of human interferons, including IFN-α2c, in various expression systems such as Escherichia coli (E. coli). This technology involves inserting the gene encoding IFN-α2c into a plasmid vector, which is then introduced into a host cell for protein expression . The recombinant protein is subsequently purified and formulated for therapeutic use.
IFN-α2c, like other interferons, is used in the treatment of various viral infections and cancers. It exerts its antiviral effects by inducing the expression of interferon-stimulated genes (ISGs) that inhibit viral replication and enhance the immune response . Additionally, IFN-α2c has antitumor properties, making it a valuable therapeutic agent in oncology .
One of the main challenges in the clinical application of interferons, including IFN-α2c, is their short half-life, which necessitates frequent dosing. Researchers are exploring strategies to extend the half-life of interferons, such as pegylation (attachment of polyethylene glycol) and fusion with other proteins . These approaches aim to improve the pharmacokinetic properties and therapeutic efficacy of interferons.
