Recombinant Human IFNα2b / IFNa2b Protein

Beta LifeScience SKU/CAT #: BL-0489PS

Recombinant Human IFNα2b / IFNa2b Protein

Beta LifeScience SKU/CAT #: BL-0489PS
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Tag N/A
Host Species Human
Synonym IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.
Background IFN-alpha is expressed by macrophages and has antiviral activities. IFN stimulates the production of two 56: protein kinase and an oligoadenylate synthetase.
Description IFN-a 2b Human Recombinant expressed in E.Coli is a single, non-glycosylated, polypeptide chain containing 166a.a. and having a molecular weight of 19400 Dalton. The difference between IFNA2A and IFNA2B is in thea.a. 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 unique purification methods.
Source E.coli
AA Sequence MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
Purity >98.0% as determined by(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Bioactivity The specific activity as determined in a viral resistance assay using Bovine
Formulation Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage 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.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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