Recombinant Cynomolgus Interferon alpha-B Protein (His Tag)

Name: Recombinant Cynomolgus Interferon alpha-B Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2990
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Cynomolgus
Accession	G7PS89
Background	Interferon alpha-B, also known as IFNA8, belongs to thealpha/beta interferon family. Interferons areproteinsmade and released byhost cellsin response to the presence ofpathogenssuch asviruses,bacteria,parasitesortumorcells. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase. They also allow for communication between cells to trigger the protective defenses of theimmune systemthat eradicate pathogens or tumors.Interferons also activate immune cells, such asnatural killer cellsandmacrophages. They increase recognition of infection or tumor cells by up-regulatingantigen presentation toT lymphocytes. They also increase the ability of uninfected host cells to resist new infection by virus. Certain symptoms, such as aching muscles and fever, are related to the production of IFNs during infection. Produced by macrophages, IFN-alpha have antiviral activities.
Description	A DNA sequence encoding the cynomolgus IFNA8 (G7PS89) (Met1-Glu189) was expressed with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Leu 33
AA Sequence	Met1-Glu189
Molecular Weight	The recombinant cynomolgus IFNA8 comprises 177 a.a. and has a calculated molecular mass of 21 KDa. The apparent molecular mass of it is approximately 33 KDa respectively in SDS-PAGE.
Purity	>95% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured in antiviral assays using WISH cells infected with vesicular stomatitis virus. The ED50 for this effect is typically 1-5 pg/mL.
Formulation	Lyophilized from sterile PBS, PH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated 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.