Recombinant Human Interferon α2A Variant (Lys46)/IFN-α2A #abs04124

abs04124-10ug

1-2 Weeks

77

abs04124-50ug

1-2 Weeks

214

abs04124-500ug

1-2 Weeks

589

abs04124-1mg

1-2 Weeks

801

Description

Our E.coli expression system is utilized to produce Recombinant Human Interferon alpha-2a, resulting in the expression of the target gene encoding Cys24-Glu188.

Other names

IFNA2, also known as Interferon Alpha-2, IFN-Alpha-2, Interferon Alpha-A, or LeIF A, is a protein with potent antiviral and immunomodulatory properties. This protein belongs to the interferon alpha family and plays a crucial role in the body's defense against viral infections.
IFNA2 is synthesized by immune cells in response to viral invasion. It acts by binding to specific cell receptors, triggering a cascade of signaling pathways that ultimately result in the upregulation of various genes involved in antiviral defense. This leads to the inhibition of viral replication and the enhancement of immune responses.
The therapeutic applications of IFNA2 are diverse. It has been used in the treatment of chronic hepatitis B and C infections, certain types of cancer such as hairy cell leukemia and malignant melanoma, and autoimmune disorders like multiple sclerosis. IFNA2 is often administered through injections and may cause side effects such as flu-like symptoms, fatigue, and depression.
Research is ongoing to explore the potential of IFNA2 in other medical areas. It has shown promise in the treatment of viral respiratory infections, such as influenza, and has been investigated for its antitumor effects in various types of cancer. The development of novel delivery methods and combination therapies involving IFNA2 is a subject of ongoing study.
In conclusion, IFNA2, also referred to as Interferon Alpha-2, IFN-Alpha-2, Interferon Alpha-A, or LeIF A, is a vital protein involved in the body's defense against viral infections. Its antiviral and immunomodulatory properties make it a valuable therapeutic agent in several medical conditions. Ongoing research aims to further elucidate its mechanisms of action and expand its clinical applications.

Source

Escherichia coli.

Format

The solution was filtered through a 0.2 μm filter and subsequently lyophilized. The filtration was done on a solution containing 20mM PB, 150mM NaCl, and a pH of 7.2. The resulting lyophilized product contains all of the same components in the original solution.

Properties

aa_sequence

RSKLSESLTNLQSSTDKFLKDETYEQQLNDLEAVIQGVVEPTETLMKEDSIARVYKFQIRIYTL LKEKRYSPCAWVEVRAEIRMSSFSLNFGNQFKAEETIPVHLEMIQQIFNLFSTDMCDLPQTHSL GSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEE.Please create a highly comparable content using the original text, but rearranging it to make it sound more natural and coherent.

Concentration

Based on the results from SDS-PAGE analysis, it has been confirmed that the sample has a purity level of over 95%. This indicates that the composition of the sample is highly uniform and free from any significant impurities or contaminants.

Endotoxin_level

The concentration of less than 0.1 ng/μg (1 IEU/μg) has been determined using the LAL test. Let me produce another piece of content by reorganizing the given information to ensure its similarity to the original text.

Activity

The potency of this substance was determined through a viral resistance assay conducted on VSV-WISH cells, yielding a Specific Activity exceeding 1.0 x 10^8 IU/ mg. As a result, this product boasts exceptional viral-resistant properties that make it highly effective in combatting viral infections.

Reconstitution

Please make sure to centrifuge the tubes before opening them. Avoid using vortex or pipetting for mixing. It is not advisable to dilute the protein to a concentration lower than 100 μg/ml. Dilute the lyophilized protein in ddH2O. Remember to aliquot the reconstituted solution to minimize freeze-thaw cycles.

Stability & Storage

The stability and storage conditions of lyophilized protein should be taken into consideration. It is recommended to store the lyophilized protein at temperatures below -20°C to maintain its integrity. However, it is worth noting that the protein can still remain stable at room temperature for a period of 3 weeks.
On the other hand, once the protein is reconstituted into a solution, a different set of storage conditions apply. The reconstituted protein solution should ideally be stored at a temperature range of 4-7°C. Under these conditions, the solution can retain its stability for a duration of 2-7 days.
To ensure long-term stability, it is advisable to aliquot the reconstituted protein samples and store them at temperatures below -20°C. These aliquots can maintain their stability for a longer period, specifically up to 3 months. This storage method helps to preserve the protein's integrity and allows for multiple uses over an extended timeframe.
It is important to adhere to these storage guidelines to prevent degradation and maintain the functionality of the lyophilized and reconstituted protein samples. Proper storage conditions play a crucial role in ensuring the reliability and effectiveness of the protein for various scientific and research applications.

Target

Background

At least 23 different variants of IFN-α are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end.

Accession

P01563