Purified anti-human IFN-α2 Antibody, IFN-α2, W20057G,BioLegend,632252

Host

Rat

Reactivity

Human

Application

Direct ELISA - Quality tested

Platform ID

BAB084726192

BioLegend

Headquarters

8999 BioLegend Way San Diego, CA 92121 United States

Contact

Tel: 1-858-455-9588
Fax: +49 (4131) 7023913

Email:

Product Specifications
Scientific Background

Specifications

NamePurified anti-human IFN-α2 Antibody, IFN-α2, W20057G
Cat. No.632252
HostRat
RRIDAB_3662350 (BioLegend Cat. No. 632252)
IsotypeRat IgG2a, κ
ReactivityHuman
ApplicationDirect ELISA - Quality tested
ClonalityMonoclonal
Clone NumberW20057G
Concentration0.5 mg/mL
TargetIFN-alpha2
ImmunogenHuman Recombinant IFN-α2 Protein
PurityThe antibody was purified by affinity chromatography.
FormulationPhosphate-buffered solution, pH 7.2, containing 0.09% sodium azide
StorageThe antibody solution should be stored undiluted between 2°C and 8°C.
Regulatory StatusResearch Use Only

Scientific Background

Interferons are divided into type I, II, and III. Type I IFNs (IFN-α and IFN-β) are most abundant in number, distribution, and expression. They are also highly conserved among mammals in both structure and function. IFN-α2 has been used in the treatment of cancer such as bladder cancer, hepatocellular carcinoma, and leukemia. IFN-α2 augments the suppressed immune functions in patients with head and neck squamous cell carcinoma (HNSCC). IFN-α2 initiated T and NK cell mediated cytotoxicity of tumor cells through IFNγ dependent and independent mechanisms. IFN-α2 enhances suppressed T cell cytotoxicity by stimulation of the perforin-granzyme B system (IFNγ dependent). IFN-α2 also induces the expression of perforin-granzyme B in NK cells (NK mediated cytotoxicity, IFNγ independent). In a preliminary study, IFN-α2 appears to be an effective immunostimulator and impacts the clinical outcome in tongue squamous cell carcinoma patients. IFN-α has been used in the treatment of chronic hepatitis C (CHC); nevertheless, IFN-α is relatively unstable and requires frequent parenteral administration. Pegylation of IFN-α, polyethylene glycol (PEG)-IFN-α, reducesin vitroactivity but increase the stability and plasma half-life of IFN-α. Therefore, PEG-IFN-α has replaced IFN-α in CHC treatment.

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