|Applications||ELISA, IHC, WB|
|Product Name||Anti-IFN gamma Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Interferon gamma(IFNG) detection. Tested with WB, IHC-P, ELISA in Rat.|
|Cite This Product||Anti-IFN gamma Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # RP1001)|
|Immunogen||E. coli-derived rat IFN gamma recombinant protein(Position: 23-156).|
Assay Dilutions Overview
ELISA , 0.1-0.5μg/ml, Rat, -
Western blot, 0.1-0.5μg/ml, Rat
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P).
Images And Assay Conditions
Figure. Western blot analysis of IFN gamma using anti-IFN gamma antibody (RP1001).
Electrophoresis was performed on a 5-20% SDS-PAGE gel at 70V (Stacking gel) / 90V (Resolving gel) for 2-3 hours. The sample well of each lane was loaded with 50ug of sample under reducing conditions.
Lane : Recombinant Rat IFN gamma Protein 0.5ng
After Electrophoresis, proteins were transferred to a Nitrocellulose membrane at 150mA for 50-90 minutes. Blocked the membrane with 5% Non-fat Milk/ TBS for 1.5 hour at RT. The membrane was incubated with rabbit anti-IFN gamma antigen affinity purified polyclonal antibody (Catalog # RP1001) at 0.5 μg/mL overnight at 4°C, then washed with TBS-0.1%Tween 3 times with 5 minutes each and probed with a goat anti-rabbit IgG-HRP secondary antibody at a dilution of 1:10000 for 1.5 hour at RT. The signal is developed using an Enhanced Chemiluminescent detection (ECL) kit (Catalog # EK1002) with Tanon 5200 system. A specific band was detected for IFN gamma at approximately 22KD. The expected band size for IFN gamma is at 22KD.
Protein Target Info (Source: Uniprot.org)
|Protein Name||Interferon gamma|
|Tissue Specificity||Released primarily from activated T lymphocytes.|
|Alternative Names||Interferon gamma;IFN-gamma;Ifng;|
|Molecular Weight||17918 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Produced by lymphocytes activated by specific antigens or mitogens. IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions. It is a potent activator of macrophages, it has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.|
|Background||Interferon-gamma(IFN-gamma) is an inflammatory cytokine that has been implicated in the development of fibrosis in inflamed tissues. The production of IFN-gamma, which is under genetic control, can influence the development of fibrosis in lung allografts. IFN-gamma is also produced by natural killer(NK) cells and most prominently by CD8 cytotoxic T cells, and is vital for the control of microbial pathogens. Interferon gamma is believed to be crucial for host defence against many infections. Genetically determined variability in IFN-gamma and expression might be important for the development of tuberculosis. IFN-gamma activates human macrophage oxidative metabolism and antimicrobial activity. In addition to having antiviral activity, IFN-gamma has important immunoregulatory functions. IFN-gamma plays an important role in the control of neointima proliferation.|
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,