|Application:||IHC, ICC, WB|
Data & Images
|Product Name||Anti-IRF1 Antibody|
|Description||Rabbit IgG polyclonal antibody for Interferon regulatory factor 1(IRF1) detection. Tested with WB, IHC-P, ICC in Human.|
|Cite This Product||Anti-IRF1 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA2237)|
|Replacement Item||This antibody may replace the following items: sc-13041|sc-13041-X|sc-135952|sc-137061|sc-137061-X|sc-497|sc-497-X|sc-514505|sc-514505-X|sc-514544|sc-514544-X|sc-514934|sc-514934-X|sc-640|sc-640-X|sc-74530|sc-74530-X from Santa Cruz Biotechnology.|
|Application||IHC, ICC, WB
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||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) and ICC.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2017!
|Immunogen||A synthetic peptide corresponding to a sequence in the middle region of human IRF1(169-183aa YMQDLEVEQALTPAL).|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.
*carrier free antibody available upon request.
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||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.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Interferon regulatory factor 1|
|Molecular Weight||36502 MW|
|Protein Function||Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon- stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti- proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells. .|
|Sequence Similarities||Belongs to the IRF family.|
|Subcellular Localization||Nucleus. Cytoplasm. MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88- associated IRF1.|
|Alternative Names||Interferon regulatory factor 1;IRF-1;IRF1;|
|Research Areas|||epigenetics and nuclear signaling|transcription|other factors| cardiovascular|atherosclerosis|apoptosis||
Background for Interferon regulatory factor 1
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-IRF1 Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat
Immunocytochemistry , 0.5-1μg/ml, Human, -
Western blot, 0.1-0.5μg/ml, Human
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-IRF1 Antibody Images
Click the images to enlarge.
Lane 1: COLO320 Cell Lysate
Lane 2: U87 Cell Lysate
Lane 3: HELA Cell Lysate
Lane 4: JURKAT Cell Lysate
Lane 5: MCF-7 Cell Lysate
IHC(P): Human Intestinal Cancer Tissue
ICC: HELA Cell
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.,