Data & Images
|Product Name||Anti-P53 Picoband™ Antibody|
|Description||Rabbit IgG polyclonal antibody for Cellular tumor antigen p53(TP53) detection. Tested with WB, IHC-P in Human.|
|Cite This Product||Anti-P53 Picoband™ Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PB9008)|
|Replacement Item||This antibody may replace the following items: sc-100350|sc-10840|sc-10843|sc-126|sc-126-X|sc-12904-R|sc-1311-R|sc-135772|sc-135772-X|sc-135773|sc-135773-X|sc-136832|sc-137173|sc-137174|sc-137175|sc-139542|sc-139543|sc-16715-R|sc-16716-R|sc-17105-R|sc-17106-R|sc-17274-R|sc-18079-R|sc-21872-R|sc-22785|sc-244647|sc-244648|sc-249070|sc-249071|sc-376973|sc-398705|sc-48262|sc-514582|sc-514703|sc-6243-G|sc-6243-X|sc-67184|sc-71783|sc-71784|sc-71785|sc-71786|sc-71817-X|sc-7997-R|sc-7997-X|sc-81511|sc-85846|sc-85848|sc-85975|sc-98-X|sc-98384 from Santa Cruz Biotechnology.|
*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).
*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||E.coli-derived human P53 recombinant protein (Position: A74-D393). Human P53 shares 83% and 85% amino acid (aa) sequences identity with mouse and rat P53, respectively.|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 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||Cellular tumor antigen p53|
|Molecular Weight||43653 MW|
|Protein Function||Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA- Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1- mediated transcriptional activation of PER2 (PubMed:24051492). .|
|Tissue Specificity||Ubiquitous. Isoforms are expressed in a wide range of normal tissues but in a tissue-dependent manner. Isoform 2 is expressed in most normal tissues but is not detected in brain, lung, prostate, muscle, fetal brain, spinal cord and fetal liver. Isoform 3 is expressed in most normal tissues but is not detected in lung, spleen, testis, fetal brain, spinal cord and fetal liver. Isoform 7 is expressed in most normal tissues but is not detected in prostate, uterus, skeletal muscle and breast. Isoform 8 is detected only in colon, bone marrow, testis, fetal brain and intestine. Isoform 9 is expressed in most normal tissues but is not detected in brain, heart, lung, fetal liver, salivary gland, breast or intestine. .|
|Sequence Similarities||Belongs to the p53 family.|
|Subcellular Localization||Cytoplasm. Nucleus. Nucleus, PML body. Endoplasmic reticulum. Mitochondrion matrix. Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress.|
|Alternative Names||Cellular tumor antigen p53;Antigen NY-CO-13;Phosphoprotein p53;Tumor suppressor p53;TP53;P53;|
|Research Areas|||cell biology|apoptosis|intracellular|p53 pathway||
Background for Cellular tumor antigen p53
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-P53 Picoband™ 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|
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-P53 Picoband™ Antibody Images
Click the images to enlarge.
IHC(P): Human Lung Cancer Tissue
All lanes: Anti-P53(PB9008) at 0.5ug/ml
Lane 1: HEPG2 Whole Cell Lysate at 40ug
Lane 2: COLO320 Whole Cell Lysate at 40ug
Predicted bind size: 53KD
Observed bind size: 53KD
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.,