|Application:||IHC-P, ICC, WB|
Data & Images
|Product Name||Anti-Ku70 Antibody|
|Description||Rabbit IgG polyclonal antibody for X-ray repair cross-complementing protein 6(XRCC6) detection. Tested with WB, IHC-P, ICC in Human.|
|Cite This Product||Anti-Ku70 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1642)|
|Replacement Item||This antibody may replace the following items: sc-12729|sc-135355|sc-135963|sc-1486|sc-1487|sc-166386|sc-169824|sc-169824-X|sc-169825|sc-169825-X|sc-17789|sc-365766|sc-5309|sc-55505|sc-56129|sc-56130|sc-56131|sc-65575|sc-71469|sc-71470|sc-71471|sc-9033 from Santa Cruz Biotechnology.|
*This antibody is predicted to react with the above species based on antigen sequence similarities. Our Boster Guarantee covers the use of this product with the above species.
|Application||IHC-P, 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 at the C-terminus of human Ku70(530-545aa YPPDYNPEGKVTKRKH).|
|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||X-ray repair cross-complementing protein 6|
|Molecular Weight||69843 MW|
|Protein Function||Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. Required for osteocalcin gene expression. Probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose- 5-phosphate at an abasic site near double-strand breaks. 5'-dRP lyase activity allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription. .|
|Sequence Similarities||Belongs to the ku70 family.|
|Subcellular Localization||Nucleus . Chromosome .|
|Alternative Names||X-ray repair cross-complementing protein 6;3.6.4.-;4.2.99.-;5'-deoxyribose-5-phosphate lyase Ku70;5'-dRP lyase Ku70;70 kDa subunit of Ku antigen;ATP-dependent DNA helicase 2 subunit 1;ATP-dependent DNA helicase II 70 kDa subunit;CTC box-binding factor 75 kDa subunit;CTC75;CTCBF;DNA repair protein XRCC6;Lupus Ku autoantigen protein p70;Ku70;Thyroid-lupus autoantigen;TLAA;X-ray repair complementing defective repair in Chinese hamster cells 6;XRCC6;G22P1;|
|Research Areas|||epigenetics and nuclear signaling|dna / rna|dna damage & repair|non homol. end joining||
Background for X-ray repair cross-complementing protein 6
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Ku70 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:|
Immunocytochemistry , 0.5-1μg/ml, Human, -|
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-Ku70 Antibody Images
Click the images to enlarge.
All lanes: Anti Ku70 (PA1642) at 0.5ug/ml
Lane 1: HT1080 Whole Cell Lysate at 40ug
Lane 2: SGC Whole Cell Lysate at 40ug
Lane 3: MM453 Whole Cell Lysate at 40ug
Lane 4: SW620 Whole Cell Lysate at 40ug
Lane 5: HELA Whole Cell Lysate at 40ug
Lane 6: A431 Whole Cell Lysate at 40ug
Lane 7: A549 Whole Cell Lysate at 40ug
Lane 8: RAJI Whole Cell Lysate at 40ug
Predicted bind size: 70KD
Observed bind size: 70KD
IHC(P): Human Placenta Tissue
ICC: A549 Cell
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.,