Data & Images
|Product Name||Anti-Aurora B Antibody|
|Description||Rabbit IgG polyclonal antibody for Aurora kinase B(AURKB) detection. Tested with WB in Mouse;Rat.|
|Cite This Product||Anti-Aurora B Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1806)|
|Replacement Item||This antibody may replace the following items: sc-14326|sc-14327|sc-25426|sc-293127|sc-393357|sc-65987 from Santa Cruz Biotechnology.|
|Validated Species||Mouse, Rat|
*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.
*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 N-terminus of mouse Aurora B(72-87aa QNKQPFTIDNFEIGRP), different from the related rat sequence by two anino acids.|
|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||Aurora kinase B|
|Molecular Weight||39384 MW|
|Protein Function||Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission- competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes. .|
|Tissue Specificity||Expressed in testis, intestine and spleen. All of them are tissues that contain a large number of proliferating cells. Expressed during S phase, in a cell-cycle-dependent fashion.|
|Sequence Similarities||Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.|
|Subcellular Localization||Nucleus . Chromosome . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle . Midbody . Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the mid-body (By similarity). Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody (By similarity). .|
|Alternative Names||Aurora kinase B;22.214.171.124;Aurora 1;Aurora- and IPL1-like midbody-associated protein 1;Aurora/IPL1-related kinase 2;ARK-2;Aurora-related kinase 2;STK-1;Serine/threonine-protein kinase 12;Serine/threonine-protein kinase 5;Serine/threonine-protein kinase aurora-B;Aurkb;Aik2, Aim1, Airk2, Ark2, Stk1, Stk12, Stk5;|
Background for Aurora kinase B
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Aurora B 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:|
Western blot, 0.1-0.5μg/ml, Rat, Mouse|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-Aurora B Antibody Images
Click the images to enlarge.
Lane 1: Rat Liver Tissue Lysate
Lane 2: 22RV Cell Lysate
Lane 3: HELA Cell Lysate
Lane 4: SW620 Cell Lysate
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.,