|Sample Size:||30ug for $99, contact us for details|
Data & Images
|Product Name||Anti-survivin Antibody|
|Description||Rabbit IgG polyclonal antibody for Baculoviral IAP repeat-containing protein 5(BIRC5) detection. Tested with WB in Human.|
|Cite This Product||Anti-survivin Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1474)|
|Replacement Item||This antibody may replace the following items: sc-163274|sc-163273 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.
*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 C-terminus of human survivin(121-142aa KKEFEETAKKVRRAIEQLAAMD).|
|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||Baculoviral IAP repeat-containing protein 5|
|Molecular Weight||16389 MW|
|Protein Function||Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. .|
|Tissue Specificity||Expressed only in fetal kidney and liver, and to lesser extent, lung and brain. Abundantly expressed in adenocarcinoma (lung, pancreas, colon, breast, and prostate) and in high-grade lymphomas. Also expressed in various renal cell carcinoma cell lines. .|
|Sequence Similarities||Belongs to the IAP family.|
|Subcellular Localization||Cytoplasm. Nucleus. Chromosome. Chromosome, centromere. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Midbody. Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1- mediated nuclear export.|
|Alternative Names||Baculoviral IAP repeat-containing protein 5;Apoptosis inhibitor 4;Apoptosis inhibitor survivin;BIRC5;API4, IAP4;|
|Research Areas|||cell biology|apoptosis|intracellular|survivin / iaps| epigenetics and nuclear signaling|chromosome structure|chromosome|scaffold proteins|cell cycle|nuclear|transcription|transcription factors| cell biology|cell division|other cell division antibodies| cancer|invasion/microenvironment| kits/ lysates/ other|elisa kits|apoptosis marker and proteins elisa kits|neuroscience target elisa kits|cell death||
Background for Baculoviral IAP repeat-containing protein 5
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-survivin 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, Human|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-survivin Antibody Images
Click the images to enlarge.
Lane 1: HELA Cell Lysate
Lane 2: JURKAT Cell Lysate
Lane 3: CEM Cell Lysate
Lane 4: COLO320 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.,