|Validated Species:||Human, Mouse, Rat|
Data & Images
|Product Name||Anti-Livin Antibody|
|Description||Rabbit IgG polyclonal antibody for Baculoviral IAP repeat-containing protein 7(BIRC7) detection. Tested with WB, IHC-P in Human;Mouse;Rat.|
|Cite This Product||Anti-Livin Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1427)|
|Replacement Item||This antibody may replace the following items: sc-166390|sc-22963|sc-22964|sc-30161|sc-33954|sc-33955|sc-393237|sc-71592 from Santa Cruz Biotechnology.|
|Validated Species||Human, Mouse, Rat|
*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, 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 2018!
|Immunogen||A synthetic peptide corresponding to a sequence at the N-terminus of human Livin(115-132aa)(a) HTGHQDKVRCFFCYGGLQ), different from the mouse sequence by one amino acid.|
|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.|
|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 7|
|Molecular Weight||32798 MW|
|Protein Function||Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing. .|
|Tissue Specificity||Isoform 1 and isoform 2 are expressed at very low levels or not detectable in most adult tissues. Detected in adult heart, placenta, lung, lymph node, spleen and ovary, and in several carcinoma cell lines. Isoform 2 is detected in fetal kidney, heart and spleen, and at lower levels in adult brain, skeletal muscle and peripheral blood leukocytes.|
|Sequence Similarities||Belongs to the IAP family.|
|Subcellular Localization||Nucleus . Cytoplasm . Golgi apparatus . Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively in the cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis.|
|Alternative Names||Baculoviral IAP repeat-containing protein 7;6.3.2.-;Kidney inhibitor of apoptosis protein;KIAP;Livin;Melanoma inhibitor of apoptosis protein;ML-IAP;RING finger protein 50;Baculoviral IAP repeat-containing protein 7 30kDa subunit;Truncated livin;p30-Livin;tLivin;BIRC7;KIAP, LIVIN, MLIAP, RNF50;UNQ5800/PRO19607/PRO21344;|
|Research Areas|||cell biology|apoptosis|intracellular|survivin / iaps| cancer|invasion/microenvironment|death receptors & ligands|cell death|receptors||
Background for Baculoviral IAP repeat-containing protein 7
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Livin 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, Rat, Mouse
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-Livin Antibody Images
Click the images to enlarge.
Lane 1: HT1080 Cell Lysate
Lane 2: SW620 Cell Lysate
IHC(P): Human Mammary Cancer Tissue
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.,