Data & Images
|Product Name||Anti-Factor VIII Antibody|
|Description||Rabbit IgG polyclonal antibody for Coagulation factor VIII(F8) detection. Tested with WB in Human.|
|Cite This Product||Anti-Factor VIII Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA2061)|
|Replacement Item||This antibody may replace the following items: sc-19665|sc-27647|sc-27649|sc-27650|sc-27651|sc-33583|sc-33584|sc-52026|sc-53465|sc-53466|sc-59508|sc-59510|sc-59512|sc-59514|sc-65947|sc-65948|sc-65949|sc-65950|sc-73597 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.
*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 in the middle region of human Factor VIII(1264-1278aa APVLQDFRSLNDSTN).|
|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||Coagulation factor VIII|
|Molecular Weight||267009 MW|
|Protein Function||Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.|
|Sequence Similarities||Belongs to the multicopper oxidase family.|
|Subcellular Localization||Secreted, extracellular space.|
|Alternative Names||Coagulation factor VIII;Antihemophilic factor;AHF;Procoagulant component;Factor VIIIa heavy chain, 200 kDa isoform;Factor VIIIa heavy chain, 92 kDa isoform;Factor VIII B chain;Factor VIIIa light chain;F8;F8C;|
|Research Areas|||cardiovascular|blood|serum proteins| cardiovascular|platelets|coagulation|extrinsic|regulatory| cancer|invasion/microenvironment|angiogenesis|angiogenic growth factors| stem cells|endothelial progenitors|endothelial markers||
Background for Coagulation factor VIII
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-Factor VIII 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-Factor VIII Antibody Images
Click the images to enlarge.
Lane 1: A431 Cell Lysate
Lane 2: HELA Cell Lysate
Lane 3: SMMC Cell Lysate
Lane 4: JURKAT Cell Lysate
Lane 5: RAJI Cell Lysate
Lane 6: CEM Cell Lysate
Lane 7: HL-60 Cell Lysate
Lane 8: MCF-7 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.,