Data & Images
|Product Name||Anti-FMO5 Antibody|
|Description||Rabbit IgG polyclonal antibody for Dimethylaniline monooxygenase[N-oxide-forming] 5(FMO5) detection. Tested with WB in Human;Mouse;Rat.|
|Cite This Product||Anti-FMO5 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA2108)|
|Replacement Item||This antibody may replace the following items: sc-103495|sc-103494|sc-368225|sc-393732 from Santa Cruz Biotechnology.|
|Validated Species||Human, 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 human FMO5(77-90aa DHYPNFMHNAQVLE), different from the related rat sequence by one amino acid, and different from the related mouse sequence by two amino 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||Dimethylaniline monooxygenase[N-oxide-forming] 5|
|Molecular Weight||60221 MW|
|Protein Function||In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme.|
|Tissue Specificity||Expressed in fetal and adult liver.|
|Sequence Similarities||Belongs to the FMO family.|
|Subcellular Localization||Microsome membrane. Endoplasmic reticulum membrane.|
|Alternative Names||Dimethylaniline monooxygenase [N-oxide-forming] 5;18.104.22.168;Dimethylaniline oxidase 5;Hepatic flavin-containing monooxygenase 5;FMO 5;FMO5;|
|Research Areas|||signal transduction|metabolism|drug metabolism| metabolism|pathways and processes|metabolic signaling pathways||
Background for Dimethylaniline monooxygenase[N-oxide-forming] 5
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-FMO5 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, Mouse, Rat|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-FMO5 Antibody Images
Click the images to enlarge.
All lanes: Anti FMO5 (PA2108) at 0.5ug/ml
Lane 1: Mouse Liver Tissue Lysate at 50ug
Lane 2: Mouse Testis Tissue Lysate at 50ug
Lane 3: Mouse Spleen Tissue Lysate at 50ug
Predicted bind size: 60KD
Observed bind size: 60KD
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.,