|Product Name||Anti-DDT Antibody|
|Storage & Handling||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.|
|Description||Rabbit IgG polyclonal antibody for D-dopachrome decarboxylase(DDT) detection. Tested with WB, IHC-P, ELISA in Human.|
|Cite This Product||Anti-DDT Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # RP1011)|
|Contents/Buffer||Each vial contains 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3. Carrier free (No BSA) form available in stock. If you want this antibody carrier free please specify "Carrier Free" or "No BSA" in your order note.|
|Immunogen||E. coli-derived human DDT recombinant protein(Position: M1-L118).|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Human
Immunohistochemistry(Paraffin-embedded Section), 0.5-1μg/ml, Human, By Heat
ELISA , 0.1-0.5μg/ml, Human,
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.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).
Images And Assay Conditions
Figure. Western blot analysis of DDT using anti- DDT antibody (RP1011).
Electrophoresis was performed on a 5-20% SDS-PAGE gel at 70V (Stacking gel) / 90V (Resolving gel) for 2-3 hours. The sample well of each lane was loaded with 50ug of sample under reducing conditions.
Lane: Recombinant Human DDT Protein 0.5ng
After Electrophoresis, proteins were transferred to a Nitrocellulose membrane at 150mA for 50-90 minutes. Blocked the membrane with 5% Non-fat Milk/ TBS for 1.5 hour at RT. The membrane was incubated with rabbit anti- DDT antigen affinity purified polyclonal antibody (Catalog # RP1011) at 0.5 μg/mL overnight at 4°C, then washed with TBS-0.1%Tween 3 times with 5 minutes each and probed with a goat anti-rabbit IgG-HRP secondary antibody at a dilution of 1:10000 for 1.5 hour at RT. The signal is developed using an Enhanced Chemiluminescent detection (ECL) kit (Catalog # EK1002) with Tanon 5200 system. A specific band was detected for DDT at approximately 15KD. The expected band size for DDT is at 15KD.
Figure 2. IHC analysis of DDT using anti- DDT antibody (RP1011).
DDT was detected in paraffin-embedded section of human placenta tissues. Heat mediated antigen retrieval was performed in citrate buffer (pH6, epitope retrieval solution) for 20 mins. The tissue section was blocked with 10% goat serum. The tissue section was then incubated with 1μg/ml rabbit anti- DDT Antibody (RP1011) overnight at 4°C. Biotinylated goat anti-rabbit IgG was used as secondary antibody and incubated for 30 minutes at 37°C. The tissue section was developed using Strepavidin-Biotin-Complex (SABC)(Catalog # SA1022) with DAB as the chromogen.
Protein Target Info (Source: Uniprot.org)
|Protein Name||D-dopachrome decarboxylase|
|Alternative Names||D-dopachrome decarboxylase;220.127.116.11;D-dopachrome tautomerase;Phenylpyruvate tautomerase II;DDT;|
|Subcellular Localization||Cytoplasm .|
|Molecular Weight||12712 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI).|
|Research Areas||Cell Biology
*You can search these to find other products in these research areas.
|Background||DDT, D-dopachrome tautomerization, converts D-dopachrome into 5,6-dihydroxyindole. Northern blot analysis revealed that DDT was expressed as a 0.6-kb mRNA in all tissues tested, with the strongest expression in liver. The DDT gene in human and mouse is identical in exon structure to the MIF gene. Both genes have 2 introns that are located at equivalent positions, relative to a 2-fold repeat in protein structure.the genes for DDT and MIF are closely linked on human chromosome 22 and mouse chromosome 10.|
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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.,