Recombinant Phospho-Smad2 (S255) Monoclonal Antibody (AN302094L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa |
| Dilution | WB 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Smad2 (phospho S255) fragment |
| Abbre | Phospho-Smad2 (S255) |
| Synonyms | MADH, MADR, hMAD, SMAD, hSMAD, JV18, JV18-1, MADH2, MADR2, hMAD-2, hSMAD2, Smad2, Drosophila, homolog of, hSMAD family member 2, JV181, MAD, MAD homolog 2, MAD Related Protein 2, Mad-related protein 2, MGC22139, MGC34440, Mother against DPP homolog 2, Mothers against decapentaplegic, Mothers against decapentaplegic homolog 2, Mothers against DPP homolog 2, OTTHUMP00000163489, Sma and Mad related protein 2, Sma- and Mad-related protein 2 MAD, SMAD 2, SMAD family member 2 |
| Swissprot | |
| Calculated MW | 52 kDa |
| Observed MW |
58 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cytoplasm, Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Epigenetics and Nuclear Signaling, Stem Cells, Cancer, Kits, Lysates, Other, Metabolism |
| Clone No. | A818 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | SMAD2, also named as MADH2 and MADR2, belongs to the dwarfin/SMAD family, contains 1 MH1 (MAD homology 1) domain and 1 MH2 (MAD homology 2) domain. SMAD2 is a receptor-regulated SMAD(R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. This protein may act as a tumor suppressor in colorectal carcinoma. It is phosphorylated on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, It is phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases, and then able to interact with SMURF2, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, it is phosphorylated on Ser-240 by CaMK2. It is phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. |
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