Recombinant Smad3 Monoclonal Antibody (E-AB-81437)
For research use only.
Verified Samples |
Verified Samples in WB: Jurkat, C6, Hela Verified Samples in IHC: Human breast cancer |
Dilution | WB 1:1000-1:2000, IHC 1:20-1:500 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human, Rat |
Applications | WB, IHC-P |
Clonality | Rabbit Monoclonal |
Immunogen | A synthetic peptide of human Smad3 |
Synonyms | DKFZP586N0721, DKFZp686J10186, HSPC193, HST17436, JV15 2, JV15-2, JV152, LDS1C, LDS3, MAD, MAD (mothers against decapentaplegic Drosophila) homolog 3, MAD homolog 3, Mad homolog JV15 2, Mad protein homolog, hMAD 3, hMAD-3, hSMAD3, mothers against decapentaplegic homolog 3 |
Swissprot | |
Calculated MW | 48 kDa |
Observed MW |
52 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. Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 (PubMed:15799969). Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1 (PubMed:16751101, PubMed:19289081). Co-localizes with LEMD3 at the nucleus inner membrane (PubMed:15601644). MAPK-mediated phosphorylation appears to have no effect on nuclear import (PubMed:19218245). PDPK1 prevents its nuclear translocation in response to TGF-beta (PubMed:17327236). |
Concentration | 300 μg/mL |
Buffer | 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.01% Sodium azide and 0.05% protective protein |
Purification Method | Affinity Purified |
Research Areas | Cancer, Epigenetics and Nuclear Signaling, Metabolism, Signal Transduction, Stem Cells |
Clone No. | R09-7H4 |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
background | The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein functions as a transcriptional modulator activated by transforming growth factor-beta and is thought to play a role in the regulation of carcinogenesis. |
Other Clones
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Unconjugated
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