Recombinant SMARCB1/BAF47 Monoclonal Antibody (AN302046L)
For research use only.
| Verified Samples | Verified Samples in WB: Jurkat,?NIH-3T3, PC-12 |
| Dilution | WB 1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | SMARCB1/BAF47 |
| Synonyms | MRD, SNF, CSS, INI, BAF, Snr, RTPS, PPP1R, SNF5L, SWNTS, SMARCB, SMARCB1, BAF47, CSS3, INI1, MRD15, PPP1R144, RDT, RTPS1, SNF5, SNF5L1, SWNTS1, Sfh1p, Snr1, hSNFS, BRG1-associated factor 47, hSNF5, Integrase interactor 1 protein, Malignant rhabdoid tumor suppressor, SNF5 homolog, Sucrose nonfermenting yeast homolog like 1, SWI/SNF complex component SNF5, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1, SWI10, Transcription factor TYE4, Transcription regulatory protein SNF5, TYE4 |
| Swissprot | |
| Calculated MW | 44 kDa |
| Observed MW |
47 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 | Nucleus |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Epigenetics and Nuclear Signaling, Cancer |
| Clone No. | A766 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | ATP-dependent chromatin remodeling complexes play an essential role in the regulation of nuclear processes such as transcription and DNA replication and repair. The SWI/SNF chromatin remodeling complex consists of more than 10 subunits and contains a single molecule of either BRM or BRG1 as the ATPase catalytic subunit. The activity of the ATPase subunit disrupts histone-DNA contacts and changes the accessibility of crucial regulatory elements to the chromatin. The additional core and accessory subunits play a scaffolding role to maintain stability and provide surfaces for interaction with various transcription factors and chromatin. The interactions between SWI/SNF subunits and transcription factors, such as nuclear receptors, p53, Rb, BRCA1, and MyoD, facilitate recruitment of the complex to target genes for regulation of gene activation, cell growth, cell cycle, and differentiation processes.SMARCB1/BAF47, one of the core subunits of the SWI/SNF complex, is necessary for efficient nucleosome remodeling by BRG1 in vitro. SMARCB1/BAF47 is an essential part of the esBAF (mouse embryonic stem cell specific SWI/SNF complex) and is necessary for early embryogenesis and hepatocyte differentiation. In addition, SMARCB1/BAF47 is considered to be a tumor suppressor protein; inactivating mutations have been indentified in a large number of malignant rhabdoid tumors. |
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