Recombinant N-Myc Monoclonal Antibody (AN302034L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa (negative control), IMR-32 |
| Dilution | WB 1:50000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Peptide. This information is proprietary to PTMab. |
| Abbre | N-Myc |
| Synonyms | bHLHe, MODED, N-myc, NMYC, ODED, bHLHe37, MYCN, Class E basic helix-loop-helix protein 37, N myc, N myc proto oncogene protein, Neuroblastoma derived v myc avian myelocytomatosis viral related oncogene, Neuroblastoma MYC oncogene, NMYC proto oncogene protein, N-myc proto-oncogene protein, Oncogene NMYC, pp65/67, V myc avian myelocytomatosis viral oncogene neuroblastoma derived homolog, v myc avian myelocytomatosis viral related oncogene neuroblastoma derived, v myc myelocytomatosis viral related oncogene neuroblastoma derived |
| Swissprot | |
| Calculated MW | 50 kDa |
| Observed MW |
62 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. | A754 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior, including proliferation, differentiation, and apoptosis. These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription. Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families. The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior. The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3, and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes, such as proliferation, transformation, and prevention of apoptosis by inhibiting transcription.In humans the Myc family consists of 5 genes: c-Myc, N Myc, L-Myc, R-Myc, and B-Myc. While c-Myc is expressed in many proliferating cells, N-Myc expression is very restricted, with highest levels in during embryonic development and then in the adult during B-cell development. These expression patterns and results from targeted deletion of N-Myc suggest that N-Myc plays an important role in tissue development and differentiation. In addition, amplification or overexpression of N-Myc has been found in human neuroblastomas and is associated with rapid progression and poor prognosis. |
Other Clones
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Unconjugated
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