MDM2 Polyclonal Antibody (E-AB-31995)

For research use only.
Verified Samples |
Verified Samples in WB: Hela |
Dilution | WB 1:500-1:2000, IHC 1:100-1:300, IF 1:200-1:1000 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human, Mouse, Monkey |
Applications | WB, IHC-p, IF |
Clonality | Polyclonal |
Immunogen | Synthesized peptide derived from human MDM2 around the non-phosphorylation site of Ser166. |
Abbre | MDM2 |
Synonyms | ACTFS, Double minute 2 protein, E3 ubiquitin-protein ligase Mdm2, HDMX, Hdm 2, Hdm2, MDM 2, MDM2, MDM2 oncogene E3 ubiquitin protein ligase, Mdm2 p53 E3 ubiquitin protein ligase homolog, Mdm2 transformed 3T3 cell double minute 2 p53 binding protein (mouse) binding |
Swissprot | |
Calculated MW | 55 kDa |
Observed MW |
90 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>nucleoplasm. Cytoplasm. Nucleus>nucleolus. Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus. |
Concentration | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol. |
Purification Method | Affinity purification |
Research Areas | Cancer, Cell Biology, Epigenetics and Nuclear Signaling |
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 | This gene encodes a nuclear-localized E3 ubiquitin ligase. The encoded protein can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. This gene is itself transcriptionally-regulated by p53. Overexpression or amplification of this locus is detected in a variety of different cancers. There is a pseudogene for this gene on chromosome 2. Alternative splicing results in a multitude of transcript variants, many of which may be expressed only in tumor cells. |
Other Clones
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Other Formats
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Unconjugated
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