Recombinant Cdc25C Monoclonal Antibody (AN301883L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa, K562, HEK293, NIH/3T3, C6 |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Cdc25C fragment |
| Abbre | Cdc25C |
| Synonyms | CDC, PPP1R, CDC25C, CDC25, PPP1R60 |
| Swissprot | |
| Calculated MW | 53 kDa |
| Observed MW |
53 kDa
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 | Cell Biology, Epigenetics and Nuclear Signaling |
| Clone No. | A595 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Cdc25C is a protein phosphatase responsible for dephosphorylating and activating cdc2, a crucial step in regulating the entry of all eukaryotic cells into mitosis. Cdc25C is constitutively phosphorylated at Ser216 throughout interphase by c-TAK1, while phosphorylation at this site is DNA damage-dependent at the G2/M checkpoint. When phosphorylated at Ser216, Cdc25C binds to members of the 14-3-3 family of proteins, sequestering Cdc25C in the cytoplasm and thereby preventing premature mitosis. The checkpoint kinases Chk1 and Chk2 phosphorylate Cdc25C at Ser216 in response to DNA damage. |
Other Clones
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Unconjugated
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