|Detection of Human/Mouse/Rat CDC25B by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, DA3 mouse myeloma cell line, and Nb2‑11 rat lymphoma cell line. PVDF membrane was probed with 0.3 µg/mL of Goat Anti-Human/Mouse/Rat CDC25B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1649) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for CDC25B at approximately 61 - 67 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|CDC25B in HL‑60 Human Cell Line. CDC25B was detected in immersion fixed HL‑60 human acute promyelocytic leukemia cell line using Goat Anti-Human/Mouse/Rat CDC25B Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1649) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
Cell Division Cycle 25B (Cdc25B) phosphatase removes inorganic phosphate groups covalently attached to tyrosine, serine and threonine residues in proteins (1). Breast cancer patients bearing tumors containing high levels of Cdc25B have been found to have a greater incidence of aggressive, high-grade tumors than those with low Cdc25B levels (2). In cells, the levels of Cdc25B activity are highest during the G2/M transition of the cell cycle, where it is suspected to be involved in “checkpoint” control of cell cycle progression (3). Overexpression of Cdc25B reduces the G2/M cell cycle block caused by ionizing radiation (4). Although activated by phosphorylation, Ser323 phosphorylation causes the enzyme to bind the protein 14-3-3, preventing substrate access to the catalytic site (5). One of the major substrates of Cdc25B is Cdc2, a kinase that is activated by dephosphorylation (6). The recombinant protein is truncated to remove the N‑terminal regulatory domains and is fully active.
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