Rabbit Polyclonal CDK15 Antibody

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     Western blot analysis of Adenylate Kinase 6 expression in Jurkat, HepG2 whole cell lysates.    

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     Immunofluorescent analysis of CDK15 staining in HepG2 cells. Formalin-fixed cells were permeabilized with 0.1% Triton X-100 in TBS for 5-10 minutes and blocked with 3% BSA-PBS for 30 minutes at room temperature. Cells were probed with the primary antibody in 3% BSA-PBS and incubated overnight at 4 C in a hidified chamber. Cells were washed with PBST and incubated with a DyLight 594-conjugated secondary antibody (red) in PBS at room temperature in the dark. DAPI was used to stain the cell nuclei (blue).    

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     Immunohistochemical analysis of CDK15 staining in human breast cancer formalin fixed paraffin embedded tissue section. The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.    

The cyclin-dependent kinase 15 (CDK15), also known as PCTAIRE-3. belongs to the CDK family of serine/threonine kinases, which regulate cell cycle progression, transcription, and neuronal functions. Unlike canonical CDKs (e.g., CDK1 or CDK2), CDK15 exhibits unique expression patterns and regulatory mechanisms. It is primarily expressed in the brain and testis, suggesting roles in neurodevelopment and germ cell regulation. CDK15 activation involves binding to cyclin Y or related cyclins and phosphorylation by upstream kinases, though its precise biological functions remain less characterized compared to other CDKs.

CDK15 antibodies are essential tools for studying its expression, localization, and molecular interactions. These antibodies enable detection of CDK15 in tissues or cultured cells via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Research has linked CDK15 dysregulation to neurological disorders and cancers, though its mechanistic contributions are still under investigation. For example, aberrant CDK15 expression has been observed in glioblastoma and prostate cancer, hinting at potential oncogenic roles. Commercially available CDK15 antibodies are typically raised against specific epitopes (e.g., N-terminal or kinase domains) and validated for specificity in knockout models or siRNA-treated samples. Challenges in CDK15 research include its low abundance and overlapping functions with other PCTAIRE family members (CDK16/PCTAIRE-1. CDK17/PCTAIRE-2), necessitating rigorous antibody validation. Ongoing studies aim to clarify CDK15’s physiological targets and explore its therapeutic potential in disease contexts.