What Is CABLES1 and Why Does It Matter?

CABLES1 (CDK5 and ABL1 Enzyme Substrate 1) is a linker protein that physically bridges cyclin-dependent kinase 5 (CDK5) and the non-receptor tyrosine kinase ABL1. First identified as an interactor of CDK3 and CDK5, CABLES1 plays a central role in coordinating cell cycle progression and apoptotic signaling. Its expression is frequently downregulated in a range of human cancers, including colorectal, ovarian, and head-and-neck carcinomas, suggesting a tumor-suppressive function.

At the molecular level, CABLES1 modulates p53 and p73 stability and transcriptional activity, thereby coupling DNA-damage signals to apoptotic outcomes. Researchers studying checkpoint pathways, kinase–substrate interactions, or tumor suppressor networks rely on well-characterized recombinant CABLES1 protein to perform in vitro binding assays, kinase activity measurements, and structural studies.

Biochemical Properties of Recombinant Human CABLES1 Protein

Recombinant Human CABLES1 Protein (rp374224) is produced using a recombinant expression system to yield a protein that faithfully represents the human CABLES1 sequence. Key biochemical considerations for working with this reagent include:

• Molecular weight: The CABLES1 gene encodes a protein of approximately 78–80 kDa; the apparent molecular weight on SDS-PAGE may differ slightly depending on tag additions and post-translational modifications present in the expression system used.
• Binding partners: CABLES1 interacts with CDK3, CDK5, and ABL1 kinases, as well as with the tumor suppressors p53 and p73.
• Post-translational modifications: CABLES1 is a substrate for both CDK5 and ABL1-mediated phosphorylation, which regulates its stability and interactions.
• Storage and handling: Recombinant proteins should be stored according to the datasheet instructions, typically at −80 °C, and repeated freeze–thaw cycles should be avoided to preserve activity.

Note: Specific purity, tag information, formulation buffer, and endotoxin levels should be confirmed in the official product datasheet for rp374224.

Research Applications of Recombinant Human CABLES1 Protein

Recombinant Human CABLES1 Protein is a versatile reagent suited to multiple experimental workflows:

1. Protein–protein interaction studies: CABLES1 can be used as bait or prey in pull-down assays and co-immunoprecipitation experiments to map its interactome with CDK5, ABL1, p53, and p73.
2. In vitro kinase assays: As a validated substrate for CDK5 and ABL1, recombinant CABLES1 serves as a positive control or experimental substrate in kinase activity assays and inhibitor screening.
3. Structural biology: Purified recombinant CABLES1 can support X-ray crystallography, cryo-EM, or biophysical studies (SPR, ITC) aimed at defining its domain architecture and interaction interfaces.
4. Cell cycle and apoptosis pathway research: CABLES1 can be used to reconstitute or supplement cell-free systems studying p53/p73-dependent transcription and DNA-damage checkpoints.
5. Antibody validation: Recombinant CABLES1 serves as a reliable positive control antigen for validating anti-CABLES1 antibodies in Western blot, ELISA, and immunofluorescence applications.

Ordering and Handling Recommendations

Recombinant Human CABLES1 Protein is available from Aladdin Scientific under SKU rp374224. When planning your experiments, consider the following best practices:

• Aliquot upon receipt: Prepare single-use aliquots immediately after receipt to minimize freeze–thaw cycles.
• Confirm lot-specific data: Always refer to the Certificate of Analysis (CoA) supplied with each lot for purity, concentration, and activity data.
• Pilot experiments: Titrate the protein concentration in your assay system before committing to large-scale experiments.
• Cold-chain shipping: The product is shipped on dry ice; inspect packaging integrity immediately upon delivery.

For volume pricing, custom formulations, or bulk orders, contact Aladdin Scientific's sales team directly. Product specifications and safety data are available on the product page.