Recombinant Human CDC37L1 Protein: Properties & Research Use

Recombinant Human CDC37L1 Protein is a recombinant form of the human CDC37-like 1 co-chaperone, produced for use in biochemical, cell biology, and protein interaction studies requiring high-purity, well-characterized protein reagents.

Product Name

Recombinant Human CDC37L1 Protein

SKU

rp374042

Protein Family

CDC37 co-chaperone family

Species Origin

Human (Homo sapiens)

Primary Function

Co-chaperone activity; assists HSP90 in client kinase stabilization

Research Areas

Cell cycle regulation, kinase biology, chaperone biology

Background: CDC37L1 and the Co-chaperone System

CDC37L1 (Cell Division Cycle 37-Like 1) is a member of the CDC37 family of co-chaperone proteins. CDC37 family members are recognized for their role in assisting the HSP90 (Heat Shock Protein 90) molecular chaperone machinery, particularly in the folding, stabilization, and maturation of client protein kinases. CDC37L1 shares structural homology with CDC37 but is considered a distinct paralog with potentially unique client protein interactions and tissue-specific expression patterns.

The HSP90–CDC37 co-chaperone axis is critical for maintaining the stability and activity of numerous signaling kinases involved in cell proliferation, differentiation, and survival. Dysregulation of co-chaperone networks has been implicated in oncogenesis and other pathological conditions, making proteins like CDC37L1 of significant interest in both basic research and translational studies.

Protein Characteristics and Production

Recombinant Human CDC37L1 Protein (SKU: rp374042) is produced using recombinant expression systems to ensure consistency, reproducibility, and high purity suitable for research applications. Recombinant production eliminates batch-to-batch variability inherent to protein purification from native tissue sources and provides a well-defined reagent for quantitative assays.

Key characteristics of recombinant proteins in this class typically include defined amino acid sequence corresponding to the human CDC37L1 isoform, controlled expression host for proper folding, and quality-control testing such as SDS-PAGE and functional assays prior to release. Researchers should consult the product datasheet for confirmed specifications including purity, molecular weight, formulation, and storage recommendations.

Research Applications

Recombinant Human CDC37L1 Protein is suitable for a range of in vitro research applications, including but not limited to:

• Protein–protein interaction studies: Investigating the binding of CDC37L1 with HSP90 or client kinases using co-immunoprecipitation, pull-down assays, or surface plasmon resonance (SPR).
• Biochemical assays: Use as a reference standard or positive control in Western blot, ELISA, or activity-based assays targeting co-chaperone function.
• Structural biology: As a component for crystallography or cryo-EM studies aimed at resolving the CDC37L1 interaction interface.
• Drug discovery: Screening small-molecule inhibitors that disrupt CDC37L1–HSP90 or CDC37L1–kinase interactions as potential anti-cancer leads.
• Cell-free systems: Reconstitution experiments to study chaperone-assisted kinase folding in vitro.

This protein is intended for research use only and is not suitable for diagnostic or therapeutic applications.

Handling, Storage, and Quality Considerations

To maintain the activity and integrity of Recombinant Human CDC37L1 Protein, researchers should adhere to the storage and handling guidelines provided in the official product datasheet. General best practices for recombinant proteins include:

• Store at the temperature specified on the datasheet (typically −20°C or −80°C for long-term storage).
• Avoid repeated freeze–thaw cycles; aliquot upon receipt if multiple uses are anticipated.
• Centrifuge briefly before opening to collect contents at the bottom of the vial.
• Dissolve or dilute in the recommended buffer to preserve protein stability.
• Record lot number and expiry date for experimental traceability.

All specific purity percentages, concentration values, and formulation details should be verified against the current product datasheet, as these may vary by lot. Contact Aladdin Scientific technical support for application-specific guidance.

Frequently asked questions

What is the function of CDC37L1 in the cell?

CDC37L1 is a co-chaperone protein related to CDC37 that works within the HSP90 molecular chaperone system. Its primary role involves assisting in the stabilization and maturation of client protein kinases, thereby supporting proper kinase signaling pathways involved in cell cycle regulation and proliferation.

What expression system is used to produce Recombinant Human CDC37L1 Protein (rp374042)?

The specific expression system used for rp374042 should be confirmed by consulting the official Aladdin Scientific product datasheet, as expression host details (e.g., E. coli, baculovirus, or mammalian systems) can affect protein folding and post-translational modifications relevant to your application.

Is Recombinant Human CDC37L1 Protein suitable for use in drug screening assays?

Yes, Recombinant Human CDC37L1 Protein is suitable for in vitro drug discovery applications, including screening for small-molecule inhibitors that disrupt CDC37L1 interactions with HSP90 or client kinases. Researchers should validate assay conditions using the specific lot and confirm purity and activity data from the datasheet before initiating screening campaigns.

How should Recombinant Human CDC37L1 Protein be stored to maintain stability?

Follow the storage conditions specified on the product datasheet. Generally, recombinant proteins of this type should be stored at −20°C or −80°C, with repeated freeze–thaw cycles avoided by aliquoting the protein upon first use. Specific buffer and carrier protein requirements should be confirmed from the datasheet.

References

1. Taipale M, Jarosz DF, Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol. 2010;11(7):515-528. doi:10.1038/nrm2918
2. Caplan AJ. What is a co-chaperone? Cell Stress Chaperones. 2003;8(2):105-107.
3. Roe SM, Ali MM, Clarke P, et al. The mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell. 2004;116(1):87-98. doi:10.1016/S0092-8674(03)01027-4

Products are supplied for research and development use only. Not for use in humans, animals, diagnosis, or therapy.