Anti-PDF Rabbit Polyclonal Antibody for WB and ELISA - Q9HBH1

Core Product Specifications and Parameters

Biological Background: Peptide Deformylase Function and Localization

• Peptide deformylase (PDF) is a mitochondrial enzyme that catalyzes the removal of the formyl group from the N-terminal methionine of nascent polypeptides, a critical step in protein maturation during mitochondrial translation.
• The enzyme belongs to the deformylase family and requires cobalt as a cofactor for its hydrolase activity, as indicated by structural and biochemical studies.
• PDF is ubiquitously expressed across human tissues, reflecting its fundamental role in maintaining mitochondrial protein homeostasis.
• The protein localizes to the mitochondrion, directed by a transit peptide that is cleaved upon import.
• Key structural and functional features include a metal-binding site (cobalt), 3D-structure available, and classification as a hydrolase.

Experimental Guidance and Technical Tips

• The immunogen (amino acids 40–243) corresponds to the mature region of PDF, post transit peptide cleavage. For WB, consider enriching mitochondrial fractions to improve signal intensity.
• Suggested applications are WB and ELISA; validate performance in your specific sample type (human, mouse, or rat) and optimize dilution for your assay conditions.
• Sequence conservation between human, mouse, and rat PDF supports cross-reactivity; confirm by sequence alignment if required for your experiment.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers and researchers with one-stop access to IVD raw materials, including validated antibody pairs, optimized polyclonal antibodies, and bulk ancillary reagents. This anti-PDF antibody supports mitochondrial protein biosynthesis research and assay development. Let CamelBio handle your procurement needs so you can focus on accelerating your diagnostic projects.