Anti-BPI Rabbit Polyclonal Antibody for WB, ELISA - P17213

Core Product Specifications and Parameters

Biological Background: BPI Function and Localization

• Bactericidal permeability-increasing protein (BPI) is a 53.9 kDa secreted glycoprotein belonging to the BPI/LBP/Plunc superfamily, also known as CAP 57. It is encoded by the BPI gene in humans.
• BPI exerts potent antimicrobial activity selectively against many Gram-negative bacteria by binding with high affinity to lipopolysaccharides (LPS) in the bacterial outer membrane, leading to membrane permeabilization and bacterial killing.
• Specifically, recombinant BPI demonstrates antibacterial activity against Pseudomonas aeruginosa, and this activity is neutralized by excess LPS from the same organism, confirming LPS-dependent targeting.
• The protein localizes primarily to the membrane of cytoplasmic granules in myeloid cells and is secreted upon neutrophil activation, playing a critical role in innate immune defense.
• Tissue expression is restricted to cells of the myeloid lineage, including neutrophils and monocytes, consistent with its function in early host defense against bacterial infection.
• Post-translational modifications include disulfide bond formation and glycosylation, as indicated by UniProt keywords, which are likely important for structural stability and activity.

Experimental Guidance and Technical Tips

• The immunogen corresponds to amino acids 248–487 within the C-terminal region of human BPI. This region is distinct from the N-terminal LPS-binding domain, potentially allowing recognition of both full-length BPI and C-terminal fragments.
• For Western blot (WB), consider using reduced and non-reduced conditions to evaluate disulfide bond-dependent migration, as BPI contains multiple disulfide linkages that may affect apparent molecular weight.
• In ELISA applications, the antibody may be suitable for detecting native or recombinant BPI in solution; however, optimal coating conditions and antibody dilutions should be empirically determined.
• Given the myeloid-restricted expression, validate the antibody’s specificity in relevant positive control cell lines (e.g., differentiated HL-60 or primary neutrophils) and include knockout controls or blocking peptides where possible.
• Cross-reactivity with mouse BPI (predicted) should be confirmed experimentally in the target sample system, as sequence homology in the immunogen region may vary.

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