PLBD1 is a secreted protein with weak phospholipase activity, capable of hydrolyzing phospholipids such as phosphatidylcholine, phosphatidylinositol, and lysophospholipids . Structural studies indicate it contains a putative binding pocket that may function as an amidase or peptidase, though its precise catalytic mechanism remains under investigation .
Enzymatic activity: Exhibits phospholipase B-like activity but with lower efficiency compared to canonical phospholipases .
Subcellular localization: Secreted into extracellular spaces, suggesting roles in intercellular signaling or lipid remodeling .
PLBD1 is evolutionarily conserved across mammals, with notable homology in mice (100%), rats (92%), dogs (86%), and humans (79%) .
| Species | Homology (%) |
|---|---|
| Mouse | 100 |
| Rat | 92 |
| Dog | 86 |
| Guinea Pig | 82 |
| Human | 79 |
| Zebrafish | 82 |
| Category | Identifier |
|---|---|
| UniProt ID (Mouse) | Q8VCI0 |
| Entrez Gene ID (Mouse) | 66857 |
| Protein Aliases | LAMA-like protein 1, Phospholipase B-like 1 |
PLBD1 antibodies are primarily used to study lipid metabolism and immune responses. For example:
Western blotting: Detects PLBD1 in tissue lysates or serum samples .
Immunoprecipitation: Isolates PLBD1 for functional studies on its enzymatic activity .
Neutralization assays: Assesses the impact of PLBD1 inhibition on lipid-mediated signaling pathways .
Antibody fragmentation protocols (e.g., pepsin digestion) are often employed to generate antigen-binding fragments (F(ab')₂) for improved tissue penetration .