SUMMARY, EXPLANATION AND LIMITATIONS:
Pulmonary surfactant is a complex mixture of phospholipids and proteins that is secreted from type II cells in alveoli and reduces the surface tension at the alveolar air-liquid interface, providing alveolar stability necessary for normal ventillation. Four distinct proteins isolated from pulmonary surfactant are termed surfactant proteins A, B, C, and D. SP-A (28-36kDa) and SP-D (43kDa) are collagenous carbohydrate-binding proteins, whereas SP-B (8-9kDa) and SP-C (4kDa) are non-collagenous hydrophobic proteins. SP-B is expressed in pulmonary adenocarcinomas with acinar, papillary, bronchioloalveolar, and solid growth patterns. Squamous cell and large cell carcinomas of the lung and nonpulmonary adenocarcinomas do not express SP-B. ProSP-B is glycosylated in the Golgi apparatus and undergoes carboxy- and aminoterminal proteolysis by a cathepsin D-like protease.
This antibody is specific to pro-SP-B and shows no reaction with mature SP-B.
Immunogen: Recombinant pro-surfactant protein B.
Staining pattern: Cytoplasmic.
Positive control: Tissue sample from lung.
This antibody is designed for the specific localization of human Surfactant B precursor using IHC techniques in formalin-fixed, paraffin-embedded tissue sections.