OIF Antibody / Osteoinductive Factor Polyclonal Antibody (RQ4434)

OIF Antibody by IHC in Mouse Lung. Immunohistochemistry of paraffin-embedded mouse lung sections using OIF Antibody. Strong extracellular and pericellular staining is visible around pulmonary blood vessels and airway-associated structures, while much of the surrounding alveolar parenchyma shows comparatively limited labeling. The Osteoinductive Factor Polyclonal Antibody demonstrates a matrix-associated OGN staining pattern that is particularly prominent in connective tissue surrounding vascular and bronchial structures.

OIF Antibody by IHC in Rat Lung. Immunohistochemistry of paraffin-embedded rat lung sections using OIF Antibody. Strong OGN/OIF staining is concentrated in connective tissue surrounding pulmonary vascular and airway-associated structures, with weaker labeling of some airway epithelium and comparatively limited staining throughout the alveolar parenchyma. The Osteoinductive Factor Polyclonal Antibody demonstrates a predominantly extracellular and pericellular staining pattern consistent with the extracellular matrix association of osteoglycin.

OIF Antibody by IHC in Rat Bladder. Immunohistochemistry of paraffin-embedded rat bladder sections using OIF Antibody. Strong extracellular and stromal staining is visible around glandular and epithelial structures, while the epithelial cells themselves show substantially less labeling. The Osteoinductive Factor Polyclonal Antibody demonstrates prominent OGN localization within the supporting connective tissue and extracellular matrix surrounding these structures, with little nuclear staining.

OIF Antibody by WB in Mouse Heart and NIH3T3 Cells. Western blot testing of mouse heart tissue lysate (lane 1) and mouse NIH3T3 whole cell lysate (lane 2) with OIF Antibody. A prominent band is detected at approximately 40 kDa in both samples, slightly above the predicted 34 kDa molecular weight of OGN. The Osteoinductive Factor Polyclonal Antibody produces particularly strong target-region reactivity in NIH3T3 cells, while mouse heart shows a weaker but distinct band at a similar position. Migration above the calculated protein mass is compatible with post-translational modification of osteoglycin.