There are limited reliable information on the commercial production and utilization of proteases for detergent and other industrial uses in Nigeria. Hence, the purification and characterization of Bacillus sp. Gs-3 protease for its potential industrial uses were investigated. The dialyzed crude enzyme was purified 17-fold in a two-step procedure involving carboxymethyl sepharose ionic-exchange chromatography and phenyl sepharose 6-fast flow hydrophobic interaction chromatography. The purified enzyme had its optimal activity at pH 9.0 and 90°C and was stable over a pH range 8.0-11.0. It readily hydrolyzed all the tested protein substrates but exhibited highest affinity for gelatin (Km 0.15 mg mL-1). It retained at least 66.2±0.02% of its original activity in the presence of the tested local commercial detergents and removed bloodstains completely. Its activity was significantly (p>0.05) enhanced by Cu2+ ion but strongly inhibited (75.6±0.07%) by Phenyl-methyl Sulfonyl Fluoride (PMSF). Thus, the enzyme demonstrated desirable properties suitable for its biotechnological applications especially in detergent industry.