S7651
Sphingomyelinase from Bacillus cereus
lyophilized powder, ≥100 units/mg protein
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form
lyophilized powder
Quality Level
specific activity
≥100 units/mg protein
mol wt
36873 Da
composition
Protein, ~10% Lowry
storage temp.
2-8°C
Gene Information
Bacillus cereus ATCC 14579 ... BC0671(1203022)
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General description
Sphingomyelinase from Bacillus cereus (Bc-Smase) is a Mg2+-containing metalloenzyme. Bacillus cereus sphingomyelinase induces hemolysis of sheep erythrocytes.
Sphingomyelinase modulates adenosine triphosphate (ATP)-independent endocytosis of fibroblast and large vesicles of macrophages. Sphingomyelinase causes hemolysis of human erythrocytes. It is also a potent virulence factor leading to invasive diseases.
Application
Sphingomyelinase from Bacillus cereus has been used:
- in the measurement of membrane capacitance in brain slices
- for testing and confirming its silkworm-killing activity
- in enzyme activity assay and for elucidating its effect on hydrolysis of sphingomyelin in complex lipid mixtures
Sphingomyelinase has been used in a study to investigate skeletal manifestations in pediatric and adult patients with Niemann Pick disease.
Biochem/physiol Actions
Initiates the formation of sphingomyelin-based second messengers. Activates MAPK (mitogen-activated protein kinase) and SAPKs (stress-activated protein kinases); generates ceramide from sphingomyelin.
Unit Definition
One unit will hydrolyze 1.0 μmole of TNPAL-sphingomyelin per min at pH 7.4 at 37 °C.
Physical form
Lyophilized powder containing potassium phosphate buffer salts and stabilizer.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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Masataka Oda et al.
Biochimica et biophysica acta, 1798(6), 1073-1080 (2010-03-11)
Bacillus cereus sphingomyelinase (Bc-SMase) induces hemolysis of sheep erythrocytes which contain large amounts of sphingomyelin. We investigated the mechanism of this hemolysis in comparison to that induced by Clostridium perfringens alpha-toxin. Pertussis toxin, a Gi-specific inhibitor, N-oleoylethernolamine, a ceramidase inhibitor
Lipid bilayers containing sphingomyelins and ceramides of varying N-acyl lengths: a glimpse into sphingolipid complexity
Jimenez-Rojo N, et al.
Biochimica et Biophysica Acta - Biomembranes, 1838(1), 456-464 (2014)
Masataka Oda
Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan, 129(10), 1233-1238 (2009-10-03)
Bacillus cereus is one that causes of opportunistic human infections. Sphingomyelinase produced by B. cereus is assumed a virulence factor for the infection. Sphingomyelinase from Bacillus cereus (Bc-SMase) is Mg(2+)-containing metalloenzyme. Bc-SMase is a family of neutral SMase (nSMase) and
Purification of a soil bacteria exotoxin using silkworm toxicity to measure specific activity
Usui K, et al.
Microbial Pathogenesis, 46(2), 59-62 (2009)
Melissa Wasserstein et al.
Journal of inherited metabolic disease, 36(1), 123-127 (2012-06-22)
Niemann-Pick disease (NPD) due to acid sphingomyelinase deficiency is a lipid storage disease resulting from the accumulation of sphingomyelin, predominantly within cells of the monocyte-macrophage system. In contrast to other lysosomal storage disorders, skeletal involvement in NPD has not been
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