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一般描述
A product of Novozyme Corp.
生化/生理作用
水解 β-两性甘油磷脂的酯键。首选底物为磷脂酰胆碱、磷脂酰乙醇胺及其缩醛磷脂类似物。磷脂酰肌醇和磷脂酰丝氨酸也被水解。其会攻击完整细胞膜上的磷脂。
其他说明
One unit is equivalent to the amount of enzyme producing 1 μmole of free fatty acid per minute at pH 8 and 40 °C.
储存分类代码
13 - Non Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Willem van de Veen et al.
The Journal of allergy and clinical immunology, 131(4), 1204-1212 (2013-03-05)
IL-10-producing regulatory B cells suppress immune responses, and lack of these cells leads to exacerbated symptoms in mouse models of chronic inflammation, transplantation, and chronic infection. IgG4 is a blocking antibody isotype with anti-inflammatory potential that is induced in human
Cedric H De Smet et al.
Biochimica et biophysica acta, 1831(6), 1167-1176 (2013-03-19)
In the yeast Saccharomyces cerevisiae, the molecular species profile of the major membrane glycerophospholipid phosphatidylcholine (PC) is determined by the molecular species-selectivity of the biosynthesis routes and by acyl chain remodeling. Overexpression of the glycerol-3-phosphate acyltransferase Sct1p was recently shown
P K Larsson Forsell et al.
European journal of biochemistry, 262(2), 575-585 (1999-05-21)
Recently, we reported the human 88-kDa calcium-independent phospholipase A2 (iPLA2) cDNA sequence, as well as extensive alternative splicing of the iPLA2 mRNA. In this report we identified the gene coding for iPLA2, which was localized on chromosome 22q13.1. The gene
R Grataroli et al.
European journal of biochemistry, 122(1), 111-117 (1982-02-01)
Upon tryptic activation of pure human prophospholipase A2, a heptapeptide is released from the N-terminal part of the protein yielding active phospholipase A2 (EC 3.1.1.4). Both the kinetics of the activation process and the amino acid sequence of the activation
J J Seilhamer et al.
The Journal of biological chemistry, 264(10), 5335-5338 (1989-04-05)
Synovial fluid from arthritic patients contains multiple forms of phospholipase A2 (PLA2), as resolved by high performance liquid chromatography (Seilhamer, J.J., Plant, S., Pruzanski, W., Schilling, J., Stefanski, E., Vadas, P., and Johnson, L. K. (1989) J. Biochem. (Tokyo), submitted
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