Phospholipase C Protein, Phosphatidylinositol-Specific (from Bacillus cereus)
인용 및 참조 문헌 (56)
Invitrogen™
Phospholipase C Protein, Phosphatidylinositol-Specific (from Bacillus cereus)
This phosphatidylinositol-specific phospholipase C is a highly purified enzyme preparation from Bacillus cereus which cleaves phospholipid phosphatidylinositol (PI) into 2자세히 알아보기
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카탈로그 번호
수량
P6466
50 μL
카탈로그 번호 P6466
제품 가격(KRW)
252,000
Exklusiv online
Ends: 31-Dec-2025
296,000
할인액 44,000 (15%)
Each
카트에 추가하기
수량:
50 μL
제품 가격(KRW)
252,000
Exklusiv online
Ends: 31-Dec-2025
296,000
할인액 44,000 (15%)
Each
카트에 추가하기
This phosphatidylinositol-specific phospholipase C is a highly purified enzyme preparation from Bacillus cereus which cleaves phospholipid phosphatidylinositol (PI) into 2 molecules. This preparation is suitable for both enzymology and cell biology applications.
For Research Use Only. Not for use in diagnostic procedures.
사양
농도100 U⁄ml
단백질 아형Other Proteins
수량50 μL
연구 카테고리Signal Transduction
배송 조건Wet Ice
소스Bacillus cereus
용도(애플리케이션)Assay Standard
형태Solution
종B. cereus
Unit SizeEach
구성 및 보관
Store in freezer (-5 to -30°C).
인용 및 참조 문헌 (56)
인용 및 참조 문헌
Abstract
Mechanism and structure based inhibitors of phospholipase C enzymes.
Authors:Roberts MF, Wu Y, Zhou C, Geng D, Tan C
Journal:Adv Enzyme Regul
PubMed ID:8869740
'PI-specific PLC enzymes are a key component of phosphatidylinositol-mediated signaling pathways since the hydrophobic product, diacylglycerol, activates protein kinase C and the water-soluble product, inositol trisphosphate, is involved in Ca2+ mobilization. Nonspecific, or PC-PLC, enzymes can generate diacylglycerol without Ca2+ mobilization. A series of inhibitors, both lipophilic and water-soluble, have ... More
Diacylglycerol induces fusion of nuclear envelope membrane precursor vesicles.
'Purified membrane vesicles isolated from sea urchin eggs form nuclear envelopes around sperm nuclei following GTP hydrolysis in the presence of cytosol. A low density subfraction of these vesicles (MV1), highly enriched in phosphatidylinositol (PtdIns), is required for nuclear envelope formation. Membrane fusion of MV1 with a second fraction that ... More
A turbidometric assay for phospholipase C and sphingomyelinase.
Authors:Torley L, Silverstrim C, Pickett W
Journal:Anal Biochem
PubMed ID:7864373
'We describe a simple turbidometric assay for phosphatidylcholine-specific phospholipase C (PC-PLC) (EC 3.1.4.3), phosphatidylinositol-specific phospholipase C (PI-PLC) (EC 3.1.4.10), and sphingomyelinase (SMase) (EC 3.1.4.12), suitable for high-volume screening using unmodified substrates. Under the conditions described, 1 to 10 U/ml of PC-PLC (Bacillus cereus) induces a rapid and continuous increase in ... More
Design, synthesis, and evaluation of water-soluble phospholipid analogues as inhibitors of phospholipase C from Bacillus cereus.
Authors:Franklin CL, Li H, Martin SF
Journal:J Org Chem
PubMed ID:12968879
'The rate of hydrolysis of natural phospholipids by the phosphatidylcholine-preferring phospholipase C from Bacillus cereus (PLC(Bc)) follows the order phosphatidylcholine > phosphatidylethanolamine >> phosphatidyl-l-serine. To probe the structural basis for this substrate specificity, a series of water-soluble, nonhydrolyzable substrate analogues were needed so their complexes with the enzyme could be ... More
Internalization of exogenously added memapsin 2 (beta-secretase) ectodomain by cells is mediated by amyloid precursor protein.
'Memapsin 2 (beta-secretase) is the protease that initiates cleavage of amyloid precursor protein (APP) leading to the production of amyloid-beta (Abeta) peptide and the onset of Alzheimer''s disease. Both APP and memapsin 2 are Type I transmembrane proteins and are endocytosed into endosomes where APP is cleaved by memapsin 2. ... More