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Citations & References (6)
Invitrogen™
PiPer™ Pyrophosphate or Phosphate Assay Kit
PiPer Pyrophosphate Assay Kit provides reagents for fluorogenic or colorimetric detection as low as 0.4 mμM (fluorescence) or 2 μM (absorbance) inorganic pyrophosphate (PPi) while Phosphate Assay kits can detect down to 0.2 μM Pi in purified enzyme systems. Each kit has enough for 1000 labelings.
製品番号（カタログ番号） P22062
価格（JPY）お問い合わせください ›
110,600
Each
製品タイプ:
ピロリン酸アッセイ
PiPer Pyrophosphate and Phosphate Assay Kit provides an ultrasensitive assay to detect the fluorescent product resorufin. These kits can be used to detect inorganic pyrophosphate (PPi) or phosphate (Pi) in a variety of samples or can monitor the kinetics of their release by a variety of enzymes, including DNA/RNA polymerases, adenylate cyclase, S-acetyl coenzyme A synthetase, ATPases, GTPases, 5′-nucleotidase, protein phosphatases, acid/alkaline phosphatases and phosphorylase kinase. As resorufin has a strong absorption, this assay can be performed either fluorometrically or colorimetrically.
Key Features:
- High Sensitivity: Can detect low levels of inorganic phosphate
- Number of labelings per kit: ~1,000 of 100 μL per assay volume
- Detection method: Colorimetric, Fluorescence
- Compatibility: Can be used with both microplate readers and spectrophotometers
- Excitation/emission maxima: 563/587 nm
- Versatility: Suitable for a wide range of applications including enzyme activity assays
- Quantitative Results: Provides accurate and reproducible results.
The PiPer Pyrophosphate Assay Kit provides a sensitive fluorogenic or colorimetric method for detecting as little as 0.4 μM (fluorescence) or 2 μM (absorbance) inorganic pyrophosphate in a 100 μL assay volume. The PiPer Phosphate Assay Kit detects as little as 0.2 μM Pi (fluorescence) in purified enzyme systems with a 100 μL assay volume.
Use the PiPer Pyrophosphate and Phosphate Assay Kit for applications such as: Anion Detection, Biochemical Toxicology Assays, Cell Analysis, Cell Metabolism, Cell Viability, Cellular Toxicology Assays, Drug Discovery and Development, Enzyme and Protein Activity Assays, Ionic Homeostasis and Signaling, Phosphatase Activity, Phosphatase Activity Assays, Phosphatase Biology, Target and Lead Identification and Validation.
The absorption and fluorescence of resorufin are pH dependent. There is a pKa at ~6.0 where the absorption maximum shifts to ~480 nm and the fluorescence quantum yield is markedly lower. Given Amplex™ Red reagent is unstable at high pH (>8.5) and is sensitive to light, we recommend this reaction be performed using the provided reaction buffer (at optimal pH ~7.5) for best results and reagents kept protected from light. All kits should follow user manual guidelines.
研究用にのみ使用できます。診断用には使用いただけません。
仕様
検出法比色、蛍光
染色剤タイプAmplex™ Red
励起／発光563/587 nm
フォーマット96-ウェルプレート
数量1000 Assays
出荷条件室温
色Red
使用対象（アプリケーション）ピロリン酸アッセイ
使用対象 (装置)分光光度計, マイクロプレートリーダー
製品ラインPiPer
製品タイプピロリン酸アッセイ
Unit SizeEach
組成および保存条件
フリーザー(-5°C~-30°C)に保存し、遮光してください。
よくあるご質問（FAQ）
What is the excitation/emission maxima of resorufin?
引用および参考文献 (6)
引用および参考文献
Abstract
The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme.
Journal:J Biol Chem
PubMed ID:16377641
'We report crystal structures of the citrate and sn-glycerol-1-phosphate (G1P) complexes of (S)-3-O-geranylgeranylglyceryl phosphate synthase from Archaeoglobus fulgidus (AfGGGPS) at 1.55 and 2.0 A resolution, respectively. AfGGGPS is an enzyme that performs the committed step in archaeal lipid biosynthesis, and it presents the first triose phosphate isomerase (TIM)-barrel structure with
Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities.
Journal:J Biol Chem
PubMed ID:12657645
'MazG proteins form a widely conserved family among bacteria, but their cellular function is still unknown. Here we report that Thermotoga maritima MazG protein (Tm-MazG), the product of the TM0913 gene, has both nucleoside triphosphate pyrophosphohydrolase (NTPase) and pyrophosphatase activities. Tm-MazG catalyzes the hydrolysis of all eight canonical ribo- and
Binding modes of zaragozic acid A to human squalene synthase and staphylococcal dehydrosqualene synthase.
Journal:J Biol Chem
PubMed ID:22474324
'Zaragozic acids (ZAs) belong to a family of fungal metabolites with nanomolar inhibitory activity toward squalene synthase (SQS). The enzyme catalyzes the committed step of sterol synthesis and has attracted attention as a potential target for antilipogenic and antiinfective therapies. Here, we have determined the structure of ZA-A complexed with
Selectivity of fungal sesquiterpene synthases: role of the active site's H-1 alpha loop in catalysis.
Journal:Appl Environ Microbiol
PubMed ID:20889795
'Sesquiterpene synthases are responsible for the cyclization of farnesyl pyrophosphate into a myriad of structurally diverse compounds with various biological activities. We examine here the role of the conserved active site H-a1 loop in catalysis in three previously characterized fungal sesquiterpene synthases. The H-a1 loops of Cop3, Cop4, and Cop6
Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response.
Journal:J Biol Chem
PubMed ID:20529853
MazG nucleoside triphosphate pyrophosphohydrolase (NTP-PPase, EC 3.6.1.8) from the avirulent Mycobacterium tuberculosis H37Ra contains a spontaneous mutation on a highly conserved residue, resulting in an A219E substitution (MtMazG[A219E]). In this work, we show that mycobacterial MazG from either the virulent M. tuberculosis H37Rv (MtMazG) or the fast-growing Mycobacterium smegmatis (MsMazG)