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EC 3.1.3.1

EC 3.1.3.1 Suppliers list
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Products Intro: Product Name:EC 3.1.3.1
CAS:9001-78-9
Purity:99% Package:100g,500g,1kg,5kg,10kg
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Products Intro: CAS:9001-78-9
Purity:99% Package:500G;1KG;5KG;25KG
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Products Intro: Product Name:Alkaline phosphatase
CAS:9001-78-9
Purity:2.8u/mg Package:10mg 100mg 500mg:150 675 2550
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Products Intro: Product Name:Alkaline Phosphatase, 3000-6000 U/mg protein
CAS:9001-78-9
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Products Intro: Product Name:Phosphatase, Alkaline froM Calf Intestinal Mucosa
CAS:9001-78-9
Package:100Mg;1g Remarks:P0252
EC 3.1.3.1 Basic information
Product Name:EC 3.1.3.1
Synonyms:alkaline;phosphatasealkalinefrome.coli;ALKALINE PHOSPHATASE, SHRIMP;ALKALINE PHOSPHATASE, BOVINE;ALKALINE PHOSPHATASE CALF INTESTINAL;EC 3.1.3.1;EC: 3.1.3.1;CALF INTESTINAL ALKALINE PHOSPHATASE
CAS:9001-78-9
MF:C21H36N8O6
MW:496.56054
EINECS:232-631-4
Product Categories:enzyme;HPLC Fittings;SSI Fittings;Stainless Steel Fittings
Mol File:9001-78-9.mol
EC 3.1.3.1 Structure
EC 3.1.3.1 Chemical Properties
density 1.12 g/mL at 20 °C
storage temp. 2-8°C
form suspension
color white
Specific Gravity1
Water Solubility It is soluble in water.
Stability:Stability Incompatible with strong oxidizing agents
Safety Information
Hazard Codes B,Xi
Risk Statements 36/37/38
Safety Statements 26-36-24/25-22-23
WGK Germany 3
3-10
TSCA Yes
HS Code 35079090
MSDS Information
ProviderLanguage
SigmaAldrich English
EC 3.1.3.1 Usage And Synthesis
Chemical Propertiessolid
UsesHydrolyzes 5′-terminal monophosphate (dephosphorylation) from DNA and RNA. Prevents fragments from self annealing. 5′-nucleic acid targeting for probes.
UsesCommonly used to remove the 5′-terminal phosphate from nucleic acids.
Purification MethodsThe E.coli supernatant in sucrose (20%, 33mM) in Tris-HCl pH 8.0 is purified through a DEAE-cellulose column and recrystallised. To the column eluates in 0.125M NaCl is added MgCl2 (to 0.01M) and brought to 50% saturation in (NH4)2SO4 by adding the solid (0.20g/mL). The mixture is centrifuged to remove bubbles and is adjusted to pH 8.0 (with 2N NaOH). Saturated (NH4)2SO4 at pH 8.0 is added dropwise until the solution becomes faintly turbid (~61% saturation). It is set aside at ~25o for 1hour (turbidity will increase). The mixture is placed in an ice bath for several minutes when turbidity disappears and a clear solution is obtained. It is then placed in a large ice bath at 0o (~5L) and allowed to warm slowly to room temperature in a dark room whereby crystals are formed appearing as a silky sheen. The crystals are collected by centrifugation at 25o if necessary. The crystalline solutions are stable at ~25o for many months. They can be stored at 0o, but are unstable when frozen. Cysteine at 10-3M and thioglycolic acid at 10-4M are inhibitory. This is reversed on addition of Zn2+ ions. Many organic phosphates are good substrates for this phosphatase. [Molamy & Horecker Methods Enzymol 9 639 1966, Torriani et al. Methods Enzymol 12b 212 1968, Engstrom Biochim Biophys Acta 92 71 1964.] Alkaline phosphatase from rat osteosarcoma has been purified by Me2CO precipitation and chromatography on DEAE-cellulose, Sephacryl S-200, and hydroxylapatite. [Nair et al. Arch Biochem Biophys 254 18 1987.] Phosphoproteins (various). These are purified by adsorbing onto an iminodiacetic acid substituted agarose column to which are bound ferric ions. This chelate complex acts as a selective immobilised metal affinity adsorbent for phosphoproteins. [Muszyfiska et al. Biochemistry 25 6850 1986.]
EC 3.1.3.1 Preparation Products And Raw materials
Raw materials1-Butanol
Tag:EC 3.1.3.1(9001-78-9) Related Product Information
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