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539480 Sigma-AldrichProteinase K, Tritirachium album

Proteinase K, Tritirachium album MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

SDS
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References
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Data Sheet

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Overview

Replacement Information

Pricing & Availability

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539480-25MG	Retrieving availability... — Limited Availability Stocked Discontinued Limited Quantities Available Available Login to See Inventory Stocked Limited Availability Stocked Remaining : Will advise Remaining : Will advise Will advise Contact Customer Service Contact Customer Service Contact Customer Service Contact Customer Service	Plastic ampoule	25 mg	Retrieving price... Price could not be retrieved Minimum Quantity is a multiple of Maximum Quantity is Upon Order Completion More Information You Saved () — Request Pricing Login to See Your Pricing	Check Availability —	Add To Favorites Add To Favorites Added To My Favorites

Description
Overview	Serine protease that exhibits strong proteolytic activity on a wide variety of denatured and native proteins of high molecular weight. Because of its rapid proteolytic inactivation of endogenous nucleases, it can be used for isolation of mRNA and high molecular weight DNA. Preferentially cleaves bonds next to the carbonyl group of N-substituted hydrophobic, aliphatic, and aromatic amino acids. Inhibited by DFP, Hg²⁺, and PMSF. Not inactivated by metal chelators, sulfhydryl reagents, TLCK, or TPCK.
Catalogue Number	539480
Brand Family	Calbiochem®

References
References	Watazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81. Lebherz, H.G., et al. 1986. Biochem. J. 233, 51. Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.

Product Information
CAS number	39450-01-6
Activity	≥30 mAnsonU/mg dry weight
Unit of Definition	One mAnson unit is defined as the amount of enzyme that will liberate 1.0 µmol of Folin-positive amino acids (calculated as tyrosine) per min at 37°C, pH 7.5.
EC number	3.4.21.14
Form	White lyophilized solid
Formulation	Lyophilized from calcium acetate
Quality Level	MQ300

Applications

Biological Information
Specific Activity	≥40 mAnsonU/mg protein

Physicochemical Information
Contaminants	DNase: no detectable nicking activity with pBR322, incubation for 6 h at 37°C; RNase: no ribonuclease activity with MS2 RNA detected after incubation for 6 h at 37°C

Dimensions

Materials Information

Toxicological Information

Safety Information according to GHS

Safety Information

Product Usage Statements

Storage and Shipping Information
Ship Code	Ambient Temperature Only
Toxicity	Irritant
Storage	+2°C to +8°C
Do not freeze	Ok to freeze
Special Instructions	Following reconstitution, store in the refrigerator (4°C). Stock solutions prepared in 50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0 are stable for up to 1 year at 4°C.

Packaging Information

Transport Information

Supplemental Information

Specifications

Global Trade Item Number
Catalog Number	GTIN
539480-100MG	04055977269147
539480-25MG	07790788051327

Documentation

Proteinase K, Tritirachium album SDS

Title
Safety Data Sheet (SDS)

Proteinase K, Tritirachium album Certificates of Analysis

Title	Lot Number
539480	Enter Lot Number

References

Reference overview
Watazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81. Lebherz, H.G., et al. 1986. Biochem. J. 233, 51. Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.

Brochure

Title
Bulk packaging

Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision	16-November-2016 JSW
Description	Serine protease that exhibits strong proteolytic activity on a wide variety of denatured and native proteins of high molecular weight. Because of its rapid proteolytic inactivation of endogenous nucleases, it can be used for isolation of mRNA and high molecular weight DNA. Preferentially cleaves bonds next to the carbonyl group of N-substituted hydrophobic, aliphatic, and aromatic amino acids. Inhibited by DFP, Hg²⁺, and PMSF. Not inactivated by metal chelators, sulfhydryl reagents, TLCK, or TPCK.
Form	White lyophilized solid
Formulation	Lyophilized from calcium acetate
Recommended reaction conditions	Anson Enzyme Activity Assay: Materials Required • 5 ml of Hemoglobin (20 mg/ml) in 100 mM phosphate buffer, pH 7.5 (6 M urea, 5 mM NaCl). • 0.6 ml of 20 mM CaCl₂ dissolved in distilled water. • 0.1 ml of proteinase K (40 µg/ml) in 20 mM CaCl₂ Activity Assay Protocol 1. Mix the 5 ml hemoglobin, 0.6 ml CaCl₂, and 0.1 ml proteinase K and make up the volume to 6 ml with 20 mM CaCl₂; incubate for 10 min at 25°C. 2. Add 10 ml 300 mM Trichloroacetic acid and incubate at room temperature for 30 min. 3. Centrifuge and transfer 5 ml of the supernatant to a clean tube. Add 10 ml 500 mM NaOH and 3 ml Folin reagent (diluted 1:2 with redistilled water); incubate for 5 min at room temperature. 4. Measure the ΔA at 750 nm. For calibration use tyrosine solutions. 1 mAnson unit liberates 1 µmole of Folin-positive amino acids per min (calculated as tyrosine) under test conditions.
CAS number	39450-01-6
EC number	3.4.21.14
Contaminants	DNase: no detectable nicking activity with pBR322, incubation for 6 h at 37°C; RNase: no ribonuclease activity with MS2 RNA detected after incubation for 6 h at 37°C
Specific activity	≥40 mAnsonU/mg protein
Activity	≥30 mAnsonU/mg dry weight
Unit definition	One mAnson unit is defined as the amount of enzyme that will liberate 1.0 µmol of Folin-positive amino acids (calculated as tyrosine) per min at 37°C, pH 7.5.
Solubility	50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0
Storage	+2°C to +8°C
Do Not Freeze	Ok to freeze
Special Instructions	Following reconstitution, store in the refrigerator (4°C). Stock solutions prepared in 50 mM Tris-HCl, 2 mM calcium acetate, pH 8.0 are stable for up to 1 year at 4°C.
Toxicity	Irritant
References	Watazu, Y., et al. 1993. J. Lab. Clin. Anal. 7, 81. Lebherz, H.G., et al. 1986. Biochem. J. 233, 51. Ebeling, W., et al. 1974. Eur. J. Biochem. 47, 91.

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