Proteinase K Solution (20 mg/mL) - BioReagent,DNase, RNase free,Suitable for molecular biology,sterile,≥95%(Native-PAGE),20 mg/mL , CAS No.39450-01-6

CAS: 39450-01-6 Cat. No.: P1520268 EC Number: 254-457-8,3.4.21.64

GRADE & PURITY Suitable for molecular biology, BioReagent, DNase, RNase free, Sterile, ≥95%(Native-PAGE), 20 mg/mL

Storage

Store at 2-8°C

Shipped In

Wet ice

Application

Nucleic Acid Extraction and Purification

Overview

This product is derived from Pichia pastoris expressing a site-directed mutagenesis-optimized gene for Proteinase K from Engyodontium album. It offers advantages such as higher specific activity, higher yield, and a broader active pH/temperature range compared to the native enzyme. Advanced protein engineering techniques and a 28,000-liter yeast fermentation platform effectively reduce unit costs, providing a cost-effective solution for biopharmaceutical R&D and production. Yeast-based high-efficiency expression and chromatographic purification ensure product purity. This product is free from bacterial endotoxins, resulting in a broader range of applications compared to native Proteinase K.

Proteinase K is one of the most active proteases available, with an active pH range of 4-12 and a temperature range of 0-75°C. It retains activity even in the presence of SDS, Urea, or EDTA. It cleaves peptide bonds at the carboxyl side of aliphatic and aromatic amino acids and is capable of degrading all proteins.

Catalog	P1520268
Product Name	Proteinase K Solution (20 mg/mL)
Source/Species	Pichia pastoris expressing a genetically engineered Engyodontium album Proteinase K gene.
Molecular Weight	29.3 kDa
Isoelectric Point (pI)	8.9
Dilution Buffer	20 mM Tris-HCl (pH 7.4), 1 mM CaCl₂; or 20 mM Tris-HCl (pH 7.4), 1 mM CaCl₂, 2% Glycerol.
Storage Buffer	20 mM Tris-HCl (pH 7.4), 1 mM CaCl₂, 50% Glycerol.
Storage	Stable for 1 year at 4°C.
Note	After opening, if stored at 2–8°C for more than one week, it is recommended to filter sterilize the solution to prevent microbial contamination.

Applications

1. In genetic diagnostic kits, genomic DNA extraction kits, and RNA extraction kits for removing nucleases and other protein contaminants.
2. In the biopharmaceutical industry for the extraction of nucleic acids, polysaccharide-based drugs, and other non-protein biological products, such as in the preparation of DNA vaccines and heparin.
3. In the daily chemical industry for skin care (removing aged stratum corneum cells), as well as in leather tanning, the production of hydrolyzed protein flavorings, cosmetics, and feed processing.

Usage Instructions

Use the 20-40 mg/mL stock solution to achieve a final concentration of 50-200 μg/mL in the digestion or lysis buffer. Incubation times can range from 30 minutes to 18 hours depending on the application requirements. Prolonged incubation may lead to autodegradation of the enzyme.

Enzyme Activity and Unit Definition

• Activity: ≥ 900 U/mL
• Unit Definition: One unit (U) is defined as the amount of enzyme that catalyzes the release of 1 μmol of tyrosine per minute from a casein substrate at 37°C and pH 7.5.

Optimal Conditions and Influencing Factors

Optimal pH Range	7.5-11.5
Optimal Temperature Range	Recommended range: 37-70°C (Highest activity at 70°C)
Activators	1-5 mM Ca²⁺
Inhibitors	Diisopropyl fluorophosphate (DIFP), Phenylmethylsulfonyl fluoride (PMSF)
Inactivation Method	Add PMSF to the reaction system to a final concentration of 5 mM.

Residual Impurities Testing

• This product is free from DNA and RNA, and contains no detectable DNase or RNase activity.
• No deoxyribonuclease activity was detected after incubating with λDNA substrate for over 3 hours at 37°C.
• No ribonuclease activity was detected after incubating with an RNA substrate for over 3 hours at 37°C.

Precautions

1. To ensure your safety and health, please wear appropriate laboratory attire, protective gloves, and goggles during operation.
2. This product may cause skin allergic reactions; handle with care.
3. If the Proteinase K solution requires repeated use, aliquot it to avoid contamination and loss of activity.

Specifications

Specifications & Purity

BioReagent, DNase, RNase free, Suitable for molecular biology, sterile, ≥95%(Native-PAGE), 20 mg/mL

Stability And Storage

Store at 4℃ long term (12 months). Upon receipt,  it is recommended to aliquot.

Storage

Store at 2-8°C

Shipped In

Wet ice

This product requires cold chain shipping. Ground and other economy services are not available.

Grade

BioReagent, DNase, RNase free, Sterile, Suitable for molecular biology

Purity

≥95%(Native-PAGE)

Names and Identifiers

• Enzyme Commission Number: 3.4.21.64
• Isomeric SMILES: C[C@H]([C@@H]1C(=O)N2[C@]1([C@](C(=C2C(=O)OCC3=CC=C(C=C3)[N+](=O)[O-])OC4=CC=CC=C4)(C)OC5=CC=CC=C5)OP(=O)(O)O)O
• WGK Germany: 1
• Reaxy-Rn: 38293759
• Reaxys-RN_link_address: https://www.reaxys.com/reaxys/secured/hopinto.do?context=S&query=IDE.XRN=38293759&ln=

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63. Dandan Feng, Zhu Zhu, Shangpeng Wang, Yangcan Gao, Yingwen Li, Yuying Sun, Jiquan Zhang.  (2025)  A type I crustin with an inhibitory effect on proteases and strong binding capacity to chitin from Neocaridina denticulata sinensis.  Comparative Immunology Reports,      [PMID:] [10.1016/j.cirep.2025.200226]

64. Jing Zhao, Maoning Li, Wenbang Liao, Yufei Shao, Qingyuan Du, Dandan Li, Yu Nan, Zhi Zhang, Dazhi Sun.  (2025)  Hierarchically porous degradable foam prepared by water-in-oil high internal phase emulsion template for high-performance recyclable oil - water separation.  JOURNAL OF HAZARDOUS MATERIALS,      [PMID:41207227] [10.1016/j.jhazmat.2025.140385]

65. Ling Ma, Shu-Ling Yang, Wen-Qian Lian, Xin-Feng Wei, Kai Zhang, Rui-Ying Bao, Wei Yang.  (2025)  Encapsulation of Enzymes in Metal–Organic Frameworks with Dual Thermal Protection for Melt Processing of Self-Biodegradable Plastics.  MACROMOLECULES,      [PMID:] [10.1021/acs.macromol.5c00584]

66. Ke Zhan, Yuting Zhao, Haiying Li, Shan Jiang.  (2025)  Octopod-shaped silver–gold alloy for NIR-driven synergistic photothermal and catalytic bacterial ablation.  COLLOIDS AND SURFACES B-BIOINTERFACES,      [PMID:41380240] [10.1016/j.colsurfb.2025.115353]

67. Zhen-Yu Zhao, Ya-Ning Che, Qian Huang, Han-Wen Yang, Xian-Hua Wang, Lin-Yi Dong.  (2025)  Rapid and sensitive detection of Candida albicans using nystatin-functionalized magnetic spheres.  JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES,      [PMID:41447893] [10.1016/j.jchromb.2025.124896]

68. Nazish Muzaffar, Shujie Zhang, Qian Li, Yuhui Yang, Yanli Xie, Yuan Tian.  (2025)  Thermostable extracellular enzyme-mediated biodegradation of Aflatoxin B1 and Zearalenone in maize flour: A promising strategy.  INTERNATIONAL BIODETERIORATION & BIODEGRADATION,      [PMID:] [10.1016/j.ibiod.2025.106212]

69. Wanning Gao, Shengyuan Shi, Youcong Li, Fangyuan Liu, Yudi Cheng, Jie Zheng, Meng Qiao, Shuai Yuan, Xing Zhang.  (2026)  DNA-directed assembly of core-satellite MOF structures for spatially compartmentalized multi-enzyme cascade catalysis.  CHEMICAL ENGINEERING JOURNAL,      [PMID:] [10.1016/j.cej.2026.173137]

70. Lu Tian, Baiqiang Chen, Jingxue Huang, Yu Cao, Tingting Wu.  (2026)  A multifunctional biomimetic interface biosensor for one-step amplified detection of tumor-derived exosomal miRNA.  CHEMICAL ENGINEERING JOURNAL,      [PMID:] [10.1016/j.cej.2026.173463]

71. Han Pang, Qiang Zhao.  (2026)  Microscale thermophoresis sensor for homogeneous and one-step protein detection based on dual aptamers binding induced DNA switch.  TALANTA,      [PMID:41702041] [10.1016/j.talanta.2026.129535]

72. Dandan Feng, Yakun Song, Zuqi Wu, Wuruo Liu, Yuting Pu, Yangcan Gao, Yuying Sun, Jiquan Zhang.  (2026)  Physiological and biochemical characterization of trypsin from Neocaridina denticulata sinensis and its roles in ontogenesis and immune response.  PLoS One,  21  (2): (e0342746).  [PMID:41701695] [10.1371/journal.pone.0342746]

73. Xuan Ling, Ting Han, Pengfei Yang, Qian Zhang, Yong Xiang, Zhao Wang, Shikai Hu, Xiaoran Hu.  (2026)  Artificial Intelligence-Assisted Identification and Prevention of Chronic Obstructive Pulmonary Disease Using Biodegradable and Reusable Piezoelectric Elastomer/Poly(l-lactic acid) Composite Nanofiber Membrane.  ACS Applied Materials & Interfaces,      [PMID:41672635] [10.1021/acsami.5c23120]

74. Peng Wei, Junhui Li, Yuheng Chen, Jichao Zhang, Yuchen Liu, Yumin Xia, Yanping Wang.  (2026)  Comparative study the hydrolytic degradation behavior of high-performance biobased aromatic-aliphatic liquid crystal copolyesters in different degradation medium.  INTERNATIONAL JOURNAL OF POLYMER ANALYSIS AND CHARACTERIZATION,      [PMID:] [10.1080/1023666X.2025.2582797]

75. Lei Gong, Yuesheng Zhang, Enyang Xu, Hongtao Lu, Junrui Duan, Jianna Bao.  (2026)  Construction of Fully Biodegradable Poly(L-Lactide-Co-Caprolactone) Random Copolymer/Poly(D-Lactide) Blend: Crystallization, Toughness, and Biodegradability.  POLYMER ENGINEERING AND SCIENCE,      [PMID:] [10.1002/pen.70520]