CAT Human
Catalase Human Recombinant
Cat. No.
BT23032
Source
Escherichia Coli.
Synonyms
Catalase, CAT.
Appearance
Sterile filtered yellowish solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
CAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 547 amino acids (1-527) and having a molecular mass of 61.9kDa.
CAT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CAT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Catalase (CAT) is a crucial antioxidant enzyme that plays a vital role in protecting the body from oxidative stress. As a heme enzyme found in the peroxisomes of nearly all aerobic cells, Catalase converts harmful hydrogen peroxide into harmless water and oxygen, mitigating its toxic effects. Catalase also exhibits growth-stimulating properties in various cells, including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells, and both normal and transformed fibroblast cells. While genetic variations in the Catalase gene are associated with reduced catalase activity, acatalasemia is the only known disease directly caused by CAT gene mutations.
Description
Recombinant human CAT, expressed in E.coli, is a non-glycosylated polypeptide chain composed of 547 amino acids (1-527). With a molecular weight of 61.9 kDa, this monomeric protein is fused to a 20 amino acid His-tag at its N-terminus and purified through proprietary chromatographic techniques.
Physical Appearance
A clear, yellowish solution that has been sterilized by filtration.
Formulation
The CAT solution is provided at a concentration of 1mg/ml in a buffer containing 20mM Tris-HCl (pH 8.0), 0.15M NaCl, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze the solution at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Avoid repeated freezing and thawing cycles.
Purity
The purity is determined to be greater than 90% using SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured to be greater than 30,000 units per milligram of protein.
Unit Definition
One unit of Catalase activity is defined as the amount of enzyme required to catalyze the decomposition of 1.0 micromole of hydrogen peroxide (H₂O₂) per minute at a pH of 8.0 and a temperature of 25°C.
Synonyms
Catalase, CAT.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADSRDPASD QMQHWKEQRA AQKADVLTTG AGNPVGDKLN VITVGPRGPL LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITKYSKAKVF EHIGKKTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDPIL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA ARLSQEDPDY GIRDLFNAIA TGKYPSWTFY IQVMTFNQAE TFPFNPFDLT KVWPHKDYPL IPVGKLVLNR NPVNYFAEVE QIAFDPSNMP PGIEASPDKM LQGRLFAYPD THRHRLGPNY LHIPVNCPYR ARVANYQRDG PMCMQDNQGG APNYYPNSFG APEQQPSALE HSIQYSGEVR RFNTANDDNV TQVRAFYVNV LNEEQRKRLC ENIAGHLKDA QIFIQKKAVK NFTEVHPDYG SHIQALLDKY NAEKPKNAIH TFVQSGSHLA AREKANL.
Product Science Overview
Introduction
Catalase is a crucial enzyme found in nearly all living organisms exposed to oxygen. It catalyzes the decomposition of hydrogen peroxide into water and oxygen, a vital reaction for protecting cells from oxidative damage. Human recombinant catalase is a form of this enzyme that is produced through recombinant DNA technology, allowing for large-scale production and use in various applications.
Structure and Function
Production of Human Recombinant Catalase
Human recombinant catalase is produced by inserting the gene encoding the human catalase enzyme into a suitable host cell, such as bacteria or yeast. The host cells are then cultured, and the enzyme is expressed and purified. This method allows for the production of large quantities of catalase with high purity and activity .
Applications
Catalase has several industrial and medical applications:
- Food Industry: It is used to remove hydrogen peroxide from milk before cheese production and in food wrappers to prevent oxidation.
- Textile Industry: Catalase is used to remove hydrogen peroxide from fabrics, ensuring they are peroxide-free before dyeing.
- Medical Research: Catalase is studied for its role in protecting cells from oxidative stress and its potential therapeutic applications .
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