LACTB E.coli, His

Beta Lactamase E.coli Recombinant, His Tag
Cat. No.
BT28042
Source
Escherichia Coli.
Synonyms
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

Beta Lactamase is an E.coli Recombinant protein produced in E.Coli containing 379 amino acids (20-377) and having a molecular mass of 41.8kDa. Beta Lactamase is expressed with a 21 N-terminal His tag.
The LACTB is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Beta-lactamase is an enzyme that provides some bacteria with resistance to beta-lactam antibiotics. These antibiotics, including penicillins, cephalosporins, and carbapenems, share a beta-lactam ring in their structure. Beta-lactamase enzymes break this ring, rendering the antibiotics ineffective.
Description
This product is a recombinant Beta-Lactamase protein, produced in E. coli. It consists of 379 amino acids (specifically, amino acids 20-377) and has a molecular weight of 41.8 kDa. This Beta-Lactamase variant is expressed with a 21-amino acid His tag at its N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
This product appears as a colorless solution that has been sterilized by filtration.
Formulation
This LACTB enzyme is provided at a concentration of 1 mg/ml in a buffer solution of 20mM Tris-HCl with a pH of 8.0 and 10% glycerol.
Stability
For optimal storage, keep the product refrigerated at 4°C if you plan to use the entire vial within 2-4 weeks. For longer storage, freeze the product at -20°C. Consider adding a carrier protein (0.1% HSA or BSA) for extended storage. Minimize repeated freezing and thawing.
Purity
The purity of this product is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Beta-lactamase, Cephalosporinase, ampC, ampA, b4150, JW4111.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ.

Product Science Overview

Recombinant Beta Lactamase

Recombinant beta-lactamase refers to the enzyme that has been genetically engineered and produced in a host organism, such as E. coli. This recombinant form is often used in research and industrial applications due to its high purity and consistency. The recombinant beta-lactamase is typically expressed with a His tag (histidine tag), which is a sequence of histidine residues added to the protein to facilitate purification through affinity chromatography .

Expression and Purification

The recombinant beta-lactamase is produced in E. coli cells, which are genetically modified to include the gene encoding the enzyme. The His tag is usually added to the N-terminus of the protein, allowing for easy purification. The His tag binds to nickel ions, enabling the protein to be isolated from other cellular components using a nickel-affinity column .

Structure and Properties

The recombinant beta-lactamase from E. coli typically consists of 379 amino acids, including the His tag, and has a molecular mass of approximately 41.8 kDa . The enzyme is a single, non-glycosylated polypeptide chain and is highly purified using proprietary chromatographic techniques . The His tag not only aids in purification but also does not interfere with the enzyme’s activity.

Applications

Recombinant beta-lactamase is widely used in various research applications, including:

  • Antibiotic resistance studies: Understanding how bacteria develop resistance to beta-lactam antibiotics.
  • Drug development: Screening for new inhibitors of beta-lactamase to combat antibiotic resistance.
  • Protein engineering: Modifying the enzyme to study its structure-function relationships and improve its properties for industrial applications.
Storage and Stability

Recombinant beta-lactamase is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid repeated freeze-thaw cycles to maintain the enzyme’s activity and stability .

In summary, recombinant beta-lactamase from E. coli with a His tag is a valuable tool in scientific research and industrial applications. Its ability to confer antibiotic resistance and its ease of purification make it an essential component in the study of bacterial resistance mechanisms and the development of new therapeutic strategies.

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