Chitinase Protein

Chitinase Clostridium Paraputrificum Recombinant
Cat. No.
BT30937
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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

Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. 
The Chitinase is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Chitinase is an enzyme that breaks down chitin, a component found in fungal cell walls and some animal exoskeletons. Organisms that produce chitinase, such as bacteria, fungi, and some animals, use it for various purposes like digestion, cell wall remodeling, or defense against pathogens. In humans, chitinase is found in gastric juices for digestion and has been implicated in allergies and asthma.
Description
This product is a recombinant Chitinase protein from Clostridium Paraputrificum, produced in E. coli. It is a single, non-glycosylated polypeptide chain with a His tag at the N-terminus. The protein has a molecular weight of 64.2kDa and is purified using chromatographic techniques.
Physical Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.
Formulation
The Chitinase protein is lyophilized from a 0.2µm filtered solution in phosphate-buffered saline (PBS).
Solubility
To reconstitute the lyophilized Chitinase, dissolve it in sterile 18MΩ-cm H2O at a concentration of at least 100µg/ml. The reconstituted solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Chitinase is stable at room temperature for up to 3 weeks. For long-term storage, store desiccated below -18°C. Reconstituted Chitinase should be stored at 4°C for 2-7 days or below -18°C for longer periods. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of this Chitinase protein is greater than 95% as determined by SDS-PAGE.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.

Product Science Overview

Introduction to Chitinase

Chitinase is an enzyme that breaks down chitin, a long-chain polymer of N-acetylglucosamine, which is a component of the cell walls of fungi, the exoskeletons of arthropods, and the scales of fish and amphibians. Chitinases are found in a variety of organisms, including bacteria, fungi, plants, and animals, where they play roles in defense mechanisms, digestion, and morphogenesis.

Clostridium Paraputrificum

Clostridium paraputrificum is a species of anaerobic, spore-forming bacteria that belongs to the genus Clostridium. This bacterium is known for its ability to produce various enzymes, including chitinases, which enable it to degrade chitin. Clostridium paraputrificum is commonly found in soil, marine environments, and the gastrointestinal tracts of animals.

Recombinant Chitinase from Clostridium Paraputrificum

Recombinant chitinase from Clostridium paraputrificum is produced using recombinant DNA technology, where the gene encoding the chitinase enzyme is cloned and expressed in a host organism, typically Escherichia coli. This allows for the production of large quantities of the enzyme for research and industrial applications.

The recombinant chitinase from Clostridium paraputrificum is a non-glycosylated polypeptide chain containing 582 amino acids and has a molecular mass of approximately 64.2 kDa . It is fused with a His tag at the N-terminus to facilitate purification using affinity chromatography techniques .

Production and Purification

The production of recombinant chitinase involves the following steps:

  1. Gene Cloning: The gene encoding chitinase is isolated from Clostridium paraputrificum and inserted into a suitable expression vector.
  2. Transformation: The expression vector is introduced into a host organism, such as Escherichia coli, through a process called transformation.
  3. Expression: The host organism is cultured under conditions that induce the expression of the chitinase gene, leading to the production of the recombinant enzyme.
  4. Purification: The recombinant chitinase is purified using chromatographic techniques, such as affinity chromatography, which exploits the His tag fused to the enzyme .
Applications

Recombinant chitinase from Clostridium paraputrificum has several applications in various fields:

  • Agriculture: Chitinase can be used as a biopesticide to control fungal pathogens and insect pests that contain chitin in their cell walls or exoskeletons.
  • Biotechnology: Chitinase is used in the production of chitooligosaccharides, which have applications in medicine, agriculture, and food industries.
  • Medical Research: Chitinase is studied for its potential role in treating diseases such as asthma and allergies, where chitinase activity is linked to the degradation of chitin-containing allergens .
Stability and Storage

The lyophilized recombinant chitinase is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage . Upon reconstitution, it should be stored at 4°C for short-term use and below -18°C for long-term use, with the addition of a carrier protein to prevent freeze-thaw cycles .

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