Product List

CHI3L1 (22-383) Human

Chitinase 3-Like 1 (22-383 a.a) Human Recombinant

CHI3L1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 370 amino acids (22-383 a.a.) and having a molecular mass of 41.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
CHI3L1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT30872
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

CHI3L1 Human

Chitinase 3-Like 1 Human Recombinant

CHI3L1 Human Recombinant produced in CHO is a single, glycosylated polypeptide chain containing 408 amino acids (1-383) and having a molecular mass of 45.5kDa. CHI3L1 is fused to a 25 amino acid myc-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30883
Source
CHO (chinese hamster ovary cells).
Appearance
Sterile Filtered colorless solution.

CHI3L2 Human

Chitinase 3-Like 2 Recombinant

CHI3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr27-Leu390) containing 374 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 42.1kDa.
Shipped with Ice Packs
Cat. No.
BT30901
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

CHI3L2 Human, Sf9

Chitinase 3-Like 2 Human Recombinant, Sf9

CHI3L2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 372 amino acids (27-390a.a.) and having a molecular mass of 41.9kDa. 
(Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
CHI3L2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT30922
Source
Sf9, Baculovirus cells.
Appearance
Sterile filtered colorless solution.

Chitinase Protein

Chitinase Clostridium Paraputrificum Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT30937
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Introduction

Definition and Classification

Chitinases are hydrolytic enzymes that catalyze the breakdown of 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 . Chitinases are classified into two main types: endochitinases and exochitinases. Endochitinases randomly cleave chitin at internal sites, producing low molecular weight chitooligosaccharides, while exochitinases sequentially cleave off monomers or dimers from the ends of the chitin chains .

Biological Properties

Chitinases exhibit a variety of biological properties, including antimicrobial, antifungal, and insecticidal activities . They are expressed in a wide range of organisms, including bacteria, fungi, plants, and animals . In plants, chitinases are often induced in response to pathogen attack and are part of the plant’s defense mechanism . In animals, chitinases are found in tissues such as the stomach and lungs, where they play roles in digestion and immune responses .

Biological Functions

The primary biological functions of chitinases include the degradation of chitin for nutrient acquisition and defense against chitin-containing pathogens . In plants, chitinases contribute to the defense against fungal pathogens by degrading the chitin in fungal cell walls . In animals, chitinases are involved in immune responses, recognizing and breaking down chitin from pathogens . They also play roles in processes such as molting in arthropods and morphogenesis in fungi .

Modes of Action

Chitinases act by hydrolyzing the β-1,4-glycosidic bonds in chitin, resulting in the production of chitooligosaccharides . They interact with other molecules and cells through binding partners and downstream signaling cascades . For example, in plants, chitinase activity can trigger signaling pathways that lead to the production of other defense-related proteins . In animals, chitinases can bind to chitin-containing pathogens, facilitating their recognition and destruction by the immune system .

Regulatory Mechanisms

The expression and activity of chitinases are regulated at multiple levels, including transcriptional regulation and post-translational modifications . In plants, chitinase genes are often upregulated in response to pathogen attack through signaling pathways involving salicylic acid and jasmonic acid . Post-translational modifications, such as glycosylation, can also affect the stability and activity of chitinases .

Applications

Chitinases have a wide range of applications in biomedical research, agriculture, and industry . In agriculture, chitinases are used as biocontrol agents to protect crops from fungal pathogens and insect pests . In biomedical research, chitinases are studied for their potential roles in diagnosing and treating diseases such as asthma and fungal infections . They are also used in the production of chitooligosaccharides, which have various health benefits, including antimicrobial and anti-inflammatory properties .

Role in the Life Cycle

Throughout the life cycle of organisms, chitinases play crucial roles in development, aging, and disease . In fungi, chitinases are involved in cell wall remodeling during growth and morphogenesis . In arthropods, they are essential for molting and metamorphosis . In humans, chitinases are implicated in various diseases, including asthma and chronic obstructive pulmonary disease (COPD), where they are thought to contribute to inflammation and tissue remodeling .

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