Recombinant Proteins

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Product List

Gliadin Alpha Wheat

Gliadin Alpha Wheat Recombinant

Recombinant Wheat Gliadin Alpha protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 34557.64 Dalton, pI 7.70.
Purified by proprietary chromatographic technique.
Shipped with Ice Packs
Cat. No.
BT11373
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Gliadin Gamma 18.6kDa Wheat

Gliadin Gamma 18.6kD Wheat Recombinant

Gliadin is a cDNA coding for an epitope-carrying fragment of a wheat gamma-gliadin isoform, having a molecular mass of 19 kDa (high proline content and the low pI are likely causes for the observed discrepancy between calculated molecular weight and the observed electrophoretic mobility of approx. 50 kDa on standard SDS-PAGE), pH 4.6. By sequence design the epitopes correspond to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation. Gliadin protein is fused to a hexa-histidine purification tag.

Shipped with Ice Packs
Cat. No.
BT11477
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Gliadin Gamma Wheat

Gliadin Gamma Wheat Recombinant

Recombinant Wheat Gliadin Gamma protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 37945.14 Dalton, pI 7.70.
Purified by proprietary chromatographic technique.
Shipped with Ice Packs
Cat. No.
BT11557
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Gliadin Native

Gliadin Triticum Aestivum Grain Native

The native Gliadin Triticum Aestivum Grain is purified from wheat by protein chemical methods.

Shipped with Ice Packs
Cat. No.
BT11608
Source
Appearance

Sterile Filtered clear solution.

Introduction

Definition and Classification

Gliadin is a type of prolamin, a class of proteins found in wheat and several other cereals within the grass genus Triticum. Gliadins, along with glutenins, are the two main components of gluten, which is essential for giving bread its ability to rise properly during baking . Gliadins are classified into three main types based on their amino acid sequences: α/β-gliadins, γ-gliadins, and ω-gliadins .

Biological Properties

Gliadins are known for their role in the formation of gluten. They are slightly soluble in ethanol and contain only intramolecular disulfide links . Gliadins are composed of different isoforms classified by their electrophoretic mobility: α (25–35 kDa), β (30–35 kDa), γ (35–40 kDa), and ω (55–75 kDa) . These proteins are also called prolamins due to their high content of proline and glutamine . Gliadins are expressed in wheat seeds and are distributed throughout the endosperm .

Biological Functions

Gliadins play a crucial role in the formation of gluten, which is essential for the elasticity and extensibility of dough . They are also involved in immune responses, particularly in individuals with celiac disease. Gliadin peptides can cross the intestinal epithelium and elicit immune responses, leading to inflammation and damage to the intestinal lining . Gliadins are recognized by the immune system as antigens, triggering an immune response in susceptible individuals .

Modes of Action

Gliadins interact with other molecules and cells through various mechanisms. They can aggregate into larger oligomers and interact with other gluten proteins due to their large hydrophobic sections, poly-Q, and repetitive sequences . Gliadin peptides can bind to receptors on immune cells, leading to the activation of downstream signaling cascades that result in inflammation and immune responses . Gliadins also cause the release of zonulin, a protein that opens the tight junctions between intestinal cells, increasing intestinal permeability .

Regulatory Mechanisms

The expression and activity of gliadins are regulated at multiple levels. Transcriptional regulation involves various transcription factors that control the expression of gliadin genes . Post-translational modifications, such as deamidation, can also affect the activity of gliadin peptides . Deamidation increases the immunogenicity of gliadin peptides, enhancing their ability to bind to immune receptors and trigger immune responses .

Applications

Gliadins have several applications in biomedical research, diagnostic tools, and therapeutic strategies. In biomedical research, gliadins are used to study gluten-related disorders, such as celiac disease and non-celiac gluten sensitivity . Diagnostic tools, such as serological tests for anti-gliadin antibodies, are used to diagnose gluten-related disorders . Therapeutic strategies include the development of gluten-free diets and potential therapies to reduce the immunogenicity of gliadins .

Role in the Life Cycle

Gliadins play a role throughout the life cycle of wheat, from seed development to aging. During seed development, gliadins accumulate in the endosperm, providing a source of nitrogen and amino acids for the growing seedling . In individuals with gluten-related disorders, gliadins can contribute to the development of symptoms and complications throughout life . The role of gliadins in aging and disease is an area of ongoing research, with potential implications for understanding the long-term effects of gluten consumption .

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