Recombinant Proteins
Product List
CRYGS Human
Crystallin, Gamma S Human Recombinant
The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
CRYM Human
Crystallin, Mu Human Recombinant
CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
CRYZ Human
Crystallin Zeta Human Recombinant
CRYZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
MAP1LC3B Mouse
Microtubule-Associated Protein 1 Light Chain 3 Beta Mouse Recombinant
MAP1LC3B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-120 a.a.) and having a molecular mass of 16.7kDa.
MAP1LC3B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Crystallins are a family of water-soluble proteins predominantly found in the lens of the eye. They are classified into three main types: α-crystallins, β-crystallins, and γ-crystallins. Each type has distinct structural and functional properties:
- α-Crystallins: Function as molecular chaperones, preventing protein aggregation.
- β-Crystallins: Serve as structural proteins, contributing to the transparency and refractive index of the lens.
- γ-Crystallins: Highly stable proteins that maintain lens clarity and function.
Key Biological Properties:
- Stability: Crystallins are remarkably stable, which is essential for maintaining lens transparency over a lifetime.
- Solubility: They are highly soluble, allowing them to form a dense, transparent medium in the lens.
Expression Patterns:
- Crystallins are primarily expressed in the lens, but some are also found in other tissues such as the retina, brain, and heart.
Tissue Distribution:
- α-Crystallins: Found in the lens and other tissues like the heart and brain.
- β-Crystallins and γ-Crystallins: Predominantly located in the lens.
Primary Biological Functions:
- Lens Transparency: Crystallins maintain the transparency and refractive properties of the lens.
- Protein Homeostasis: α-Crystallins act as chaperones, preventing the aggregation of other proteins.
Role in Immune Responses and Pathogen Recognition:
- Crystallins have been implicated in immune responses, particularly in the context of autoimmune diseases like uveitis.
Mechanisms with Other Molecules and Cells:
- α-Crystallins: Interact with misfolded proteins to prevent aggregation.
- β- and γ-Crystallins: Form stable complexes that contribute to lens structure.
Binding Partners:
- Crystallins bind to various proteins and small molecules, stabilizing them and preventing aggregation.
Downstream Signaling Cascades:
- α-Crystallins are involved in signaling pathways that regulate cell survival and stress responses.
Expression and Activity Control:
- Transcriptional Regulation: Crystallin gene expression is regulated by transcription factors such as Pax6 and Sox2.
- Post-Translational Modifications: Phosphorylation, acetylation, and glycosylation modify crystallin activity and stability.
Biomedical Research:
- Crystallins are studied for their role in cataract formation and other lens-related disorders.
Diagnostic Tools:
- Crystallin levels can serve as biomarkers for lens health and certain diseases.
Therapeutic Strategies:
- Targeting crystallin pathways offers potential treatments for cataracts and other protein aggregation diseases.
Development:
- Crystallins are essential for lens development and differentiation.
Aging:
- Age-related modifications in crystallins contribute to cataract formation.
Disease:
- Mutations and post-translational modifications in crystallins are linked to various lens disorders, including cataracts and presbyopia.
