Recombinant Proteins
Product List
CRYGS Human
Crystallin, Gamma S Human Recombinant
CRYM Human
Crystallin, Mu Human Recombinant
Recombinant human CRYM, expressed in E. coli bacteria, is a single polypeptide chain devoid of any glycosylation modifications. It comprises 334 amino acids, with the first 314 representing the CRYM protein and an additional 20 amino acids forming a His-Tag at the N-terminus. The protein has a molecular weight of 35.9 kDa and is purified using proprietary chromatographic methods.
CRYZ Human
Crystallin Zeta Human Recombinant
MAP1LC3B Mouse
Microtubule-Associated Protein 1 Light Chain 3 Beta Mouse Recombinant
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.
