Recombinant Proteins

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CRYAA Human

Crystallin Alpha A Human Recombinant

Recombinant Human CRYAA, expressed in E.Coli, is a non-glycosylated polypeptide chain with 173 amino acids and a molecular weight of 19.9 kDa. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19871
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile solution.

CRYAB Human

Crystallin Alpha B Human Recombinant

Recombinant CRYAB, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 20.1 kDa. It consists of 175 amino acids and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19948
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

CRYAB Human, His

Crystallin Alpha B Human Recombinant, His Tag

Recombinant human CRYAB protein, expressed in E.coli, is a non-glycosylated polypeptide chain comprising 183 amino acids (residues 1-175) with a molecular weight of 21.2kDa. An 8 amino acid histidine tag is fused to the C-terminus of the protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20017
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

CRYAB Mouse

Crystallin Alpha B Mouse Recombinant

Recombinant Mouse CRYAB, produced in E.Coli, is a non-glycosylated polypeptide chain comprising 175 amino acids, resulting in a molecular weight of 20 kDa. The protein is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20112
Source
Escherichia Coli.
Appearance
Colorless, sterile-filtered solution.

CRYBA4 Human

Crystallin Beta A4 Human Recombinant

Recombinant human CRYBA4, produced in E. coli, is a single polypeptide chain that lacks glycosylation. It consists of 216 amino acids (with amino acids 1 to 196 being present) and has a molecular weight of 24.5 kDa. The protein has a 20 amino acid His-tag attached to its N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20240
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

CRYBB1 Human

Crystallin Beta B1 Human Recombinant

Recombinant Human CRYBB1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 260 amino acids (with positions 1-252 being relevant) and has a molecular weight of 29.1 kDa. An 8-amino acid His-Tag is fused to the C-terminus of the CRYBB1 protein. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20340
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

CRYGC Human

Crystallin, Gamma C Human Recombinant

Recombinant human CRYGC, expressed in E. coli, is a single polypeptide chain with a molecular weight of 23.5 kDa. The protein comprises 198 amino acids, including a 24 amino acid His-tag at the N-terminus (1-174). Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20464
Source
E.coli.
Appearance
Clear, colorless solution, sterilized by filtration.

CRYGD Human

Crystallin, Gamma D Human Recombinant

Recombinant human CRYGD, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 194 amino acids (amino acids 1-174) with a molecular weight of 22.9 kDa. The protein features a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20570
Source
Escherichia Coli.
Appearance
The product is a sterile, colorless solution.

CRYGD Mouse

Crystallin, Gamma D Mouse Recombinant

CRYGD Mouse Recombinant, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 197 amino acids (1-174 a.a.) with a molecular mass of 23.5kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20642
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

CRYGN Human

Crystallin, Gamma N Human Recombinant

Recombinant human CRYGN, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 206 amino acids (1-182 a.a) with a molecular weight of 23.1 kDa. It features a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20761
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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.
Biological Properties

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.
Biological Functions

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.
Modes of Action

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.
Regulatory Mechanisms

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.
Applications

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.
Role in the Life Cycle

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.
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