CRYGN Human
Crystallin, Gamma N Human Recombinant
Cat. No.
BT20761
Source
E.coli.
Synonyms
Gamma-crystallin N, Gamma-N-crystallin, CRYGN.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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In Stock 
Description
CRYGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-182 a.a) and having a molecular mass of 23.1kDa.
CRYGN is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
CRYGN is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Crystallin gamma N (CRYGN), a member of the Crystallins family, is a protein found in the vertebrate eye lens. Crystallins, including CRYGN, are essential for maintaining the lens's transparency and refractive index, which are crucial for vision. Unlike other crystallins, CRYGN possesses both beta and gamma crystallin protein motifs. Its expression is regulated differently after early development, and it plays a role in cataract formation, which can be caused by age-related protein degradation or genetic mutations.
Description
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.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
A solution of CRYGN protein (1 mg/ml) in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity level exceeding 90%, as determined by SDS-PAGE analysis.
Synonyms
Gamma-crystallin N, Gamma-N-crystallin, CRYGN.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAQRSG KITLYEGKHF TGQKLEVFGD CDNFQDRGFM NRVNSIHVES GAWVCFNHPD FRGQQFILEH GDYPDFFRWN SHSDHMGSCR PVGMHGEHFR LEIFEGCNFT GQCLEFLEDS PFLQSRGWVK NCVNTIKVYG DGAAWSPRSF GAEDFQLSSS LQSDQGPEEA TTKPATTQPP FLTANL.
Product Science Overview
Classification and Structure
Function and Importance
Genetic and Clinical Relevance
CRYGN is a protein-coding gene, and mutations in this gene can be associated with various conditions, including familial hypertrophic cardiomyopathy and cataracts . These mutations can lead to protein misfolding or aggregation, disrupting the transparency of the lens and leading to vision impairment .
Recombinant CRYGN
Recombinant CRYGN is produced using genetic engineering techniques, typically expressed in E. coli . This recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification . The recombinant form is used extensively in research to study the protein’s structure, function, and role in disease.
Applications in Research
Recombinant CRYGN is valuable in various research applications, including:
- Structural studies: Understanding the protein’s 3D structure and how mutations affect its stability and function.
- Disease modeling: Investigating how mutations in CRYGN contribute to cataract formation and other related conditions.
- Drug development: Screening for compounds that can stabilize CRYGN and prevent aggregation, potentially leading to new treatments for cataracts .
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