CRYBB1 Human
Crystallin Beta B1 Human Recombinant
Cat. No.
BT20340
Source
Escherichia Coli.
Synonyms
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% 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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Description
CRYBB1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (1-252 a.a.) and having a molecular mass of 29.1 kDa.
The CRYBB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
The CRYBB1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
Crystallins are the primary structural proteins found in the lens of vertebrate eyes. They play a crucial role in maintaining the lens's transparency and refractive index, which are essential for vision. Crystallins are categorized into three protein families: α, β, and γ. During development, the central fiber cells of the lens lose their nuclei. Consequently, the crystallins produced before this process are maintained throughout an organism's lifespan, making them exceptionally stable proteins. CRYBB1, a member of the beta basic group of crystallins, undergoes significant cleavage at its N-terminal extension as the lens matures.
Description
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.
Physical Appearance
A clear solution that has been sterilized through filtration.
Formulation
The CRYBB1 solution is provided at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8), 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To further enhance stability during long-term storage, consider adding a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing of the product should be avoided.
Purity
Purity is determined by SDS-PAGE analysis and is consistently greater than 90.0%.
Synonyms
EC 1.17.4.1, RR2M, Beta-B1 crystallin, CATCN3.
Source
Escherichia Coli.
Amino Acid Sequence
MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PKRSHHHHHH.
Product Science Overview
Structure and Function
Crystallin Beta B1 is a highly stable protein due to its role in the lens, where it is synthesized and retained throughout life. This stability is essential because the central fiber cells of the lens lose their nuclei during development, meaning they cannot replace damaged proteins . The CRYBB1 protein undergoes extensive cleavage at its N-terminal extension during lens maturation .
Recombinant Human CRYBB1
Recombinant human CRYBB1 protein is produced using Escherichia coli (E. coli) expression systems. The recombinant protein typically includes a C-terminal His-tag to facilitate purification . The amino acid sequence of the recombinant CRYBB1 corresponds to the first 252 amino acids of the human protein .
Applications
Storage and Stability
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