Recombinant Human CRYbB2 protein

HSP90AB1. a member of the heat shock protein 90 (HSP90) family, is a molecular chaperone critical for maintaining cellular homeostasis under stress conditions. It plays a central role in folding, stabilizing, and activating client proteins, many of which are involved in signal transduction, cell cycle regulation, and stress response. Unlike its isoform HSP90AA1. HSP90AB1 (also known as HSP90β) is constitutively expressed and contributes to basal cellular functions, even in non-stressed environments. Structurally, it contains three domains: an N-terminal ATP-binding domain, a middle domain for client protein interaction, and a C-terminal dimerization domain.

Recombinant HSP90AB1 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. This allows large-scale production of the purified protein for research and therapeutic applications. The recombinant form retains its functional properties, including ATPase activity and client protein-binding capacity, making it invaluable for studying HSP90-mediated pathways, drug screening, and structural biology. Its applications extend to cancer research, as HSP90AB1 overexpression is linked to tumor progression, drug resistance, and poor prognosis. Inhibitors targeting HSP90 (e.g., geldanamycin derivatives, 17-AAG) are under investigation for anticancer therapies.

Additionally, HSP90AB1 is implicated in neurodegenerative diseases, inflammation, and infection, highlighting its broad biomedical relevance. Recombinant HSP90AB1 serves as a tool to explore these roles and develop targeted therapies, emphasizing its dual utility in basic science and translational medicine.

CRYBB2 (β-crystallin B2) is a member of the β/γ-crystallin superfamily, primarily expressed in the vertebrate eye lens. Encoded by the *CRYBB2* gene located on chromosome 22 in humans, it contributes to lens transparency and refractive properties by forming structural components of crystallins, which account for ~90% of lens proteins. β-crystallins, including CRYBB2. adopt a conserved two-domain "Greek key" fold, enabling tight packing and stability critical for maintaining lens integrity over decades. They typically form hetero- or homo-oligomers, with CRYBB2 interacting with other β-crystallins (e.g., CRYBB1. CRYBB3) to regulate solubility and prevent aggregation.

Mutations in *CRYBB2* are linked to congenital cataracts, a leading cause of childhood blindness. Over 20 pathogenic variants (e.g., Q155X, G220W) disrupt protein folding, solubility, or interactions, promoting light-scattering aggregates. These autosomal dominant or recessive mutations highlight CRYBB2's structural sensitivity and its role in lens homeostasis.

Recombinant CRYBB2 protein is produced via bacterial (e.g., *E. coli*) or mammalian expression systems for functional studies. Its production enables analysis of folding kinetics, aggregation mechanisms, and mutational effects in vitro. Researchers use techniques like X-ray crystallography, CD spectroscopy, and thermal stability assays to probe structure-function relationships. Recombinant CRYBB2 also aids in screening anti-cataract compounds and developing gene therapies. Despite challenges in expressing full-length soluble protein due to its aggregation-prone nature, advancements in fusion tags (e.g., His-tag) and refolding protocols have improved yields. Current studies focus on understanding CRYBB2's role in age-related cataracts and its potential as a therapeutic target, bridging basic research and clinical applications.