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Agrisera
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Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
For reconstitution add 200 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana, Hordeum vulgare
HSP18.5 encodes a small heat shock protein of the HSP20 family that localizes predominantly to the cytoplasmic/nuclear compartment, consistent with a role in cellular proteostasis under stress. The protein is organized around the conserved alpha-crystallin domain (a beta-sheet rich core typical of small heat shock proteins) flanked by flexible, largely unstructured N- and C-terminal regions; these terminal arms are highly accessible and contribute to substrate interactions. Biophysically, HSP18.5 can exist as low-order assemblies (notably dimers) with dynamic subunit exchange, and it can form higher-molecular-weight complexes upon binding partially unfolded client proteins. Functionally, HSP18.5 acts as an ATP-independent molecular chaperone that binds destabilized proteins during heat and other proteotoxic stresses to suppress irreversible aggregation and maintain substrates in a refolding-competent state for downstream recovery by ATP-dependent chaperone systems.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
蛋白别名: 18.5 kDa class IV heat shock protein; 18.5 kDa heat shock protein; AT2G19310; AtHsp18.5; Class IV heat shock protein 18.5; F27F23.11; HSP20-like chaperones superfamily protein