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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: Synechocystis PCC 6803
DnaK2 encodes a canonical bacterial Hsp70-family molecular chaperone that is predominantly cytosolic in cyanobacteria and is expressed as a soluble ~70 kDa protein; like other DnaK proteins, it is organized into an N-terminal ATPase (nucleotide-binding) domain linked via a conserved flexible interdomain connector to a C-terminal substrate-binding domain capped by a helical "lid" that helps stabilize bound client polypeptides. In the cyanobacteria Synechocystis sp. PCC 6803 and Synechococcus elongatus PCC 7942, DnaK2 is the principal stress-responsive DnaK paralog and is essential for viability, consistent with a central role in proteostasis under both basal and stress conditions. Functionally, DnaK2 cooperates with J-domain co-chaperones and the nucleotide-exchange factor GrpE to bind exposed hydrophobic segments on nascent, misfolded, or stress-denatured proteins, using ATP-driven cycling to prevent aggregation and promote productive folding and recovery after heat and other environmental stresses. Beyond general protein quality control, DnaK2 also contributes to regulation of the heat-shock program in S. elongatus by participating in a negative-feedback loop that dampens Hik2-Rre1 two-component-system-dependent stress transcription, thereby helping restore homeostasis after thermal or redox perturbation.
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: chloroplast heat shock protein 70-2; cpHsc70-2; HEAT SHOCK PROTEIN 70-7; HSC70-7; HSP70-7; K9P8.5; K9P8_5