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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 50 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana, Arabidopsis thaliana cell culture, Cicer arietinum, Nicotiana tabacum, Phaseolus vulgaris, Pisum sativm, Zea mays
CPN60A1 encodes a nuclear-encoded chloroplast chaperonin 60 alpha subunit that is synthesized with an N-terminal chloroplast transit peptide and accumulates predominantly in the chloroplast stroma, where it assembles with Cpn60 beta subunits into a type I chaperonin complex. Structurally, CPN60A1 belongs to the GroEL-like chaperonin family, with conserved ATPase and substrate-binding domains that support formation of large ring-shaped oligomers; in plants these oligomers are heterogeneous, containing both alpha and beta polypeptides within the same chaperonin particle. Functionally, the CPN60A1-containing chloroplast chaperonin uses ATP-dependent conformational cycling to prevent aggregation and promote folding/assembly of newly imported, newly synthesized, or stress-denatured chloroplast proteins, thereby supporting chloroplast biogenesis and proteostasis; genetic disruption of the dominant Cpn60 alpha subunit in Arabidopsis impairs plastid development and can cause severe developmental defects consistent with an essential housekeeping folding role in chloroplasts.
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: CH-CPN60A; chaperonin-60alpha; chaperonin-60alpha1; CHLOROPLAST CHAPERONIN 60ALPHA; CPN-60 alpha 1; Cpn60-A(2); Cpn60alpha1; SCHLEPPERLESS; SLP; T1E2.8; T1E2_8