The At3g26430 Antibody is a polyclonal rabbit-derived antibody specifically targeting the recombinant protein encoded by the At3g26430 gene in Arabidopsis thaliana. This antibody is utilized for immunological detection and biochemical studies of the At3g26430 protein, which has been characterized as a serine hydrolase with lipase activity .
Substrate Preference: Activity increases with longer hydrocarbon chains (PNPA < PNPB < PNPP) .
Inhibition Profile: PMSF blocks catalysis, while neostigmine (a cholinesterase inhibitor) has no effect, confirming lipase-specific activity .
Bacterial Production: Expressed in E. coli as insoluble inclusion bodies, with a minor soluble fraction .
Immunoblotting: Anti-His antibodies confirmed expression in E. coli, while the At3g26430 Antibody is used for plant-derived protein detection .
Lipase Activity: Hydrolysis of triglycerides and esters was confirmed in both bacterial and plant-derived fractions .
Cholinesterase Activity: No hydrolysis of acetylthiocholine (ATCh) or butyrylthiocholine (BtCh) was observed, ruling out acetylcholinesterase-like function .
The At3g26430 protein’s lipase activity suggests involvement in lipid metabolism, potentially regulating fatty acid synthesis or degradation in A. thaliana . This aligns with its classification as a GDSL-like lipase, a family known for diverse enzymatic roles in plants .
The antibody enables precise quantification of At3g26430 in plant tissues, facilitating studies on:
Developmental Regulation: Expression patterns during growth stages.
Stress Responses: Lipid remodeling under environmental stressors.
While unrelated to therapeutic antibodies (e.g., nipocalimab or anti-drug antibodies ), the At3g26430 Antibody shares structural and functional parallels with plant-targeted reagents:
Specificity: No data on cross-reactivity with homologs in other plant species.
Functional Insights: Further studies are needed to link At3g26430 activity to phenotypic outcomes in A. thaliana.