FATA Antibody

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Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Made-to-order (14-16 weeks)
Synonyms
FATA antibody; FATA1 antibody; At3g25110 antibody; MJL12.5Oleoyl-acyl carrier protein thioesterase 1 antibody; chloroplastic antibody; EC 3.1.2.14 antibody; 18:0-acyl-carrier protein thioesterase antibody; 18:0-ACP thioesterase antibody; Acyl-[acyl-carrier-protein] hydrolase antibody
Target Names
FATA
Uniprot No.

Target Background

Function
FATA Antibody plays a crucial role in the termination of fatty acid synthesis during the de novo process. It exhibits high thioesterase activity towards oleoyl-ACP compared to other acyl-ACPs. Notably, its substrate preference follows the order: 18:1 > 18:0 > 16:1.
Gene References Into Functions
  1. Research in Arabidopsis has demonstrated that reduced expression of FatA thioesterases significantly impacts the oil content and fatty acid composition of seeds. PMID: 22002626
Database Links

KEGG: ath:AT3G25110

STRING: 3702.AT3G25110.1

UniGene: At.19907

Protein Families
Acyl-ACP thioesterase family
Subcellular Location
Plastid, chloroplast.

Q&A

Basic Questions

  • What are the key considerations in designing experiments for FATA antibody development?

    • Experimental design for FATA antibodies should account for antigen specificity, binding affinity, and structural stability. Techniques such as ELISA, Surface Plasmon Resonance (SPR), and immunoassays are essential for screening and characterizing antibodies. These methods help identify clones with optimal specificity and monitor changes during development .

  • How can computational tools be used to optimize FATA antibody design?

    • Computational approaches, including machine learning models like Generative Adversarial Networks (GANs) and diffusion probabilistic models, can generate antibody sequences with desirable properties. These tools simulate antibody-antigen interactions, predict binding affinities, and optimize developability attributes such as stability and low immunogenicity .

  • What methods are available to measure the pharmacokinetics of FATA antibodies?

    • Pharmacokinetics can be assessed using in vitro assays like SPR to measure FcRn binding kinetics and in vivo models such as humanized FcRn mouse models or non-human primates for clinical relevance. These methods evaluate half-life, clearance rates, and biodistribution .

  • What are the challenges in ensuring the specificity of FATA antibodies?

    • Specificity challenges include off-target binding and cross-reactivity. Approaches to address these include co-optimization of affinity and specificity using machine learning models or mutagenesis libraries to refine complementarity-determining regions (CDRs) .

  • How does the structure of FATA antibodies influence their function?

    • The functional efficacy of antibodies is largely determined by their variable regions (Fab) for antigen binding and constant regions (Fc) for immune modulation. Structural studies using X-ray crystallography or cryo-EM can provide insights into these interactions .

Advanced Research Questions

  • How can data inconsistencies in FATA antibody experiments be resolved?

    • Data inconsistencies may arise from variability in experimental conditions or biological systems. Strategies include standardizing protocols, using automated platforms to minimize human error, and employing independent validation across multiple laboratories .

  • What role does deep learning play in predicting the developability of FATA antibodies?

    • Deep learning models analyze large datasets of antibody sequences to predict properties like thermal stability, solubility, and aggregation propensity. These predictions guide the selection of candidates with optimal biophysical characteristics for further development .

  • How can FATA antibodies be optimized for antigen-specific targeting?

    • Optimization involves sequence-structure co-design using diffusion models, which allow iterative refinement of CDRs based on antigen 3D structures. This ensures high binding affinity while maintaining structural integrity .

  • What experimental approaches validate computationally designed FATA antibodies?

    • Validation involves expressing computationally designed sequences in mammalian cells, followed by purification and biophysical characterization (e.g., thermal stability, hydrophobicity). Comparative studies with marketed antibodies ensure reliability .

  • How do trade-offs between affinity and specificity affect therapeutic potential?

    • High-affinity antibodies may exhibit reduced specificity due to non-specific interactions. Machine learning models explore these trade-offs by identifying mutations that balance both properties along a Pareto frontier .

Methodological Insights

  • What are effective strategies for generating antigen-agnostic antibody libraries?

    • Antigen-agnostic libraries can be generated using deep learning algorithms trained on diverse antibody datasets. These libraries prioritize developability attributes such as expression yield and low aggregation risk over antigen specificity .

  • How can experimental reproducibility be ensured in FATA antibody research?

    • Reproducibility is enhanced by adopting automated systems for cloning, expression, and purification processes. Cross-validation with independent laboratories further confirms experimental findings .

  • What are the emerging trends in in silico antibody discovery?

    • Trends include integrating generative deep learning with molecular dynamics simulations to predict antibody-antigen interactions at atomic resolution. These methods accelerate discovery while reducing reliance on traditional hybridoma techniques .

  • How do linker chemistries affect the efficacy of antibody-drug conjugates (ADCs) involving FATA antibodies?

    • Linker stability influences drug release profiles and therapeutic index in ADCs. Studies focus on optimizing linker design to ensure selective cytotoxic payload delivery without compromising antibody integrity .

  • What are the limitations of current animal models in preclinical testing of FATA antibodies?

    • Standard animal models often fail to replicate human FcRn interactions accurately, leading to discrepancies in pharmacokinetic data. Humanized mouse models offer improved relevance but remain costly compared to traditional approaches .

Example Data Table: Comparison of GAN-Generated vs Marketed Antibodies

PropertyGAN-Generated AntibodiesMarketed Antibodies
Expression YieldHigherModerate
Thermal StabilityComparableComparable
HydrophobicityLowerModerate
Binding AffinityHighHigh
SpecificityOptimized via MLVariable

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