Customize FRS8 Antibody

Description

Key Features of FRMD8 Antibodies

Attribute	Description
Target	FRMD8 protein (gene aliases: Bili, Band4.1 inhibitor LRP interactor)
Applications	Western blot, immunocytochemistry, immunohistochemistry, ELISA
Species Specificity	Primarily studied in humans and mice (cross-reactivity depends on epitope)
Forms	Polyclonal, monoclonal (e.g., tissue culture supernatant, purified IgG)

Antibody Structure

FRMD8 antibodies follow the classic immunoglobulin structure:

Heavy Chains: Determine isotype (IgG, IgM, etc.) and Fc-mediated effector functions .
Light Chains: Contribute to antigen-binding specificity via complementarity-determining regions (CDRs) .
Variable Regions: CDRs drive binding to FRMD8 epitopes, while framework regions (FRs) maintain structural stability .

Somatic Hypermutation in CDRs

During affinity maturation, FRMD8-specific antibodies undergo somatic hypermutation in CDRs to enhance antigen binding. For example:

Mutation Site	Impact on Binding	Example
CDR2	Enhanced affinity via amino acid substitutions (e.g., Ser→Ala, Gly→Tyr)	H8L0 variant (K<sub>D</sub> = 1.75E+06)
CDR3	Insertions/deletions alter epitope recognition	H11L0 variant (deletion S)

Diagnostic and Experimental Uses

FRMD8 antibodies are employed in:

Western Blotting: Detection of FRMD8 in cell lysates or tissue homogenates .
Immunohistochemistry (IHC): Localization of FRMD8 in tumor or inflammatory tissue sections .
ELISA: Quantification of FRMD8 levels in biological fluids (e.g., serum, culture supernatant) .

Therapeutic Potential

While FRMD8 antibodies are not yet clinically approved, insights from analogous systems (e.g., anti-EDA antibodies) highlight potential strategies:

Strategy	Mechanism	Example
Targeting Tumor Angiogenesis	Inhibiting FRMD8’s role in endothelial cell adhesion and migration	Anti-EDA antibodies (K<sub>D</sub> = 3.1–17 nM)
Antibody Engineering	Humanizing rodent antibodies for reduced immunogenicity	DT40 cell-based affinity maturation

Production and Purification

Challenge	Solution
Low Affinity	Affinity maturation via B cell-based systems (e.g., DT40 cells)
Cross-Reactivity	Immunopurification using antigen-bound agarose to remove non-specific IgG
Glycosylation Variability	Protein A/G chromatography to isolate homogeneous IgG fractions

Stability and Specificity

Physical Stability: FRMD8 antibodies may require stabilization via disulfide bonds or glycosylation optimization .
Epitope-Specific Binding: Avoid F(ab)<sub>2</sub> fragments if Fc-mediated effector functions (e.g., ADCC) are required .

Table 1: FRMD8 Antibody Forms and Applications

Antibody Form	Description	Use Case
Whole Antiserum	Contains non-specific host proteins	Initial screening for FRMD8
IgG Fraction	Purified via ion exchange chromatography	High-affinity applications
F(ab)<sub>2</sub> Fragment	Divalent, Fc-free fragment	Tissue staining, reduced background

Table 2: Affinity Maturation Outcomes for Analogous Antibodies

Clone	K<sub>D</sub> (M)	CDR Mutation	Fold Improvement
H8L0	1.75E+06	H-CDR2:S→A, G→S	2.29E-09
H9L0	2.66E+06	H-CDR2:G→Y	9.1-fold
F8	3.1E-09	Humanized scFv	8.2-fold cytotoxicity

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

FRS8 antibody; At1g80010 antibody; F18B13.10 antibody; F19K16.2Protein FAR1-RELATED SEQUENCE 8 antibody

Target Names

FRS8

Uniprot No.

Q9S793

Target Background

Function

FRS8 Antibody targets a putative transcription activator involved in regulating light control of development. It may play a role in controlling flowering time.

Database Links

KEGG: ath:AT1G80010

STRING: 3702.AT1G80010.1

UniGene: At.52575

Protein Families

FHY3/FAR1 family

Subcellular Location

Nucleus. Note=The nuclear localization is independent of the light treatment.

Tissue Specificity

Expressed in hypocotyls, rosette and cauline leaves, inflorescences stems, flowers and siliques.

Q&A

Here’s a structured collection of FAQs tailored for academic researchers working with FRS8 antibodies, synthesized from peer-reviewed methodologies and experimental data:

What experimental factors influence FRS8 antibody performance in mechanistic studies?

Key variables:

Factor	Optimization Strategy	Supporting Data
Epitope stability	Pre-treat lysates with protease inhibitors	Nuclear extracts show stronger IRF8 signals than whole-cell lysates
Cross-reactivity	Validate across species (e.g., Arabidopsis vs. human homologs )	Plant FRS8 antibodies (e.g., CSB-PA882786XA01DOA ) lack human reactivity
Assay compatibility	Use HRP-conjugated secondary antibodies for IHC	Anti-Mouse HRP-DAB staining validated in tonsil tissue

How to address contradictory results in FRS8 expression levels across studies?

Advanced troubleshooting:

Context-dependent regulation: IRF8 (a related transcription factor) shows variable expression in malignant vs. normal B cells . Apply similar stratification for FRS8.
Quantitative normalization: Use Simple Western™ for precise quantification (0.5 mg/mL lysate loading ).
Multi-omics correlation: Cross-validate with RNA-seq (IRF8 mRNA-CD20 protein correlations provide a template).

What are robust experimental designs for studying FRS8 in gene regulatory networks?

Integrated workflow:

CRISPR screening: Identify FRS8-interacting partners (e.g., adapt MS4A1/CD20 screening protocols ).
Functional assays:
- ADCP/ADCC: Adapt Rituximab-based phagocytosis assays with FRS8-modulated cells.
- ChIP-seq: Optimize chromatin shearing (IRF8 studies used 25 µg nuclear extracts ).

How to optimize FRS8 detection in low-abundance systems?

Sensitivity enhancement:

Signal amplification: Combine tyramide-based systems with 15 µg/mL primary antibody .
Pre-analytical processing: For tissues, use immersion fixation over perfusion to preserve epitopes.
Multiplexing: Pair with flow cytometry (CD20 surface markers ) to contextualize FRS8 activity.

What computational tools complement FRS8 antibody-based research?

Emerging integration:

AI-driven design: Apply RFdiffusion models to predict FRS8-binding interfaces.
Structural validation: Use cryo-EM (as in C. difficile toxin studies ) for conformational epitope mapping.

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FRS8 Antibody