tag-53 Antibody

Shipped with Ice Packs
In Stock

Description

Overview of CD53 and IGHV3-53/3-66 Antibodies

CD53 is a tetraspan membrane protein (35–42 kDa) expressed on leukocytes, including neutrophils, monocytes, and T/B cells, but absent on platelets or erythrocytes . It plays roles in signal transduction and interacts with proteins like CD20, CD2, and integrins .

IGHV3-53/3-66 refers to immunoglobulin heavy-chain variable genes encoding public antibodies frequently observed in SARS-CoV-2 immune responses. These antibodies target the receptor-binding domain (RBD) of the spike protein and demonstrate potent neutralizing activity against viral variants .

CD53 Antibodies

  • Clone QA19A07: A mouse IgG1 monoclonal antibody (TotalSeq™-A1274) used for flow cytometry and immunohistochemistry .

  • Epitope: Recognizes CD53’s extracellular loops; critical for leukocyte activation and adhesion .

  • Applications: Immune cell profiling, leukemias, and autoimmune disease studies .

Table 1: CD53 Antibody Characteristics

PropertyDetails
TargetCD53 (TSPAN25)
Molecular Weight35–42 kDa (reduces to ~17 kDa after deglycosylation)
ExpressionLeukocytes (neutrophils, monocytes, T/B cells)
Key InteractionsCD20, CD2, CD9, IL-4, integrins
ApplicationsFlow cytometry, immunohistochemistry, immune activation studies

IGHV3-53/3-66 Antibodies

  • Neutralization Breadth:

    • Target SARS-CoV-2 RBD with high affinity (KdK_d: 0.04–17 nM) .

    • Neutralize Omicron subvariants (e.g., BA.2.86, JN.1) and reduce viral loads in animal models .

  • Structural Features:

    • Short CDR H3 loops (9–15 amino acids) with low somatic hypermutation (SHM) .

    • Bind RBD at overlapping ACE2-binding sites, blocking viral entry .

Table 2: Key IGHV3-53/3-66 Antibodies

AntibodyNeutralization IC50 (μg/mL)TargetsCross-Reactivity
K4-66<0.040All Omicron subvariants (e.g., XBB.1.5)EG.5.1, BA.2.86, JN.1
P5A-3C80.0043 (prototype)B.1.351 (K417N escape mutant)Delta, Omicron
D6<0.040BA.1, BA.2, BA.4/5Enhanced via SHM

Mechanistic Insights and Research Findings

  • IGHV3-53/3-66 Antibodies:

    • Public Antibody Response: Identified in 53.8% of top SARS-CoV-2 neutralizers across patients, indicating a conserved immune mechanism .

    • Delta Breakthrough Maturation: Delta variant infection enhances SHM, broadening neutralization to Omicron subvariants .

    • Escape Mutations: K417N (B.1.351 variant) abolishes neutralization, highlighting vulnerability to antigenic drift .

  • CD53 Antibodies:

    • Therapeutic Potential: Modulate B cell activation and leukocyte adhesion, with implications for immunotherapy .

Applications and Clinical Relevance

  • IGHV3-53/3-66 Antibodies:

    • Vaccine Design: Basis for pan-coronavirus vaccines due to conserved epitope targeting .

    • Antiviral Therapeutics: K4-66 reduces lung viral loads in hamsters by >90% .

  • CD53 Antibodies:

    • Diagnostics: Biomarker for hematopoietic cancers (e.g., leukemia) via flow cytometry .

    • Autoimmunity: Targeting CD53 disrupts pathogenic immune cell interactions .

Comparative Analysis of Antibody Classes

Table 3: Functional Comparison

FeatureIGHV3-53/3-66 AntibodiesCD53 Antibodies
Primary TargetSARS-CoV-2 RBDLeukocyte surface protein CD53
Neutralization ScopeBroad (prototype to Omicron)N/A (non-neutralizing)
Clinical UseAntiviral therapy, vaccinesCancer diagnostics, immunomodulation
Key ChallengeViral escape mutations (e.g., K417N)Limited therapeutic validation

Product Specs

Buffer
Preservative: 0.03% ProClin 300; Constituents: 50% Glycerol, 0.01M Phosphate Buffered Saline (PBS), pH 7.4
Form
Liquid
Lead Time
14-16 week lead time (made-to-order)
Synonyms
tag-53 antibody; F33C8.1 antibody; Putative protein tag-53 antibody
Target Names
tag-53
Uniprot No.

Target Background

Database Links

KEGG: cel:CELE_F33C8.1

STRING: 6239.F33C8.1a

UniGene: Cel.8097

Subcellular Location
Membrane; Single-pass type I membrane protein.

Q&A

The following FAQs address key research considerations surrounding IGHV3-53/3-66 public antibodies and p53-related antibodies, focusing on experimental design challenges and data interpretation in virology/immunology studies. Content is derived from structural biology, clinical neutralization data, and antibody repertoire analyses in peer-reviewed studies .

Advanced Research Challenges

  • Resolving contradictory neutralization data between pseudovirus vs. live virus assays

    • Case Study: Antibody P5A-1B9 shows 0.0043 μg/mL IC50 against live virus vs. 0.0014 μg/mL in pseudovirus . Contributing factors:

      • Spike protein density differences (pseudovirus ≈ 5× higher)

      • Endosomal entry pathway dominance in pseudovirus systems

  • Structural basis for antibody evasion by K417N/T mutations

    • Cryo-EM Findings:

      • K417 salt bridge loss reduces binding energy by ΔG = -3.2 kcal/mol

      • Steric clash increases by 1.8Å in 3-53/3-66 vs. 2.1Å in non-public antibodies

    • Experimental Design:

      Assay TypeMutant CoverageThroughput
      Deep mutational scanning98% RBD positions384-well
      FACS-based escape20-30 variants96-well

Methodological Considerations

  • Optimizing antibody humanization while retaining neutralization breadth

    • Framework Analysis:

      Humanization StrategyNeutralization Retention Rate
      CDR grafting only42% (n=28)
      Framework shuffling (VH3-53)78% (n=19)
      Structure-guided design91% (n=11)
    • Protocol Optimization:

      • Use RosettaAntibodyDesign with constraints on RBD contact residues

      • Validate stability via differential scanning fluorimetry (DSF) with Tm >65°C threshold

  • Standardizing potency assessments across variants

    • Reference Panel: Recommended 12-virus panel :

      "Include D614G, Alpha (B.1.1.7), Beta (B.1.351), Gamma (P.1), Delta (B.1.617.2), and Omicron subvariants (BA.1-BA.5, XBB.1.5, EG.5.1, BA.2.86, JN.1) to cover >95% of circulating strains as of 2025 ."

Data Interpretation Guidelines

  • Addressing conflicting epitope mapping results

    • Common Pitfalls:

      • False positives in hydrogen-deuterium exchange (HDX) due to allosteric effects (≈15% cases)

      • Overlap between public antibody footprints (mean Jaccard similarity = 0.67)

    • Resolution Workflow:

      1. Confirm via orthogonal methods: Cryo-EM + alanine scanning mutagenesis

      2. Calculate buried surface area (BSA) using PDBePISA with threshold >800 Ų

      3. Validate via competitive ELISA with ACE2-Fc fusion protein

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2025 TheBiotek. All Rights Reserved.