Recombinant Human Anti-S. aureus Alpha-hemolysin Antibody (LTM14)

CAT#: PABZ-177

Recombinant Human Antibody (LTM14) is capable of binding to S. aureus Alpha-hemolysin , expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-S. aureus Alpha-hemolysin mAb and CH1-3 region of human IgG and a light chain (LC) encoding VL from anti-S. aureus Alpha-hemolysin proteins mAb and CL of human kappa light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. The epitope of LTM14 is centered on α-hemolysin residue R66, which has been implicated in binding to the eukaryotic membrane.

Specifications

  • Immunogen
  • S. aureus Alpha-hemolysin
  • Host Species
  • Human
  • Derivation
  • Human
  • Type
  • IgG
  • Specificity
  • Tested positive against native S. aureus Alpha-hemolysin
  • Species Reactivity
  • S. aureus
  • Clone
  • LTM14
  • Applications
  • ELISA Assay-Dependent
    Neut Assay-Dependent
    Block Assay-Dependent
    FuncS 0.3-30 mg/kg

Product Property

  • Purity
  • >95% by SDS-PAGE and HPLC analysis
  • Storage
  • Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing of samples.

Applications

  • Application Notes
  • The antibody LTM14 has been reported in applications of ELISA, Neut, Block, FuncS. It's recommended that the optimal antibody concentration, dilution, incubition time etc. are best to be carefully titrated in specific assays.
    FuncS: A reported dose of the antibody LTM14 in a mouse model of S. aureus pneumonia.

Target

  • Alternative Names
  • Alpha-hemolysin
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Enhanced Experimental Flexibility
The availability of various conjugation options has proved beneficial, facilitating its adaptation across diverse assay formats, from ELISAs to functional blocking studies. This flexibility enhances our experimental design possibilities and robustness.
Breast cancer biomarkers at key points during disease progression
Essential for Pathogen Research
This antibody has become central to our investigations into the role of alpha-hemolysin in S. aureus pathogenicity. Its ability to engage specifically with this virulence factor supports clear insights and accurate data in our research efforts.
Breast cancer biomarkers at key points during disease progression
Advancing Infection Studies
By using this antibody, our understanding of S. aureus mechanisms in infections has deepened, supporting the development of targeted strategies to mitigate bacterial virulence, which is a crucial focus of our work.

Q&As

  1. From which host is this antibody derived?

    A: This antibody is of human origin. Its construction from human frameworks ensures compatibility in various assay systems, reducing the likelihood of cross-reactivity and improving specificity.

  2. How specific is this antibody to alpha-hemolysin?

    A: The antibody specifically targets the alpha-hemolysin of S. aureus, focusing on the epitope centered around residue R66. This precise targeting is crucial for accurately studying protein interactions and infection mechanisms in S. aureus research.

  3. Are there specific diseases this antibody is used to study?

    A: It is crucial for studying conditions related to S. aureus virulence, including its role in pneumonia and skin infections, providing insights into disease progression and potential therapeutic targets.

View the frequently asked questions answered by Creative Biolabs Support.

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Downloadable Resources

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Product Notes

This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:

• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production

See more details about Hi-Affi™ recombinant antibody benefits.

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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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