Vector Labs Ab05150-10.0 Anti-MenX capsular polysaccharide [MenX.01], Human IgG1, kappa (100 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: MenX.01
Synonyms: Neisseria meningitidis serogroup X capsular polysaccharide; MenX-CPS
Amount: 100 μg
Application Codes Clone: ELISA; SPR; WB; STD-NMR; ITC; Neutralization; Crystallography
Shipping Temperature: Wet Ice
Origin Pub PMID: 34722634
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: IgG1
Storage Temperature: Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement: This chimeric human antibody was made using the variable domain sequences of the original Mouse IgG1 format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement: This antibody is specific for the capsular polysaccharide of serogroup X of Neisseria meningitidis. The epitope was shown to be contained within five to six α-(1–4) phosphodiester N-acetylglucosamine-4-phosphate repeating units. It exhibited no cross-reactivity with Neisseria meningitidis serogroup A polysaccharide (MenA-PS), Group B Streptococcus type II polysaccharide (GBS-PSII), or the CRM197 carrier protein.
Application Notes: The original antibody format (mouse IgG1, kappa) was generated, and its specificity was verified using ELISA, demonstrating specific binding to MenX capsular polysaccharide (CPS) with no cross-reactivity to MenA-PS, GBS-PSII, or CRM197 protein alone. It was used in competitive ELISA with oligosaccharide (OS) fragments (DP5.5–40), showing full inhibition of CPS binding at DP5.5, indicating the minimal epitope. The antibody exhibited bactericidal activity in the rabbit serum bactericidal assay (rSBA) with a titer of 1,024 at 0.98 µg/ml against MenX strain Z9516. Surface plasmon resonance (SPR) analysis revealed a submicromolar affinity (Kd ≈ 0.32 µM) to MenX-CRM197 conjugate, with fast on/off rates. STD-NMR with a DP7 fragment identified strong interactions involving H-1 and H-4 protons near phosphodiester bridges. Isothermal titration calorimetry (ITC) confirmed entropically driven binding with Kd values of ~2–3 µM for DP5.5–7 and ~0.3 µM for DP15. Western blot/immunoblot confirmed specific detection of MenX-CRM197 conjugate bands. A Fab version of this antibody was generated and tested for functionality and binding in ELISA, confirming specific recognition of MenX CPS. SPR analysis of Fab showed a comparable affinity (Kd ≈ 0.54 µM) to the full mAb. An IgG2a recFab-His format of the antibody was constructed and crystallized, yielding a 2.16 Å resolution structure (PDB: 7OO2), which was used for in silico docking with a DP6 OS, revealing hydrogen bonds, salt bridges, and hydrophobic interactions involving all six repeating units (Pietri et al., 2021; PMID: 34722634). The findings on the minimal epitope (5–6 repeating units) were supported by a separate study on synthetic MenX-related phosphooligosaccharides, where trimeric and longer (avDP12) conjugates elicited anti-MenX IgG and bactericidal activity, though weaker than natural polysaccharide conjugates (Khatuntseva et al., 2025; DOI: 10.3390/molecules30153068).

Product Class:	Purified
Clone ID:	MenX.01
Synonyms:	Neisseria meningitidis serogroup X capsular polysaccharide; MenX-CPS
Amount:	100 μg
Application Codes Clone:	ELISA; SPR; WB; STD-NMR; ITC; Neutralization; Crystallography
Shipping Temperature:	Wet Ice
Origin Pub PMID:	34722634
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	IgG1
Storage Temperature:	Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement:	This chimeric human antibody was made using the variable domain sequences of the original Mouse IgG1 format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement:	This antibody is specific for the capsular polysaccharide of serogroup X of Neisseria meningitidis. The epitope was shown to be contained within five to six α-(1–4) phosphodiester N-acetylglucosamine-4-phosphate repeating units. It exhibited no cross-reactivity with Neisseria meningitidis serogroup A polysaccharide (MenA-PS), Group B Streptococcus type II polysaccharide (GBS-PSII), or the CRM197 carrier protein.
Application Notes:	The original antibody format (mouse IgG1, kappa) was generated, and its specificity was verified using ELISA, demonstrating specific binding to MenX capsular polysaccharide (CPS) with no cross-reactivity to MenA-PS, GBS-PSII, or CRM197 protein alone. It was used in competitive ELISA with oligosaccharide (OS) fragments (DP5.5–40), showing full inhibition of CPS binding at DP5.5, indicating the minimal epitope. The antibody exhibited bactericidal activity in the rabbit serum bactericidal assay (rSBA) with a titer of 1,024 at 0.98 µg/ml against MenX strain Z9516. Surface plasmon resonance (SPR) analysis revealed a submicromolar affinity (Kd ≈ 0.32 µM) to MenX-CRM197 conjugate, with fast on/off rates. STD-NMR with a DP7 fragment identified strong interactions involving H-1 and H-4 protons near phosphodiester bridges. Isothermal titration calorimetry (ITC) confirmed entropically driven binding with Kd values of ~2–3 µM for DP5.5–7 and ~0.3 µM for DP15. Western blot/immunoblot confirmed specific detection of MenX-CRM197 conjugate bands. A Fab version of this antibody was generated and tested for functionality and binding in ELISA, confirming specific recognition of MenX CPS. SPR analysis of Fab showed a comparable affinity (Kd ≈ 0.54 µM) to the full mAb. An IgG2a recFab-His format of the antibody was constructed and crystallized, yielding a 2.16 Å resolution structure (PDB: 7OO2), which was used for in silico docking with a DP6 OS, revealing hydrogen bonds, salt bridges, and hydrophobic interactions involving all six repeating units (Pietri et al., 2021; PMID: 34722634). The findings on the minimal epitope (5–6 repeating units) were supported by a separate study on synthetic MenX-related phosphooligosaccharides, where trimeric and longer (avDP12) conjugates elicited anti-MenX IgG and bactericidal activity, though weaker than natural polysaccharide conjugates (Khatuntseva et al., 2025; DOI: 10.3390/molecules30153068).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

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