Vector Labs Ab05121-23.0 Anti-Capsular polysaccharide [2016.3], Rabbit IgG, kappa (100 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: 2016.3
Synonyms: Capsular PS; meningococcal polysaccharide group C; serogroup C sialic acid containing capsular polysaccharides
Amount: 100 μg
Application Codes Clone: ELISA; FELISA; inhibition
Shipping Temperature: Wet Ice
Origin Pub PMID: 15589322
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: IgG3
Storage Temperature: Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement: This chimeric rabbit antibody was made using the variable domain sequences of the original Mouse IgG3 format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement: This antibody is specific for the α(2→9) sialic‑acid backbone of N. meningitidis's serogroup C capsular polysaccharide. Its basic pI (8.3–8.6) and longer IgG3 hinge suggest it approaches the backbone in a more extended, flexible orientation than Ab05119 [C2/655.7], one of our other anti–N. meningitidis group C capsular PS products. Its distinct CDR composition likewise implies a different paratope shape, so although both clones target the same motif, they likely bind from different angles or contact footprints. Functionally, this antibody shows ~30‑fold lower 50% binding affinity to OAc⁻ and ~10‑fold lower to MCPS.
Application Notes: The original antibody format (Mouse IgG3) was generated and evaluated. Its specificity was determined by FELISA. It exhibited a binding pattern of OAc⁻ >> MCPS, with 50% binding observed at approximately 0.1 µg/mL and >3 µg/mL, respectively, under the assay conditions. This indicates a strong preference for the de‑O‑acetylated serogroup C capsular polysaccharide. The original antibody's pI was measured to be in the range of 8.3–8.6 (García-Ojeda et al., 2000; PMID: 10603394). Surface plasmon resonance analysis indicated lower avidity with a preference for the OAc⁻ surface, as shown by greater concentration-dependent binding to OAc⁻; however, kinetic studies did not reflect this preference in dissociation half-lives. Furthermore, in inhibition experiments, it partially blocked the binding of conjugate vaccine immune sera to OAc⁻ surfaces, achieving less than 40% inhibition (García-Ojeda, 2004; PMID: 15155652).

Product Class:	Purified
Clone ID:	2016.3
Synonyms:	Capsular PS; meningococcal polysaccharide group C; serogroup C sialic acid containing capsular polysaccharides
Amount:	100 μg
Application Codes Clone:	ELISA; FELISA; inhibition
Shipping Temperature:	Wet Ice
Origin Pub PMID:	15589322
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	IgG3
Storage Temperature:	Store at 4⁰C for up to 3 months. For longer storage, aliquot and store at -20⁰C.
Chimeric Use Statement:	This chimeric rabbit antibody was made using the variable domain sequences of the original Mouse IgG3 format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement:	This antibody is specific for the α(2→9) sialic‑acid backbone of N. meningitidis's serogroup C capsular polysaccharide. Its basic pI (8.3–8.6) and longer IgG3 hinge suggest it approaches the backbone in a more extended, flexible orientation than Ab05119 [C2/655.7], one of our other anti–N. meningitidis group C capsular PS products. Its distinct CDR composition likewise implies a different paratope shape, so although both clones target the same motif, they likely bind from different angles or contact footprints. Functionally, this antibody shows ~30‑fold lower 50% binding affinity to OAc⁻ and ~10‑fold lower to MCPS.
Application Notes:	The original antibody format (Mouse IgG3) was generated and evaluated. Its specificity was determined by FELISA. It exhibited a binding pattern of OAc⁻ >> MCPS, with 50% binding observed at approximately 0.1 µg/mL and >3 µg/mL, respectively, under the assay conditions. This indicates a strong preference for the de‑O‑acetylated serogroup C capsular polysaccharide. The original antibody's pI was measured to be in the range of 8.3–8.6 (García-Ojeda et al., 2000; PMID: 10603394). Surface plasmon resonance analysis indicated lower avidity with a preference for the OAc⁻ surface, as shown by greater concentration-dependent binding to OAc⁻; however, kinetic studies did not reflect this preference in dissociation half-lives. Furthermore, in inhibition experiments, it partially blocked the binding of conjugate vaccine immune sera to OAc⁻ surfaces, achieving less than 40% inhibition (García-Ojeda, 2004; PMID: 15155652).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

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