Vector Labs Ab04119-23.0 Anti-hapten 5 [17E8], Rabbit IgG, kappa (100 μg) Centrifuge Bundle Savings at Sycamore Life Sciences

Description

Product Class: Purified
Clone ID: 17E8
Synonyms: Noracine phosphonate; Norleucine phenyl phosphonate analog 1; Diphenyl [1-(1-N-Succinylamino)pentyl]phosphonate; Phosphonate transition state analog (hapten)
Amount: 100 μg
Application Codes Clone: ELISA; Catalytic assays; Crystallization
Shipping Temperature: Wet Ice
Origin Pub PMID: 8066444
Buffer Composition: PBS with 0.02% Proclin 300.
Original Format: IgG2b
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 IgG2b format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement: This antibody is specific for norleucine and methionine phenyl esters enantiomers that possess the natural S configuration (L) at the α-carbon.
Application Notes: This antibody efficiently catalyzes the hydrolysis of N-formyl norleucine phenyl ester and N-formyl methionine phenyl ester, with a preference for N-formyl esters over N-acetyl esters while demonstrating a superior catalytic activity for ester hydrolysis compared to other catalytic antibodies. The catalytic efficiency is influenced by the structural dissimilarity of the substrate to the antigen at specific positions. Notably, the original format of this antibody (mouse IgG2b) exhibits a higher affinity for ester substrates with norleucine side chains than methionine side chains. This original antibody's catalytic activity showed a bell-shaped pH dependence, reaching its maximum at pH 9.5. This pH optimum is attributed to the specific ionizable groups in the antibody's active site, contributing to efficient catalysis. Importantly, this antibody does not display significant product inhibition in kinetics experiments; although weak product inhibition is observed at higher conversion levels, it does not affect the initial rate measurements. Mechanistic studies suggest that this antibody likely forms a potentially rate-limiting covalent acyl intermediate during catalysis, supported by evidence from hydroxylamine partitioning studies (Guo et al., 1994). Crystallization of the Fab-5 complex of this antibody has been accomplished. The structure showed that it has similar active site features to natural triad-based hydrolases. Additionally, the structure showed that hapten five is buried deeply in the antigen-combining site, and there are separate and well-defined binding pockets for the phenyl group and n-butyl side chain of hapten 5 (Zhou et al., 1994; PMID: 8066444) (Wade and Scanlan, 1996).

Product Class:	Purified
Clone ID:	17E8
Synonyms:	Noracine phosphonate; Norleucine phenyl phosphonate analog 1; Diphenyl [1-(1-N-Succinylamino)pentyl]phosphonate; Phosphonate transition state analog (hapten)
Amount:	100 μg
Application Codes Clone:	ELISA; Catalytic assays; Crystallization
Shipping Temperature:	Wet Ice
Origin Pub PMID:	8066444
Buffer Composition:	PBS with 0.02% Proclin 300.
Original Format:	IgG2b
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 IgG2b format, for improved compatibility with existing reagents, assays and techniques.
Specificity Statement:	This antibody is specific for norleucine and methionine phenyl esters enantiomers that possess the natural S configuration (L) at the α-carbon.
Application Notes:	This antibody efficiently catalyzes the hydrolysis of N-formyl norleucine phenyl ester and N-formyl methionine phenyl ester, with a preference for N-formyl esters over N-acetyl esters while demonstrating a superior catalytic activity for ester hydrolysis compared to other catalytic antibodies. The catalytic efficiency is influenced by the structural dissimilarity of the substrate to the antigen at specific positions. Notably, the original format of this antibody (mouse IgG2b) exhibits a higher affinity for ester substrates with norleucine side chains than methionine side chains. This original antibody's catalytic activity showed a bell-shaped pH dependence, reaching its maximum at pH 9.5. This pH optimum is attributed to the specific ionizable groups in the antibody's active site, contributing to efficient catalysis. Importantly, this antibody does not display significant product inhibition in kinetics experiments; although weak product inhibition is observed at higher conversion levels, it does not affect the initial rate measurements. Mechanistic studies suggest that this antibody likely forms a potentially rate-limiting covalent acyl intermediate during catalysis, supported by evidence from hydroxylamine partitioning studies (Guo et al., 1994). Crystallization of the Fab-5 complex of this antibody has been accomplished. The structure showed that it has similar active site features to natural triad-based hydrolases. Additionally, the structure showed that hapten five is buried deeply in the antigen-combining site, and there are separate and well-defined binding pockets for the phenyl group and n-butyl side chain of hapten 5 (Zhou et al., 1994; PMID: 8066444) (Wade and Scanlan, 1996).

Specifications

More Information
Brand	Vector Labs
UNSPSC	12161500

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