Penicillinase-resistant penicillins

Anti-Penicillinase antibody has been assayed against 1.0 ug of Penicillinase in a standard capture ELISA using Peroxidase Conjugated Streptavidin #S000-03 and ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a

Anti-Penicillinase antibody has been assayed against 1.0 ug of Penicillinase in a standard capture ELISA using Peroxidase Conjugated Streptavidin #S000-03 and ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a

Anti-Penicillinase has been assayed against 1.0 ug of Penicillinase [Enterobacter cloacae] in a standard capture ELISA using ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a substrate for 30 minutes at room

Anti-Penicillinase has been assayed against 1.0 ug of Penicillinase [Enterobacter cloacae] in a standard capture ELISA using ABTS (2,2’-azino-bis-[3-ethylbenthiazoline-6-sulfonic acid]) code # ABTS-100 as a substrate for 30 minutes at room

Anti-PENICILLINASE Antibody has been assayed against 1.0 ug of Penicillinase [Enterobacter cloacae] in a standard ELISA using Peroxidase conjugated Affinity Purified anti-Rabbit IgG [H&L] (Goat) and (ABTS

Recommended for detection of Penicillin in milk samples and in microbiological assay of different antibiotics in accordance with USP, Generally presence of penicillin in milk is detected by the cylinder plate method, using Micrococcus luteus as the

Penicillinase from Bacillus cereus has been shown to contain three distinct species when purified and examined for homogeneity by sedimentation analysis, amino-terminal analysis, and vertical acrylamide gel electrophoresis.Penicillinase can be used

BRISTOL 8

Application Highly purified &#946-Lactamase concentrate as a culture media supplement for deactivation of antibiotics in microbial samples. Inactivation of Penicillin G* 10,000,000 IU/mL/min *Not all penicillins are comparable to Penicillin G in

General description Penicillinase from Bacillus cereus has been shown to contain three distinct species when purified and examined for homogeneity by sedimentation analysis, amino-terminal analysis, and vertical acrylamide gel electrophoresis.

Penicillinase from Bacillus cereus is both an extracellular and cell-bound enzyme. It has a single polypeptide chain and has a molecular weight of 31 kDa.

General description Penicillinase from Bacillus cereus has been shown to contain three distinct species when purified and examined for homogeneity by sedimentation analysis, amino-terminal analysis, and vertical acrylamide gel electrophoresis.