| Product Name | Beta-lactamase, 20-377aa |
|---|---|
| Description | AmpC, also known as Beta-lactamase, is the most widespread resistance mechanism to beta-lactam antibiotics, such as the penicillins and the cephalosporins. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Recombinant E.coli beta-lactamase protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Synonyms | ampC, ampA, Cephalosporinase, D-alanine carboxypeptidase |
| Host | E. coli |
| Molecular Weight | 15.6 kDa(138aa), confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MAPQQINDIV HRTITPLIEQ QKIPGMAVAV IYQGKPYYFT WGYADIAKKQ PVTQQTLFEL GSVSKTFTGV LGGDAIARGE IKLSDPTTKY WPELTAKQWN GITLLHLATY TAGGLPLQVP DEVKSSSDLL RFYQNWQPAW APGTQRLYAN SSIGLFGALA VKPSGLSFEQ AMQTRVFQPL KLNHTWINVP PAEEKNYAWG YREGKAVHVS PGALDAEAYG VKSTIEDMAR WVQSNLKPLD INEKTLQQGI QLAQSRYWQT GDMYQGLGWE MLDWPVNPDS IINGSDNKIA LAARPVKAIT PPTPAVRASW VHKTGATGGF GSYVAFIPEK ELGIVMLANK NYPNPARVDA AWQILNALQ |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 50% glycerol, 0.2M NaCl,1mM DTT |
| Concentration | 0.25 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Jaurin B., et al. (1981) Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901 Morandi F, et al. (2003) J AM Chem Soc. 125(3):685-95 |
| Background | AmpC, also known as Beta-lactamase, is the most widespread resistance mechanism to beta-lactam antibiotics, such as the penicillins and the cephalosporins. These antibiotics have a common element in their molecular structure: a four-atom ring known as a beta-lactam. The lactamase enzyme breaks that ring open, deactivating the molecule's antibacterial properties. Recombinant E.coli beta-lactamase protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. |
| Supplier | ARP |
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