Recombinant Penicillin-binding protein 1A (His tag)
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Recombinant Penicillin-binding protein 1A (His tag) is a Clostridium botulinum A str. Hall Fragment protein, in the 663 to 830 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CBO3083, CLC_2985, pbpA, Penicillin-binding protein 1A, PBP1a
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Penicillin-binding protein 1A (His tag) (AB225616)
ab225616 analyzed by SDS-PAGE (Tris-Glycine gel with 5% enrichment gel and 15% separation gel).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
PBP 1A acts in the later stages of bacterial cell wall synthesis. It catalyzes the cross-linking of peptidoglycan chains which is an important process for bacterial growth and division. PBP 1A is part of a complex that includes multiple penicillin-binding proteins working together to ensure the proper formation and remodeling of the cell wall during cell division. The enzyme is central to these processes making it a target for beta-lactam antibiotics which aim to inhibit its activity disrupting bacterial cell wall synthesis and ultimately leading to cell death.
Pathways
The involvement of PBP 1A in peptidoglycan biosynthesis places it within the bacterial cell wall synthesis pathway an essential process for bacterial viability. PBP 1A functions alongside other PBPs such as PBP 1B 2 and 3 which coordinate to complete the peptidoglycan layer. Additionally PBP 1A interacts with other proteins like MurG and FtsI that participate in the assembly and elongation of the bacterial cell wall integrating it into the greater peptidoglycan assembly pathway.
Specifications
Form
Liquid
General info
Function
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
Sequence similarities
In the N-terminal section; belongs to the glycosyltransferase 51 family.. In the C-terminal section; belongs to the transpeptidase family.
Target data
Product promise
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