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% purity and suitable for SDS-PAGE.
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Key facts
- Purity
>90% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE
- Biologically active
No
Amino acid sequence
V D R I S G K L P T Q L S Y R D P R G S T V Y N E F F I N G T I P T E Y D D I H V E A Q I N K L T G K L A S K F T P S F L V E S R V F L R R D Y S P G V E L L D Q Q W L L P Y S I D E G G S L P P T E E K N N S N T R D K N K D K N K N K N K D K N P S Q D K P N N N N N D N N S N N N N N N N D N N N N T K P P E N D S N Q N H E D N K N K Q
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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Target data
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).
Alternative names
Penicillin-binding protein 1A, PBP1a, CLC_2985, CBO3083, pbpA
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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% purity and suitable for SDS-PAGE.
Key facts
- Purity
>90% SDS-PAGE
- Expression system
Escherichia coli
- Tags
His tag N-Terminus
- Applications
SDS-PAGE
- Biologically active
No
- Accession
- A5I6G4-1
- Animal free
No
- Species
Clostridium botulinum A str. Hall
- Concentration
- Storage buffer
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
Sequence info
Amino acid sequence
V D R I S G K L P T Q L S Y R D P R G S T V Y N E F F I N G T I P T E Y D D I H V E A Q I N K L T G K L A S K F T P S F L V E S R V F L R R D Y S P G V E L L D Q Q W L L P Y S I D E G G S L P P T E E K N N S N T R D K N K D K N K N K N K D K N P S Q D K P N N N N N D N N S N N N N N N N D N N N N T K P P E N D S N Q N H E D N K N K Q
- Accession
- Protein length
Fragment
- Predicted molecular weight
35.2 kDa
- Amino acids
663 to 830
- Nature
Recombinant
- Tags
His tag N-Terminus
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.
Storage
- Shipped at conditions
Blue Ice
- Appropriate short-term storage conditions
-20°C
- Appropriate long-term storage conditions
-20°C
- Aliquoting information
Upon delivery aliquot
- Storage information
Avoid freeze / thaw cycle
Supplementary info
This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Penicillin-binding protein 1A (PBP 1A) also known as PBP1a is an enzyme important for bacterial cell wall biosynthesis. It plays an essential role in the synthesis of peptidoglycan a vital polymer that provides structural strength to the bacterial cell wall. PBP 1A is expressed in the cytoplasmic membrane of many bacteria including E. coli and other Gram-negative bacterial species. It has a molecular mass of about 87 kDa and has transpeptidase activity which links the peptide chains of the peptidoglycan helping to maintain cell wall integrity and shape.
- 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.
- Associated diseases and disorders
PBP 1A is significant due to its role in antibiotic resistance. Beta-lactam antibiotics like penicillins and cephalosporins target PBPs to inhibit cell wall synthesis. Mutations or overexpression of PBP 1A can lead to antibiotic resistance presenting challenges in treating bacterial infections such as pneumonia and sepsis. This resistance is often linked to alterations in other PBPs such as PBP 2a in methicillin-resistant Staphylococcus aureus (MRSA) further complicating therapy and requiring alternative treatment strategies.
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1 product image
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).
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