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AB226275

Recombinant B. subtilis Penicillin-binding protein 3 (His tag)

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(1 Publication)

Recombinant B. subtilis Penicillin-binding protein 3 (His tag) is a Bacillus subtilis subsp. subtilis str. 168 Fragment protein, in the 21 to 240 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.

View Alternative Names

ycsM, yzsA, BSU04140, pbpC, Penicillin-binding protein 3, PBP 3, PSPB20, Penicillin-binding protein C

1 Images
SDS-PAGE - Recombinant B. subtilis Penicillin-binding protein 3 (His tag) (AB226275)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant B. subtilis Penicillin-binding protein 3 (His tag) (AB226275)

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis of ab226275 with 5% enrichment gel and 15% separation gel.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P42971

Animal free

No

Carrier free

No

Species

Bacillus subtilis subsp. subtilis str. 168

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"CSKTDSPEDRMEAFVKQWNDQQFDDMYQSLTKDVKKEISKKDFVNRYKAIYEQAGVKNLKVTAGEVDKDDQDNKTMKHIPYKVSMNTNAGKVSFKNTAVLKLEKTDDEESWNIDWDPSFIFKQLADDKTVQIMSIEPKRGQIYDKNGKGLAVNTDVPEIGIVPGELGDKKEKVIKELAKKLDLTEDDIKKKLDQGWVKDDSFVPLKKVKPDQEKLVSEAT","proteinLength":"Fragment","predictedMolecularWeight":"29.2 kDa","actualMolecularWeight":null,"aminoAcidEnd":240,"aminoAcidStart":21,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P42971","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

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
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Penicillin-binding protein 3 (PBP3) also known as FtsI is an enzyme involved in bacterial cell wall synthesis. This protein plays a central role in the last stages of peptidoglycan synthesis catalyzing transpeptidation reactions that cross-link peptide chains. PBP3 weighs about 71 kDa and is expressed in the membrane of Gram-negative bacteria. By anchoring in the bacterial inner membrane it interacts with other proteins essential for bacterial growth and division.
Biological function summary

PBP3 is important in maintaining the integrity and shape of bacterial cells. It forms part of a larger complex known as the divisome which coordinates cell division. As a central player in septum formation PBP3 ensures proper cellular division by organizing the synthesis of new cell wall material at the division site. The disruption of PBP3 function can severely affect bacterial viability making it a significant target for antibiotics.

Pathways

The synthesis of peptidoglycan represents the central role for PBP3. It integrates into the biosynthesis and remodeling pathways of the bacterial cell wall. These pathways are vital for maintaining cell structure and survival. Additionally PBP3 interacts with other penicillin-binding proteins (PBPs) in the pathway coordinating the regulated activity necessary for cell wall expansion and septation. This process is tightly linked with proteins such as FtsZ which positions the divisome complex during cell division.

The altered activity of PBP3 contributes significantly to antibiotic resistance. Bacteria modify PBP3 to decrease its affinity for beta-lactam antibiotics reducing these drugs' efficacy. This resistance mechanism plays an important role in conditions like penicillin-resistant Neisseria gonorrhoeae and methicillin-resistant Staphylococcus aureus (MRSA). Both of these bacteria utilize altered PBPs including PBP2a in MRSA to evade the bactericidal effects of beta-lactams highlighting the importance of PBP3 in the development and spread of antibiotic resistance.

Specifications

Form

Liquid

General info

Function

Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis (Probable). Probably required for both cortical and vegetative peptidoglycan synthesis (Probable). Although not usually required for cell division, in the absence of PBP 2B (pbpB) it becomes essential. Confers resistance to oxacillin and cephalexin (PubMed : 28792086).

Sequence similarities

Belongs to the transpeptidase family.

Product protocols

Target data

Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis (Probable). Probably required for both cortical and vegetative peptidoglycan synthesis (Probable). Although not usually required for cell division, in the absence of PBP 2B (pbpB) it becomes essential. Confers resistance to oxacillin and cephalexin (PubMed : 28792086).
See full target information pbpC

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Experimental and therapeutic medicine 19:2449-2456 PubMed32256721

2020

presents antimicrobial drug resistance for β-lactam through the ESBL/PBP signaling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Wei Jiang,Wenjie Yang,Xuequn Zhao,Na Wang,Haixia Ren
View all publications

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