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AB225590

Recombinant E. coli Outer membrane protein C (Tagged)

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Recombinant E. coli Outer membrane protein C (Tagged) is a Escherichia coli K-12 Full Length protein, in the 22 to 367 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

meoA, par, b2215, JW2203, ompC, Outer membrane porin C, Outer membrane protein 1B, Outer membrane protein C, Porin OmpC

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Mass Spectrometry - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab225590 could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) ompC.

Mass Spectrometry - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab225590 could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) ompC

SDS-PAGE - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant E. coli Outer membrane protein C (Tagged) (AB225590)

Discontinuous SDS-PAGE (Tris-Glycine gel) (reduced) 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, Mass Spec

applications

Biologically active

No

Accession

P06996

Animal free

No

Carrier free

No

Species

Escherichia coli K-12

Storage buffer

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

storage-buffer

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Reactivity data

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

[{"sequence":"AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF","proteinLength":"Full Length","predictedMolecularWeight":"54.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":367,"aminoAcidStart":22,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P06996","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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
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Supplementary information

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

Outer membrane protein C also known as OmpC protein is a significant component of the outer membrane in Gram-negative bacteria particularly E. coli. This protein with a mass of approximately 40 kDa spans the outer membrane and acts as a porin. It facilitates the selective transport of small molecules and ions into and out of the bacterial cell playing an important role in maintaining the cellular homeostasis. OmpC is abundantly expressed in the outer membrane of E. coli where it forms trimeric complexes contributing to the permeability barrier of the membrane.
Biological function summary

Outer membrane protein C contributes to the osmotic balance of E. coli cells. It adjusts the permeability of the outer membrane under different environmental conditions such as changes in osmolarity. OmpC forms trimeric structures working in concert with other porins like OmpF to modulate the membrane's permeability to various solutes. This ability to regulate solute passage is important for the bacteria's adaptive responses allowing E. coli to thrive in fluctuating environments.

Pathways

Outer membrane protein C plays a significant role in the regulation of osmotic stress pathways in E. coli. OmpC alongside porins like OmpF and LamB is an important player in these pathways adapting its expression and function in response to changing osmotic conditions. This regulation is essential for the effective transport of metabolites and ions impacting the larger metabolic networks within the bacterium. It influences pathways involved in nutrient uptake which are vital for bacterial survival and adaptation.

Outer membrane protein C has implications in the pathogenesis of certain infections like urinary tract infections (UTIs) caused by E. coli. Variations in the expression of OmpC along with proteins such as TolC can affect the bacterium’s resistance to antibiotics. This resistance arises from changes in membrane permeability that can influence antibiotic uptake presenting challenges for treatment. Understanding OmpC's role in such infections is essential for developing more effective therapeutic strategies.
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Specifications

Form

Liquid

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General info

Function

Forms pores that allow passive diffusion of small molecules across the outer membrane.. (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF.. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity.

Sequence similarities

Belongs to the Gram-negative porin family.

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Product protocols

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Target data

Forms pores that allow passive diffusion of small molecules across the outer membrane.. (Microbial infection) Supports colicin E5 entry in the absence of its major receptor OmpF.. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA-EC536-mediated toxicity.
See full target information ompC
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