Analytical Data
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Gene name
ompK
- Application
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Alternative Names
ompK; OMPK_VIBPA; Outer membrane protein ompK
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Species
Vibrio parahaemolyticus serotype O3:K6
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P59570
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Expression Region
21-266aa
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Molecular Weight
43.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The OmpK family of proteins, particularly OmpK35 and OmpK36, are outer membrane porins predominantly found in *Klebsiella pneumoniae,* a significant pathogen responsible for various infections, including pneumonia and bloodstream infections. These porins play a crucial role in the permeability of the bacterial outer membrane, regulating the passage of small molecules and contributing to antibiotic resistance. Understanding the structure and function of OmpK proteins is essential for developing novel therapeutic strategies, particularly in combating multidrug-resistant strains of *K. pneumoniae.* Recent studies have focused on the recombinant expression of OmpK proteins to facilitate detailed biochemical and biophysical analyses. This research is pivotal in elucidating the mechanisms of porin-mediated transport and resistance, and it may pave the way for engineered porins with enhanced functions or modified properties for biotechnological applications. Moreover, the increasing incidence of antibiotic resistance underscores the urgency in studying these porins to inform the design of new antibiotics or adjuvants that can restore the efficacy of existing drugs. Overall, the investigation of OmpK recombinant proteins stands at the intersection of microbiology, structural biology, and pharmacology, highlighting their potential implications in public health and infectious disease management.
