Analytical Data
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Gene name
yopH
- Application
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Alternative Names
yopH；Prap；Ra70；Saps；Src kinase-associated phosphoProtein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q3UND0
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Expression Region
1-358aa
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AA Sequence
MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK KIKDVKSVYL QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP SDGNQFPPIA AQDLPFVIKA GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD GKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV DHPAAVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YLMEMYDI
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Molecular Weight
40.7 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
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Protein Description
The yopH protein is a type of effector protein found in the type III secretion system of Yersinia spp., particularly Yersinia pestis, the bacterium responsible for bubonic plague. This protein plays a crucial role in the pathogenicity of these bacteria by manipulating host cell signaling pathways, specifically by targeting and dephosphorylating host proteins involved in actin cytoskeleton dynamics and immune response. Research into yopH has gained significance due to its potential as a target for therapeutic interventions, considering the public health implications of Yersinia infections. Recombinant yopH protein, produced using modern molecular biology techniques, allows researchers to investigate its biochemical properties and functional mechanisms in a controlled environment. This work has paved the way for understanding how yopH contributes to bacterial virulence, influencing the development of vaccines or novel antimicrobial strategies. Recent studies employing structural biology methods have also provided insights into the protein's structure-function relationships, revealing the molecular basis for its enzymatic activity and interactions with host targets. As a result, the research surrounding yopH not only enhances our understanding of host-pathogen interactions but also holds promise for the discovery of innovative therapeutic approaches against Yersinia pestis and similar pathogenic organisms.
