Analytical Data
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Gene name
yopM
- Application
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Alternative Names
yopM；MAPKAPK1A；RSK1；Ribosomal Protein S6 kinase alpha-1
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Species
Yersinia
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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
P17778
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Expression Region
1-409aa
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AA Sequence
MFINPRNVSNTFLQEPLRHSSNLTEMPVEAENVKSKTEYYNAWSEWERNAPPGNGEQREMAVSRLRDCLDRQAHELELNNLGLSSLPELPPHLESLVASCNSLTELPELPQSLKSLLVDNNNLKALSDLPPLLEYLGVSNNQLEKLPELQNSSFLKIIDVDNNSLKKLPDLPPSLEFIAAGNNQLEELPELQNLPFLTAIYADNNSLKKLPDLPLSLESIVAGNNILEELPELQNLPFLTTIYADNNLLKTLPDLPPSLEALNVRDNYLTDLPELPQSLTFLDVSENIFSGLSELPPNLYYLNASSNEIRSLCDLPPSLEELNVSNNKLIELPALPPRLERLIASFNHLAEVPELPQNLKQLHVEYNPLREFPDIPESVEDLRMNSERVVDPYEFAHETTDKLEDDVFE
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Molecular Weight
62.2 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
YopM is a virulence factor encoded by the pathogenic bacterium Yersinia pestis, the causative agent of the plague, as well as by Yersinia pseudotuberculosis and Yersinia enterocolitica. This protein is part of the Type III secretion system, which allows these bacteria to inject effector proteins directly into host cells, thereby subverting host immune responses and facilitating infection. Research on YopM has garnered attention due to its role in modulating immune signaling pathways, particularly its interaction with host proteins that regulate inflammatory responses. It has been shown that YopM can inhibit apoptosis in immune cells and interfere with cytokine production, leading to a more favorable environment for bacterial survival and proliferation. Understanding the structural and functional characteristics of YopM is crucial for elucidating its mechanisms of action and its contribution to the pathogenicity of Yersinia species. Furthermore, YopM is a potential target for vaccine development and therapeutic interventions, as neutralizing its function could enhance host immune responses against infection. Current studies focus on the recombinant expression and purification of YopM to facilitate detailed biochemical and structural analyses, aiming to unlock the intricacies of its interactions with host cellular machinery and explore its potential as a candidate for novel treatment strategies against Yersinia infections.
