Analytical Data
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Gene name
HRS
- Application
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Alternative Names
HGS;HRS;Hepatocyte growth factor-regulated tyrosine kinase substrate
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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
P12081
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Expression Region
1-509aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAERAALEELVKLQGERVRGLKQQKAS AELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVF DVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSL RYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFD IAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVS DSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGV SLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARG LDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKV PCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKL VSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIK LRSVTSREEVDVRREDLVEEIKRRTGQPLCIC
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Molecular Weight
60 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 research on Histidine-Rich Protein (HRS) has gained significant attention due to its crucial role in various biological processes and potential applications in medicine and biotechnology. HRS proteins, characterized by their high content of histidine residues, are involved in cellular functions such as metal ion binding, gene expression regulation, and stress response. They are particularly prominent in the context of diseases like cancer, where their expression levels can correlate with tumor progression and patient prognosis. Furthermore, HRS proteins have been implicated in the development of new therapeutic strategies, as they may serve as biomarkers for disease diagnosis or targets for drug development. The recombination of HRS proteins offers opportunities to study their structure-function relationships in detail, enabling researchers to manipulate these proteins for experimental purposes or to design novel therapeutic agents. Advances in recombinant DNA technology and protein engineering have facilitated the production of HRS proteins, allowing for in-depth studies of their properties and interactions in cellular environments. This growing body of research highlights the potential of HRS proteins in elucidating complex biological mechanisms and developing innovative solutions for health-related challenges.
