Analytical Data
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Gene name
HOP
- Application
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Alternative Names
HOP；HOD；HOP；LAGY；Homeodomain-only Protein
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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
Q9BPY8
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Expression Region
1-73aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSAETA SGPTEDQVEI LEYNFNKVDK HPDSTTLCLI AAEAGLSEEE TQKWFKQRLA KWRRSEGLPS ECRSVTD
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Molecular Weight
11 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
HOP (Hsp70-Hsp90 organizing protein) is a co-chaperone that plays a crucial role in the folding and activation of client proteins through its interactions with heat shock proteins Hsp70 and Hsp90. The study of HOP is of significant interest in the field of molecular biology and biotechnology due to its involvement in various cellular processes, including protein quality control, signal transduction, and the stress response. Dysregulation of HOP and its associated chaperone networks has been linked to several diseases, including neurodegenerative disorders and cancer, making it a potential therapeutic target. Research into HOP recombinant proteins provides insights into its structural and functional dynamics, enabling scientists to dissect the mechanisms underlying its action. Additionally, the production of HOP as a recombinant protein allows for the exploration of its role in protein-protein interactions, client protein specificity, and the regulatory mechanisms governing heat shock protein activity. Furthermore, understanding HOP's function can contribute to the development of new strategies for ameliorating diseases characterized by protein misfolding and aggregation. As such, the study of HOP recombinant proteins is not only fundamental for advancing our comprehension of chaperone biology but also holds promise for the development of innovative therapeutic interventions.
