Analytical Data
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Gene name
HSP40
- Application
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Alternative Names
HSPA8;HSC70;HSP73;HSPA10;Heat shock cognate 71 kDa 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
P25685
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Expression Region
1-340aa
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AA Sequence
MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI
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Molecular Weight
65.0kDa
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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
HSP40, also known as DnaJ, is a crucial molecular chaperone that plays an essential role in protein folding, assembly, and degradation, thus maintaining cellular proteostasis. Its importance is underscored by its involvement in various cellular processes, including stress response, thermotolerance, and neurodegenerative diseases. The HSP40 family is characterized by a highly conserved J-domain, which interacts with HSP70 chaperones to facilitate substrate protein refolding and prevent aggregation. Research into recombinant HSP40 proteins has gained momentum due to their potential therapeutic applications in treating diseases characterized by protein misfolding, such as Alzheimer’s, Parkinson’s, and Huntington’s diseases. By producing and studying recombinant HSP40, scientists aim to better understand its mechanism of action and its interactions with client proteins. This research is not only vital for unraveling the complexities of protein homeostasis but also for developing novel strategies for disease intervention by modulating the chaperone machinery in cells. The functional characterization of HSP40, including its ability to enhance HSP70 activity and its involvement in signaling pathways, presents significant implications for both basic biochemical research and potential pharmaceutical developments. Additionally, the development of reliable expression systems for HSP40 proteins, alongside their purification and functional assays, is critical in identifying small molecules that can enhance or inhibit their activity, ultimately leading to innovative therapeutic approaches in the realm of proteopathy.
