Analytical Data
-
Gene name
HSP18.1
- Application
-
Alternative Names
HSP18.1；18.1 kDa class I heat shock Protein
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P19243
-
Expression Region
1-158aa
-
AA Sequence
MSLIPSFFSGRRSNVFDPFSLDVWDPLKDFPFSNSSPSASFPRENPAFVSTRVDWKETPEAHVFKADLPGLKKEEVKVEVEDDRVLQISGERSVEKEDKNDEWHRVERSSGKFLRRFRLPENAKMDKVKASMENGVLTVTVPKEEIKKAEVKSIEISG
-
Molecular Weight
34.1kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
HSP18.1, a member of the heat shock protein family, plays a crucial role in cellular stress responses and protein homeostasis. As a molecular chaperone, it assists in the proper folding of proteins, protects cells from thermal and oxidative stress, and aids in the refolding of denatured proteins. The study of HSP18.1 is particularly relevant due to its involvement in various biological processes, including the regulation of apoptosis, inflammation, and aging. Increased expression of HSP18.1 has been associated with enhanced cell survival under stressful conditions, making it a potential target for therapeutic interventions in diseases such as cancer and neurodegenerative disorders. Recent advancements in recombinant DNA technology have facilitated the production of HSP18.1 in heterologous systems, enabling detailed investigations of its functional properties and interactions with other cellular proteins. Understanding the structure-function relationships of HSP18.1 through recombinant protein studies can provide insights into its mechanism of action, leading to the development of novel strategies for disease treatment and prevention. Moreover, HSP18.1’s potential as a biomarker for stress-related diseases further underscores its significance in biomedical research. Overall, the comprehensive study of HSP18.1 recombinant proteins not only enhances our understanding of stress response mechanisms but also opens new avenues for innovative therapeutic approaches.
