Analytical Data
-
Gene name
HSP75
- Application
-
Alternative Names
HSP75；HSP75；HSPC5；Heat shock Protein 75 kDa. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q12931
-
Expression Region
60-308aa
-
AA Sequence
STQTAEDKEEPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELISNASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEELVSNLGTIARSGSKAFLDALQNQAEASSKIIGQFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVRTGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAIWMMDPKDVRE
-
Molecular Weight
54.5kDa
-
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
HSP75, also known as heat shock protein 75, is a member of the HSP70 family and plays a critical role in cellular stress responses, protein folding, and mitochondrial function. It primarily functions within the mitochondria, where it assists in the proper folding and assembly of proteins that are vital for mitochondrial integrity and energy production. Research has shown that HSP75 is crucial for cell survival under stress conditions, making it a key player in various diseases, including neurodegenerative disorders and cancer, where it may influence cell survival and apoptosis. The recombinant production of HSP75 has garnered significant interest for potential therapeutic applications, as understanding the structure and function of this protein can lead to novel strategies for disease intervention. Various expression systems, including bacterial, yeast, and mammalian cells, have been employed to produce HSP75, facilitating the study of its biological properties and intermolecular interactions. Additionally, recombinant HSP75 can be used in biotechnological applications, such as developing protein-based therapeutics or as a biomarker for specific diseases. This work aims to elucidate the molecular mechanisms underlying HSP75's function and its implications in pathophysiology, ultimately paving the way for innovative therapeutic solutions. The ongoing investigation into the recombinant properties of HSP75 not only enriches our understanding of cellular stress responses but also highlights its potential significance in the development of next-generation therapeutic strategies.
