Analytical Data
-
Gene name
NlpC/P60
- Application
-
Species
MEDGN
-
Source
E. coli
-
Tag
N-terminal His Tag
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
A0A2N5P430
-
Expression Region
27-378aa
-
AA Sequence
APDDTTSLQNQKESAQNEVNGLQAQLNELFTKTNDLETQLINKGQEITKAQEDL AVAEEKKQQQYEDMKLRIKYMYEEGDTSALERIVASGSISEMLTQTEYVEKVHT YDRDKLREYAETVQEVEDLKTSLESDMTKLQNLDEEYKTQTAELSSTIESKRAE VSNLDAMIQEAAKAAVEAAKKEQEKNNTANNENTNTNTPSDSGDNSGETVTPAP EPTPTPTPDPTPTPTPTPTPTPTPEPNYNPSTGNAIVDRAYSWVGKAEYVWGAC SPGAFDCSGFVSYCLTGAYSRLGTTYTFLTWTQVSNPQPGDVAVNENHCGIYIG GGQMIHAADYGIGVIVGPVQSGMIYVRY
-
Molecular Weight
42.0kDa
-
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
Identification
Protein Description
HSP60, or Heat Shock Protein 60, is a crucial chaperonin that assists in the proper folding of proteins within the mitochondria and cytoplasm, playing a vital role in cellular stress response and maintaining proteostasis. Research surrounding HSP60 recombinant proteins has gained significant interest due to their potential applications in understanding various diseases, including neurodegenerative disorders, cancer, and autoimmune conditions. The ability to produce HSP60 as a recombinant protein allows for the study of its structure-function relationship and interactions with other cellular components. Furthermore, HSP60 has been implicated in the immune system, as it can act as an endogenous danger signal that triggers immune responses. This property has led researchers to explore the use of HSP60 as a target for therapeutic intervention and as a vaccine candidate. As a result, studies focusing on the expression, purification, and characterization of recombinant HSP60 proteins are essential for elucidating their biological functions and developing innovative treatments for related diseases. Hence, understanding the complex mechanisms of HSP60 and its role in both health and disease remains a frontier in molecular biology and medicine.











