Analytical Data
-
Gene name
HO-1
- Application
-
Alternative Names
P32 protein
-
Species
Mouse
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P14901
-
Expression Region
1-289aa
-
Molecular Weight
34.9 kDa
-
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
Heme oxygenase-1 (HO-1) is an enzyme that plays a pivotal role in the catabolism of heme, leading to the production of biliverdin, carbon monoxide, and free iron. It is a key player in various physiological processes, including oxidative stress response, apoptosis, and inflammation, making it a crucial target for therapeutic interventions in various diseases. Research has increasingly focused on the upregulation of HO-1 as a cytoprotective mechanism, particularly in conditions such as ischemia-reperfusion injury, neurodegenerative disorders, and cardiovascular diseases. The enzyme's expression is often induced by various stressors and cytokines, highlighting its role as a regulatory protein in cellular defense mechanisms. Investigations into recombinant HO-1 protein have allowed scientists to explore its functional properties, potential therapeutic applications, and the molecular pathways involved in its action. Given its antioxidant and anti-inflammatory properties, recombinant HO-1 is being studied for its potential in the treatment of diseases characterized by oxidative stress and inflammation. Furthermore, understanding the regulatory mechanisms of HO-1 expression and activity may lead to novel strategies for enhancing its protective effects in clinical settings. Thus, the study of HO-1, particularly in its recombinant form, holds significant promise for the development of innovative therapeutic approaches aimed at mitigating tissue damage and improving outcomes in various pathological conditions.
