Analytical Data
-
Gene name
HEBP2
- Application
-
Alternative Names
Placental protein 23 ;PP23;Protein SOUL
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y5Z4
-
Expression Region
2-205aa
-
Molecular Weight
38.7 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
HEBP2 (Heme-binding protein 2) is a crucial protein involved in heme metabolism, playing a significant role in cellular iron homeostasis and oxidative stress response. As a member of the heme-binding protein family, HEBP2’s primary function is to transport and regulate heme, the iron-containing compound essential for various biological processes, including oxygen transport and electron transfer in mitochondrial respiration. Research on HEBP2 has gained momentum due to its potential implications in various pathological conditions such as anemia, neurodegenerative diseases, and cancers, where dysregulation of heme metabolism can lead to aggravation of disease states. Furthermore, HEBP2 has been implicated in the modulation of inflammatory responses and has shown potential as a therapeutic target. Understanding the structure-function relationships of HEBP2 through recombinant protein studies can provide insights into its metabolic pathways and interaction with other cellular components. By utilizing techniques such as molecular cloning, expression in host systems, and biochemical assays, researchers aim to elucidate the functional mechanisms of HEBP2 and explore its therapeutic applications. Such studies not only contribute to our basic understanding of heme biology but also pave the way for developing new strategies for treating diseases linked to heme dysregulation. Overall, HEBP2 represents an important focus of research in cellular metabolism and disease pathology, offering avenues for innovative biotechnological and medical advancements.
