Analytical Data
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Gene name
EPB2
- Application
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Alternative Names
EPB2; Cysteine proteinase EP-B 2; EC 3.4.22.-
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Species
Hordeum vulgare
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P25250
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Expression Region
134-373aa
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Molecular Weight
41.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
EPB2, or erythrocyte membrane protein band 2, is an integral component of the erythrocyte membrane responsible for maintaining cell shape, flexibility, and structural integrity. It plays a crucial role in the formation of the cytoskeletal network that supports the cell membrane, facilitating proper red blood cell (RBC) deformation during circulation. Research into EPB2 recombinant proteins has gained momentum due to its relevance in various hematological disorders, such as hereditary spherocytosis and other membrane-related pathologies. Studies have indicated that mutations in the EPB2 gene can lead to abnormal RBC shapes, resulting in hemolytic anemia and reduced oxygen-carrying capacity. Thus, the engineering of EPB2 recombinant proteins not only aids in understanding the fundamental mechanisms of erythrocyte physiology but also offers potential therapeutic avenues for treating associated conditions. Recent advancements in molecular cloning and protein expression systems have enabled the production of functional EPB2 proteins, which can be utilized in biochemical assays and preclinical studies. Furthermore, this research holds promise for the development of diagnostic tools and targeted therapies that could improve patient outcomes in diseases linked to RBC membrane defects. Overall, the investigation of EPB2 recombinant proteins is poised to provide valuable insights into red blood cell biology and its clinical implications.
