Analytical Data
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Gene name
RHCE
- Application
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Alternative Names
RHCE；RHC；RHE；；Blood group Rh(CE) polypeptide
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18577
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Expression Region
1-417aa
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AA Sequence
MSSKYPRSVRRCLPLWALTLEAALILLFYFFTHYDASLEDQKGLVASYQVGQDLTVMAALGLGFLTSNFRRHSWSSVAFNLFMLALGVQWAILLDGFLSQFPPGKVVITLFSIRLATMSAMSVLISAGAVLGKVNLAQLVVMVLVEVTALGTLRMVISNIFNTDYHMNLRHFYVFAAYFGLTVAWCLPKPLPKGTEDNDQRATIPSLSAMLGALFLWMFWPSVNSPLLRSPIQRKNAMFNTYYALAVSVVTAISGSSLAHPQRKISMTYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISIGGAKCLPVCCNRVLGIHHISVMHSIFSLLGLLGEITYIVLLVLHTVWNGNGMIGFQVLLSIGELSLAIVIALTSGLLTGLLLNLKIWKAPHVAKYFDDQVFWKFPHLAVGF
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Molecular Weight
47.1 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
The study of recombinant human coagulation factor VIII (RHCE) has gained significant attention in recent years due to its critical role in the management of hemophilia A, a genetic disorder characterized by a lack of clotting factor VIII. Traditional treatment methods, which relied on the administration of plasma-derived factor VIII, posed risks of viral transmission and variability in biological activity. Advances in biotechnology have enabled the production of RHCE through recombinant DNA technology, providing a safer and more consistent therapeutic option. Researchers have focused on optimizing expression systems, enhancing protein stability, and improving yield and purification processes to ensure the functionality of the recombinant protein. Moreover, ongoing studies aim to understand the structure-function relationships of RHCE and explore its potential for gene therapy applications. The development of RHCE not only revolutionizes hemophilia treatment by reducing dependence on human plasma but also paves the way for innovative therapeutic strategies that could enhance patient outcomes and quality of life. Through continued research, RHCE is poised to play a pivotal role in redefining the management of bleeding disorders.
