Analytical Data
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Gene name
HPX
- Application
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Alternative Names
HPX；Hemopexin
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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
P02790
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Expression Region
24-462aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSTPLPPTSAHGNVAEGETKPDPDVTERC SDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAA FRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECH RGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYC FQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHH GPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQ WPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVG TPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPH EKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQ PQNVTSLLGCTH
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Molecular Weight
52 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
HPX, or Hemopexin, is a glycoprotein that plays a critical role in the body's response to oxidative stress and inflammation. It is primarily produced by the liver and is involved in heme scavenging, binding free heme released from hemoglobin, and facilitating its clearance from circulation. Research into HPX recombinant proteins has gained significance due to their potential therapeutic applications, particularly in conditions characterized by heme toxicity, such as hemolytic anemia, sickle cell disease, and other disorders where excess free heme can lead to oxidative damage and inflammation. The ability to produce HPX recombinantly allows for a more abundant and purified source for investigational studies, enabling researchers to explore its biological functions, mechanisms of action, and therapeutic efficacy. Additionally, recombinant HPX can serve as a valuable tool in deciphering the intricacies of heme metabolism and the inflammatory responses associated with various diseases. Overall, the investigation of recombinant HPX highlights its importance in both basic and translational research, offering insights into new treatment strategies for heme-related pathologies.
