HPX, His, Mouse
HPX, His, Mouse

The purity of HPX, His, Mouse is greater than 95% as determined by SEC-HPLC.

HPX, His, Mouse

HPX, His, Mouse on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.

HPX, His, Mouse

Hemopexin (HPX) serves as scavenger and transporter of toxic plasma heme to the liver. HPX is formed by two four-bladed beta-propeller domains, resembling two thick disks that lock together at a 90 degrees angle. The heme is bound between the two beta-propeller domains in a pocket formed by the interdomain linker peptide.HPX, acting not only as a heme carrier but also displaying transient heme-based ligand binding and (pseudo-)enzymatic properties, could be considered a 'chronosteric' heme-protein.
Z06162
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Product Introduction
Species Mouse
Protein Construction
HPX (Ser24-Gln460)_x000D_
Accession # Q91X72		 His
N-term C-term
Purity > 95% as determined by Bis­Tris PAGE 
> 95% as determined by HPLC
Endotoxin Level Less than 1EU per μg by the LAL method.
Expression System HEK293
Theoretical Molecular Weight 50 kDa
Apparent Molecular Weight Due to glycosylation, the protein migrates to 65-70 kDa based on Bis-Tris PAGE result.
Formulation Lyophilized from 0.22μm filtered solution in 50mM MES, 150mM NaCl (pH 6.0).
Reconstitution Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in 50mM MES, 150mM NaCl (pH 6.0).
Storage & Stability Upon receiving, the product remains stable up to 6 months at -20 °C or below. Upon reconstitution, the product should be stable for 3 months at -80 °C. Avoid repeated freeze-thaw cycles.

Examples
  • HPX, His, Mouse
    • HPX, His, Mouse

    The purity of HPX, His, Mouse is greater than 95% as determined by SEC-HPLC.

  • HPX, His, Mouse
    • HPX, His, Mouse

    HPX, His, Mouse on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.


Background
Target Background Hemopexin (HPX) serves as scavenger and transporter of toxic plasma heme to the liver. HPX is formed by two four-bladed beta-propeller domains, resembling two thick disks that lock together at a 90 degrees angle. The heme is bound between the two beta-propeller domains in a pocket formed by the interdomain linker peptide.HPX, acting not only as a heme carrier but also displaying transient heme-based ligand binding and (pseudo-)enzymatic properties, could be considered a 'chronosteric' heme-protein.
Synonyms Hemopexin;Hpx;Hpxn

For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.