Recombinant Human Hemoglobin Subunit θ-1/HBQ1 (N-6His)

Cat.No.: CK22

Recombinant Human HBQ1 (N-6His)
Description
Recombinant Human Hemoglobin subunit theta-1 is produced by our E.coli expression system and the target gene encoding Met1-Arg142 is expressed with a 6His tag at the N-terminus.
Accession #:P09105
Known as:Hemoglobin subunit theta-1; Hemoglobin theta-1 chain; Theta-1-globin; HBQ1
Formulation
Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0.
Quality Control
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin:Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Reconstitution
Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage
Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Background
Hemoglobin subunit theta-1 is a protein that in humans is encoded by the HBQ1 gene. Theta-globin mRNA is originally found in human fetal erythroid tissue but not in adult erythroid or other nonerythroid tissue. Theta-1 is a member of the human alpha-globin gene cluster that includes five functional genes and two pseudogenes. Research supports a transcriptionally active role for the gene and a functional role for the peptide in specific cells, possibly those of early erythroid tissue. Hemoglobin has a quaternary structure characteristically composed of many multi-subunit globular proteins. Most of the amino acids in hemoglobin form alpha helices, connected by short non-helical segments. Hydrogen bonds stabilize the helical sections inside this protein, causing attractions within the molecule, folding each polypeptide chain into a specific shape. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.

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