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Highly Rated Human Hemoglobin Theta-1 Recombinant Protein N-6 His Tag Lyophilized Massive 30% Savings [JB3N4vp9]

$78.99 $252.99 -69%

Highly Rated Human Hemoglobin Theta-1 Recombinant Protein N-6 His Tag Lyophilized Massive 30% Savings [JB3N4vp9] from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, pH

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Highly Rated Human Hemoglobin Theta-1 Recombinant Protein N-6 His Tag Lyophilized Massive 30% Savings [JB3N4vp9]

Highly Rated Human Hemoglobin Theta-1 Recombinant Protein N-6 His Tag Lyophilized Massive 30% Savings [JB3N4vp9] from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, pH 7.0. It is not recommended to reconstitute to a concentration less than 100UG/ml. Dissolve the lyophilized protein in ddH2O. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: HBQ1 Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli Storage Conditions: 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.



Additional Information:

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 rythroid 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. This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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