Recombinant Human HBQ1 Protein (His Tag) (PKSH032532)
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For research use only.
| Synonyms | HBQ1, Hemoglobin subunit theta-1, Hemoglobin theta-1 chain, Theta-1-globin |
| Species | Human |
| Expression Host | E.coli |
| Sequence | Met 1-Arg142 |
| Accession | P09105 |
| Calculated Molecular Weight | 17.7 kDa |
| Observed Molecular Weight | 15&30 kDa |
| Tag | N-His |
| Bio-activity | Not validated for activity |
| Form | Lyophilized powder |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months. |
| Shipping | This product is provided as lyophilized powder which is shipped with ice packs. |
| Formulation |
Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0. Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual. |
| Reconstitution | Please refer to the printed manual for detailed information. |
| 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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