HBQ1 Human Recombinant Protein
CAT#: TP727324
Recombinant Human Hemoglobin Subunit θ-1/HBQ1 (N-6His)
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CNY 3,140.00
货期*
2周
规格
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经常一起买 (1)
Specifications
Product Data | |
Species | Human |
Protein Source | E. coli |
Expression cDNA Clone or AA Sequence |
Met1-Arg142
|
Tag | N-His |
Buffer | Lyophilized from a 0.2 um filtered solution of 20mM PB, 150mM NaCl, pH 7.0. |
Note | 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. |
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. |
Stability | 12 months from date of despatch |
Reference Data | |
Locus ID | 3049 |
UniProt ID | P09105 |
Synonyms | Hemoglobin subunit theta-1; Hemoglobin theta-1 chain; Theta-1-globin; HBQ1 |
Summary | 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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