HBQ1 Protein (His tag)
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- Antigène Voir toutes HBQ1 Protéines
- HBQ1 (Hemoglobin theta 1 (HBQ1))
- Type de proteíne
- Recombinant
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Origine
- Humain
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Source
- Escherichia coli (E. coli)
- Purification/Conjugué
- Cette HBQ1 protéine est marqué à la His tag.
- Fonction
- Recombinant Human HBQ1 Protein (His Tag)
- Séquence
- Met 1-Arg142
- Attributs du produit
- 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.
- Pureté
- > 95 % as determined by reducing SDS-PAGE.
- niveau d'endotoxine
- < 1.0 EU per μg as determined by the LAL method.
- Top Product
- Discover our top product HBQ1 Protéine
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.0.
- Stock
- 4 °C,-20 °C,-80 °C
- Stockage commentaire
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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- Antigène
- HBQ1 (Hemoglobin theta 1 (HBQ1))
- Autre désignation
- HBQ1 (HBQ1 Produits)
- Synonymes
- GLND1 Protein, hemoglobin subunit theta 1 Protein, hemoglobin, theta 1 Protein, HBQ1 Protein, Hbq1 Protein
- Sujet
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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.
Synonym: Hemoglobin subunit theta-1, Hemoglobin theta-1 chain, Theta-1-globin, HBQ1
- Poids moléculaire
- 17.7 kDa
- UniProt
- P09105
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