HBQ1 Protein (His tag)

N° du produit ABIN7318571

Détail du produit

Antigène: HBQ1 (Hemoglobin theta 1 (HBQ1))

Type de proteíne: Recombinant

Origine: Humain

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.

Information d'application

Restrictions: For Research Use only

Stockage

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.

Détail du antigène

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:

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