Recombinant Human HBQ1 Protein (His Tag) | PKSH032532

Recombinant Human HBQ1 Protein (His Tag) | PKSH032532 | Gentaur US, UK & Europe Disrtribition

Synonyms: Hemoglobin subunit theta-1; Hemoglobin theta-1 chain; Theta-1-globin; HBQ1

Active Protein: N/A

Activity: 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.

Protein Construction: 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.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and 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.

Molecular Mass: 17.7 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0.

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.

Research Area: Cardiovascular