HBQ1 Protein (His tag)

Catalog No. ABIN7318571

Product Details

Target: HBQ1 (Hemoglobin theta 1 (HBQ1))

Protein Type: Recombinant

Origin: Human

Source: Escherichia coli (E. coli)

Purification tag / Conjugate: This HBQ1 protein is labelled with His tag.

Purpose: Recombinant Human HBQ1 Protein (His Tag)

Sequence: Met 1-Arg142

Characteristics: 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.

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

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

Application Details

Restrictions: For Research Use only

Handling

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.

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: 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.

Target Details

Target: HBQ1 (Hemoglobin theta 1 (HBQ1))

Alternative Name: HBQ1 (HBQ1 Products)

Synonyms: GLND1 Protein, hemoglobin subunit theta 1 Protein, hemoglobin, theta 1 Protein, HBQ1 Protein, Hbq1 Protein

Background:

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

Molecular Weight: 17.7 kDa

UniProt: P09105