Recombinant Human HBQ1 (N-6His)

Recombinant Human HBQ1 (N-6His)

Size1:10μg price1:$168
Size2:50μg price2:$465
Size3:500μg price3:$2350
SKU: PEH0774 Category: Target Proteins Tags: ,

Datasheet

Name

Recombinant Human HBQ1 (N-6His)

Purity

Greater than 95% as determined by reducing SDS-PAGE

Endotoxin level

<1 EU/µg as determined by LAL test.

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.

Accession #

P09105

Host

E.coli

Species

Human

Predicted Molecular Mass

17.7 KDa

Buffer

Lyophilized from a 0.2 μm filtered solution of 20mM Histidine, 10% Sucrose, 3% Mannitol, 0.5mM EDTA, 0.05% Tween80, pH 5.5.

Form

Lyophilized

Shipping

The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.

Stability&Storage

Store at ≤-70°C, stable for 6 months after receipt.Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.

Reconstitution

Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

 

 

 

Alternative Names

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

 

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. Hemoglobins quaternary structure comes from its four subunits in roughly a tetrahedral arrangement.

 

Note

For Research Use Only , Not for Diagnostic Use.