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HBQ1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00812
Synonyms: Hemoglobin subunit θ-1, Hemoglobin subunit theta-1, Hemoglobin theta-1 chain, Theta-1-globin, HBQ1, θ-1-globin, Hemoglobin θ-1 chain

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
HBQ1 Protein, Human, Recombinant (His)
Pack Size Availability Price/USD Quantity
10 μg 5 days $ 184.00
50 μg 5 days $ 545.00
500 μg 5 days $ 2,070.00
1 mg 5 days $ 2,970.00
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Biological Description
Technical Params
Product Properties
Description 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.
Species Human
Expression System E. coli
Tag N-6His
Accession Number P09105
Synonyms Hemoglobin subunit θ-1, Hemoglobin subunit theta-1, Hemoglobin theta-1 chain, Theta-1-globin, HBQ1, θ-1-globin, Hemoglobin θ-1 chain
Amino Acid Met1-Arg142
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.
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight 15&30 KDa, reducing conditions
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0.
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. 
Stability & Storage

Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping

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

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Keywords

HBQ1 Protein, Human, Recombinant (His) HBQ-1 Hemoglobin subunit θ-1 Hemoglobin subunit theta-1 HBQ 1 Hemoglobin theta-1 chain Theta-1-globin HBQ1 θ-1-globin Hemoglobin θ-1 chain recombinant recombinant-proteins proteins protein

 

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