HBQ1 Protein (His tag)
Quick Overview for HBQ1 Protein (His tag) (ABIN7318571)
Target
See all HBQ1 ProteinsProtein Type
Origin
Source
Purity
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Purification tag / Conjugate
- This HBQ1 protein is labelled with His tag.
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Purpose
- Recombinant Human HBQ1 Protein (His Tag)
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Sequence
- Met 1-Arg142
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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.
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Endotoxin Level
- < 1.0 EU per μg as determined by the LAL method.
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Hemoglobin theta 1 (HBQ1) (AA 1-142) protein (His tag)
custom-made HBQ1 Origin: Human Host: HEK-293 Cells Recombinant > 90 % as determined by Bis-Tris PAGE, anti-tag ELISA, Western Blot and analytical SEC (HPLC)
Hemoglobin theta 1 (HBQ1) (AA 1-142) protein (His-IF2DI Tag)HBQ1 Origin: Human Host: Escherichia coli (E. coli) Recombinant Greater than 90 % as determined by SDS-PAGE. ELISA, WB
Hemoglobin theta 1 (HBQ1) protein (Myc-DYKDDDDK Tag)HBQ1 Origin: Human Host: HEK-293 Cells Recombinant > 80 % as determined by SDS-PAGE and Coomassie blue staining AbP, STD
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Restrictions
- For Research Use only
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Format
- Lyophilized
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Reconstitution
- Please refer to the printed manual for detailed information.
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Buffer
- Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, pH 7.0.
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Storage
- 4 °C,-20 °C,-80 °C
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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.
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- HBQ1 (Hemoglobin theta 1 (HBQ1))
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Alternative Name
- HBQ1
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Background
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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
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Molecular Weight
- 17.7 kDa
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UniProt
- P09105
Target
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