HBQ1 Protein, Human, Recombinant (His)

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产品编号 TMPJ-00812

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.

HBQ1 Protein, Human, Recombinant (His)

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SPR兼容缓冲液

产品编号 TMPJ-00812

规格	价格	库存
5 μg	¥ 693	6-8日内发货
10 μg	¥ 1,170	6-8日内发货
20 μg	¥ 1,860	5日内发货
50 μg	¥ 3,470	5日内发货
100 μg	¥ 5,180	5日内发货
200 μg	¥ 7,730	5日内发货
500 μg	¥ 13,200	5日内发货
1 mg	¥ 18,900	5日内发货

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产品信息

生物活性	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
产品描述	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.
种属	Human
表达系统	E. coli
标签	N-6xHis
蛋白编号	P09105
别名	θ-1-globin,Theta-1-globin,Hemoglobin θ-1 chain,Hemoglobin theta-1 chain,Hemoglobin subunit θ-1,Hemoglobin subunit theta-1,HBQ1
氨基酸序列	Met1-Arg142
蛋白构建	Met1-Arg142
蛋白纯度	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
分子量	15&30 KDa (reducing condition)
内毒素	< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
缓冲液	Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM PB, 150 mM NaCl, pH 7.0.
复溶方法	Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
存储	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
运输方式	In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
研究背景	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.