HBQ1 Human

Hemoglobin Theta 1 Human Recombinant
Cat. No.
BT20087
Source
Escherichia Coli.
Synonyms
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

HBQ1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 17.9kDa.
HBQ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
HBQ1, a member of the Hemoglobin family, is a 66.7 kDa protein. It comprises four iron-binding, methenelinked tetrapyrrole rings (heme) attached to the protein. The globin part of HBQ1 consists of two alpha and two beta chains, organized as pairs to form a tetramer. Each of these four globin chains is covalently bonded to a heme group. The bonds between alpha and beta chains are weaker compared to those between identical globin chains. This difference in bond strength creates a cleavage plane crucial for oxygen binding and release. When the alpha1-beta2 cleavage plane relaxes, it leads to a high affinity for oxygen.
Description
Recombinant HBQ1 Human, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 165 amino acids (residues 1-142) and has a molecular weight of 17.9 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HBQ1 solution is prepared in a buffer containing 20mM Tris-HCl (pH 8.0), 0.15M NaCl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to store the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of HBQ1 is determined to be greater than 90% based on SDS-PAGE analysis.
Synonyms
Hemoglobin Theta 1, Hemoglobin Theta-1 Chain, Hemoglobin Subunit Theta-1, Theta-1-globin.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMALSAED RALVRALWKK LGSNVGVYTT EALERTFLAF PATKTYFSHL DLSPGSSQVR AHGQKVADAL SLAVERLDDL PHALSALSHL HACQLRVDPA SFQLLGHCLL VTLARHYPGD FSPALQASLD KFLSHVISAL VSEYR

Product Science Overview

Gene and Expression

The HBQ1 gene is part of the human alpha-globin gene cluster, which includes five functional genes and two pseudogenes . Theta-globin mRNA is primarily found in human fetal erythroid tissue but is not present in adult erythroid or other non-erythroid tissues .

Structure and Function

Hemoglobin Theta 1 consists of 142 amino acids and has a molecular mass of approximately 17.9 kDa . The recombinant form of this protein is often produced in E. coli and is fused to a His-tag at the N-terminus to facilitate purification . The protein’s structure allows it to bind oxygen with high affinity, which is essential for its role in oxygen transport.

Recombinant Production

Recombinant human HBQ1 is produced using conventional chromatography techniques. The protein is expressed in E. coli and purified to a high degree of purity, typically greater than 90% as determined by SDS-PAGE . The recombinant protein is often used in research to study hemoglobin function and structure.

Applications

Recombinant HBQ1 is used in various research applications, including studies on hemoglobin function, oxygen binding, and the effects of mutations on hemoglobin structure and function. It is also used in the development of therapeutic agents and in the study of hemoglobin-related diseases.

Storage and Handling

Recombinant HBQ1 should be stored at 4°C for short-term use and at -20°C for long-term storage. It is important to avoid freeze-thaw cycles to maintain protein integrity .

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