GPHB5 Human

Thyrostimulin Beta Human Recombinant
Cat. No.
BT20819
Source
Escherichia Coli.
Synonyms
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

GPHB5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 120 amino acids and having a total molecular mass of 13.34 kDa. The Thyrostimulin contains His tag which consists of 14 additional amino acids.
The amino acid sequence of the recombinant human Thyrostimulin beta subunit is 100% homologous to the amino acid sequence of the human Thyrostimulin beta subunit without signal sequence. (N-terminal 24AA).
Thyrostimulin is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Human thyrostimulin is a member of the glycoprotein hormone family. These hormones consist of two subunits, a common alpha-subunit and a specific beta-subunit, which combine non-covalently to form a heterodimer. The alpha-subunit can interact with four different beta-subunits, resulting in four active hormones in humans: FSH, LH, TSH, and CG. Primarily produced in the anterior pituitary, FSH, LH, and TSH are crucial for endocrine regulation within the hypothalamus-pituitary axis. These hormones act by activating specific G protein-coupled receptors located in the thyroid (TSH receptor) and gonads (LH and FSH receptors). Notably, these heterodimeric glycoprotein hormones are found exclusively in vertebrates and exhibit a high degree of conservation in both their amino acid sequences and functional characteristics across various species, ranging from primitive rayfin fish (Chondrostei) to humans. Corticotroph-derived glycoprotein hormone (CGH), also known as thyrostimulin, is a heterodimer composed of glycoprotein hormone alpha 2 (GPHA2) and glycoprotein hormone beta 5 (GPHB5). Recombinant A2/B5 heterodimeric glycoproteins demonstrate specific activation of human TSH receptors, without affecting LH or FSH receptors, and exhibit high affinity for TSH receptors in radioligand receptor assays. Furthermore, this heterodimer stimulates cAMP production and thymidine incorporation in cultured thyroid cells and increases serum thyroxine levels in TSH-suppressed rats in vivo, indicating its thyroid-stimulating activity. The presence of thyrostimulin in the anterior pituitary, a known site of TSH receptor expression, suggests a potential paracrine regulatory mechanism.
Description
Recombinant Human GPHB5, produced in E. coli, is a single, non-glycosylated polypeptide chain comprised of 120 amino acids, resulting in a molecular weight of 13.34 kDa. This Thyrostimulin variant includes a His tag consisting of 14 additional amino acids. The amino acid sequence of recombinant human Thyrostimulin beta subunit exhibits 100% homology to the corresponding sequence in the native human Thyrostimulin beta subunit, excluding the signal sequence (N-terminal 24 amino acids). Thyrostimulin undergoes purification using proprietary chromatographic techniques.
Physical Appearance
White, lyophilized powder, filtered for purity.
Formulation
GPHB5 is filtered through a 0.4 μm filter and subsequently lyophilized from a solution of 0.5 mg/ml in 0.05 M Acetate buffer at pH 4.
Solubility
To prepare a working stock solution of approximately 0.5 mg/ml, it is recommended to reconstitute the lyophilized GPHB5 pellet with 0.1 M Acetate buffer at pH 4, ensuring complete dissolution. For dilutions at higher pH values, it is advisable to dilute the stock solution extensively with the appropriate buffer to a concentration of 10 μg/ml, as the protein exhibits limited solubility at higher concentrations. Please note that this product is not sterile. Before using it in cell culture, filtration through a suitable sterile filter is necessary.
Stability
While lyophilized Thyrostimulin remains stable at room temperature for up to 3 weeks, storage in a desiccated state below -18°C is recommended. Once reconstituted, GPHB5 should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term storage. For optimal long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of GPHB5 is greater than 95.0%, as determined by the following methods: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Synonyms
Glycoprotein hormone beta-5, ZLUT1, GPHB5, GPB5.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASASSGNL RTFVGCAVRE FTFLAKKPGC RGLRITTDAC WGRCETWEKP ILEPPYIEAH HRVCTYNETK QVTVKLPNCA PGVDPFYTYP VAIRCDCGAC STATTECETI.

Product Science Overview

Introduction

Thyrostimulin is a novel glycoprotein hormone that was discovered in the early 2000s. It is composed of two subunits: glycoprotein hormone alpha 2 (GPA2) and glycoprotein hormone beta 5 (GPB5). These subunits heterodimerize to form thyrostimulin, which activates the thyroid-stimulating hormone receptor (TSHR) and exhibits thyrotropic activity .

Discovery and Structure

The discovery of thyrostimulin was a result of mining human sequence databases for similarities to known glycoprotein hormone subunits. GPA2 and GPB5 were identified as potential new subunits due to their homology to the common glycoprotein alpha-subunit (GPA1) and the glycoprotein hormone beta-subunit family, respectively . Both subunits have conserved cysteine-knot and N-glycosylation motifs, which are characteristic of glycoprotein hormones .

Expression and Function

Thyrostimulin is expressed in various tissues, including the pituitary gland, eye, and testis. Immunological studies have shown that GPA2 and GPB5 co-localize in pituitary cells, although their expression levels can vary significantly . In vitro studies have demonstrated that recombinant human GPA2 and GPB5 form a heterodimeric glycoprotein hormone that binds to TSHR with an affinity similar to that of thyroid-stimulating hormone (TSH) .

Evolutionary Significance

The presence of GPA2 and GPB5 in both protostomes and deuterostomes indicates their ancestral origin in the glycoprotein hormone family . Phylogenetic analysis suggests that these subunits have been conserved across species, including mammals, fish, and amphibians . The evolutionary history of thyrostimulin highlights its significance in the diversification and functional specialization of glycoprotein hormones .

Clinical Implications

The discovery of thyrostimulin has opened new avenues for research into thyroid function and regulation. Its ability to activate TSHR and stimulate thyroid activity suggests potential therapeutic applications in conditions related to thyroid dysfunction . Further studies are needed to explore the clinical relevance of thyrostimulin and its potential as a diagnostic or therapeutic tool.

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Source
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