HNMT Human

Histamine N-Methyltransferase Human Recombinant
Cat. No.
BT8541
Source
Escherichia Coli.
Synonyms
HMT, HNMT-S1, HNMT-S2, HNMT, Histamine N-methyltransferase.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 95.0% 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

HNMT Human Recombinant fused to 36 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 328 amino acids (1-292) and having a molecular mass of 37 kDa.
The HNMT is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Histamine N-methyltransferase (HNMT) is a cytosolic enzyme that utilizes S-adenosyl-L-methionine as a methyl donor for histamine inactivation. In the mammalian brain, N(tau)-methylation of histamine, regulated by HNMT, is crucial for controlling neurotransmitter activity, especially because diamine oxidase, another histamine-degrading enzyme, is absent in the central nervous system. Notably, a known genetic polymorphism affects HNMT activity in red blood cells. This enzyme plays a critical role in histamine degradation and modulates airway responsiveness to histamine. Histamine itself is a crucial immunomodulator, acting through four distinct receptor subtypes (H1, H2, H3, and H4) on target cells. HNMT-mediated histamine inactivation occurs in various tissues, including the bronchus, kidney, and central nervous system.
Description
Recombinant human HNMT, with a 36-amino acid His-tag at its N-terminus, is produced in E. coli. This purified protein is a single, non-glycosylated polypeptide chain containing 328 amino acids (residues 1-292) with a molecular weight of 37 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The HNMT solution is formulated in 20mM Tris-HCl buffer at pH 8.0 and contains 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To ensure long-term stability during frozen storage, consider adding a carrier protein like HSA or BSA (0.1%). Avoid repeated freeze-thaw cycles.
Purity
The purity of HNMT is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
HMT, HNMT-S1, HNMT-S2, HNMT, Histamine N-methyltransferase.
Source
Escherichia Coli.
Amino Acid Sequence

MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASS MRSLFSDHGK YVESFRRFLN HSTEHQCMQE FMDKKLPGII GRIGDTKSEI KILSIGGGAG EIDLQILSKV QAQYPGVCIN NEVVEPSAEQ IAKYKELVAK TSNLENVKFA WHKETSSEYQ SRMLEKKELQ KWDFIHMIQM LYYVKDIPAT LKFFHSLLGT NAKMLIIVVS GSSGWDKLWK KYGSRFPQDD LCQYITSDDL TQMLDNLGLK YECYDLLSTM DISDCFIDGD ENGDLLWDFL TETCNFNATA PPDLRAELGK DLQEPEFSAK KEGKVLFNNT LSFIVIEA.

Product Science Overview

Introduction

Histamine N-Methyltransferase (HNMT) is an enzyme encoded by the HNMT gene in humans. It belongs to the methyltransferases superfamily of enzymes and plays a crucial role in the inactivation of histamine, a biomolecule involved in various physiological processes .

Function and Mechanism

HNMT transfers a methyl group from S-adenosyl-L-methionine (SAM-e) to histamine, forming an inactive metabolite called Nτ-methylhistamine. This process, known as Nτ-methylation, is essential for regulating histamine levels in the body . In mammals, HNMT operates alongside diamine oxidase (DAO) as the only two enzymes responsible for histamine metabolism. However, HNMT is unique in its presence within the central nervous system (CNS), where it governs histaminergic neurotransmission .

Biological Significance

Histamine is a biogenic amine that acts as a messenger in cell-to-cell communication. It is a mediator in allergic responses, a regulator of gastric acid secretion, a messenger in bronchial asthma, and a neurotransmitter in the CNS . The local action of histamine is terminated primarily by methylation through HNMT. This enzyme is particularly important in bronchial epithelial and endothelial cells of the human airways and gut, and it is the only enzyme responsible for terminating the neurotransmitter action of histamine in the brain .

Genetic and Structural Aspects

The HNMT gene is located on chromosome 2q22.1 and consists of six exons . HNMT has a two-domain structure, with the larger N-terminal domain being a classic methyltransferase fold with an SAM binding motif . There are two polymorphic forms of human HNMT, which differ at residue 105. These polymorphisms correlate with high-activity (Thr105) and low-activity (Ile105) phenotypes . The structural differences between these variants affect their kinetic properties and stability at different temperatures .

Recombinant HNMT

Recombinant human HNMT is produced using genetic engineering techniques to express the HNMT gene in a host organism, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant HNMT is used to study the enzyme’s structure, function, and role in histamine metabolism, as well as to develop potential inhibitors for therapeutic applications .

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HNMT Human, Active
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Cat. No.
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Source
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