AHCY Human

Adenosylhomocysteinase Human Recombinant
Cat. No.
BT25929
Source
Escherichia Coli.
Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.
Appearance
Sterile filtered 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.
Shipped with Ice Packs
In Stock

Description

AHCY Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 452 amino acids (1-432 a.a.) and having a molecular mass of 49.8 kDa. The AHCY is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
S-adenosylhomocysteine hydrolase (AHCY) is an essential enzyme involved in the methionine cycle. It catalyzes the breakdown of S-adenosylhomocysteine (SAH) into adenosine and L-homocysteine. This reaction is crucial for regulating the intracellular levels of SAH, a potent inhibitor of methyltransferase enzymes. AHCY deficiency disrupts this balance, leading to a condition known as hypermethioninemia.
Description
This product consists of the recombinant human AHCY enzyme, produced in E. coli. It is a single, non-glycosylated polypeptide chain with 452 amino acids, corresponding to amino acids 1-432 of the native protein. The molecular weight of the recombinant AHCY is 49.8 kDa. For purification and detection purposes, a 20 amino acid His-Tag is fused to the N-terminus of the protein. The purification process involves proprietary chromatographic techniques.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The AHCY Human solution is supplied in a buffer of 20mM Tris (pH 8.0) and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be kept at 4°C. For extended storage, freezing at -20°C is recommended. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. Repeated freezing and thawing of the product should be minimized.
Purity
The purity of this product is greater than 95%, as assessed by SDS-PAGE.
Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, Adenosylhomocysteinase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSDKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMRERYS ASKPLKGARI AGCLHMTVET AVLIETLVTL GAEVQWSSCN IFSTQDHAAA AIAKAGIPVY AWKGETDEEY LWCIEQTLYF KDGPLNMILD DGGDLTNLIH TKYPQLLPGI RGISEETTTG VHNLYKMMAN GILKVPAINV NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI ITEIDPINAL QAAMEGYEVT TMDEACQEGN IFVTTTGCID IILGRHFEQM KDDAIVCNIG HFDVEIDVKW LNENAVEKVN IKPQVDRYRL KNGRRIILLA EGRLVNLGCA MGHPSFVMSN SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMS CDGPFKPDHY RY.

Product Science Overview

Introduction

Adenosylhomocysteinase (AHCY), also known as S-adenosyl-L-homocysteine hydrolase (SAHH), is a crucial enzyme in the methionine cycle. This enzyme is highly conserved across various species, including bacteria, plants, and mammals . The recombinant form of human AHCY is produced using advanced biotechnological methods to study its structure, function, and potential therapeutic applications.

Structure and Function

AHCY is a cytoplasmic tetramer, with each subunit tightly bound to an NAD co-factor . The enzyme catalyzes the reversible hydrolysis of S-adenosyl-L-homocysteine (SAH) into adenosine and homocysteine . This reaction is vital because SAH is a potent inhibitor of methyltransferases, enzymes responsible for transferring methyl groups to various substrates, including DNA, RNA, and proteins .

Biological Significance

The primary role of AHCY is to regulate the intracellular concentration of SAH, thereby facilitating methylation reactions. Methylation is essential for numerous biological processes, including gene expression, DNA repair, and protein function . By breaking down SAH, AHCY ensures that methyltransferases can function efficiently, maintaining cellular homeostasis.

Recombinant Production

Recombinant human AHCY is typically produced in Escherichia coli (E. coli) systems. The recombinant protein often includes an N-terminal His-tag to facilitate purification . The purified enzyme is used in various research applications, including studies on enzyme kinetics, inhibitor screening, and structural analysis.

Pathological Implications

Deficiency in AHCY activity is associated with a rare genetic disorder known as AHCY deficiency. This condition leads to elevated levels of SAH and reduced methylation capacity, resulting in developmental delays, liver dysfunction, and other severe symptoms . Understanding the function and regulation of AHCY is crucial for developing potential therapeutic strategies for this and other related disorders.

Research and Applications

Recombinant AHCY is a valuable tool in biochemical and medical research. It is used to study the enzyme’s role in the methionine cycle, its interaction with other cellular components, and its potential as a therapeutic target. Additionally, AHCY inhibitors are being explored for their potential in treating diseases characterized by aberrant methylation patterns, such as cancer and neurodegenerative disorders .

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