AHCY Human, Sf9

Adenosylhomocysteinase Human Recombinant, Sf9
Cat. No.
BT25999
Source

Sf9, Baculovirus cells.

Synonyms

EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

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.
Shipped with Ice Packs
In Stock

Description

AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
S-adenosylhomocysteine hydrolase (AHCY) is an enzyme that facilitates the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) into adenosine (Ado) and L-homocysteine (Hcy). AHCY plays a crucial role in regulating intracellular S-adenosylhomocysteine (SAH) levels, which are essential for transmethylation reactions. Deficiency in AHCY can lead to hypermethioninemia.
Description
Recombinant human AHCY, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain comprising 441 amino acids (1-432 a.a.). It has a molecular weight of 48.8kDa and appears as a band between 40-57kDa on SDS-PAGE under reducing conditions. The AHCY protein is fused with a 6 amino acid His-Tag at the C-terminus and purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The AHCY protein solution is provided at a concentration of 0.25mg/ml in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer storage, freezing at -20°C is recommended. To ensure stability during long-term storage, adding a carrier protein like 0.1% HSA or BSA is advisable. Repeated freezing and thawing should be avoided.
Purity
The purity of the AHCY protein is greater than 90% as determined by SDS-PAGE analysis.
Synonyms

EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.

Source

Sf9, Baculovirus cells.

Amino Acid Sequence

ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH H.

Product Science Overview

Introduction

Adenosylhomocysteinase (AHCY) is a crucial enzyme involved in the metabolism of S-adenosylhomocysteine (SAH). The recombinant form of this enzyme, produced in Sf9 Baculovirus cells, is widely used in research to study its function and role in various biological processes.

Structure and Production

The human recombinant AHCY produced in Sf9 cells is a single, glycosylated polypeptide chain containing 441 amino acids, with a molecular mass of approximately 48.8 kDa . This enzyme is fused to a 6-amino acid His-Tag at the C-terminus, which facilitates its purification through chromatographic techniques .

Function and Mechanism

AHCY catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) into adenosine (Ado) and L-homocysteine (Hcy) . This reaction is crucial for maintaining the intracellular concentration of SAH, which is essential for transmethylation reactions . Transmethylation is a vital process in which methyl groups are transferred from one molecule to another, playing a significant role in DNA methylation, protein function, and lipid metabolism .

Biological Significance

The regulation of SAH levels by AHCY is critical for various cellular processes. Methylation, controlled by AHCY, influences gene expression, protein function, and signal transduction . A deficiency in AHCY can lead to hypermethioninemia, a condition characterized by elevated levels of methionine in the blood .

Applications in Research

The recombinant form of AHCY produced in Sf9 cells is used extensively in laboratory research. It allows scientists to study the enzyme’s structure, function, and interactions in a controlled environment. This research can lead to a better understanding of metabolic disorders and the development of potential therapeutic interventions .

Storage and Stability

AHCY (Human Recombinant, Sf9) is typically stored at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage. It is recommended to add a carrier protein, such as 0.1% HSA or BSA, to prevent degradation during storage . The enzyme should be handled carefully to avoid multiple freeze-thaw cycles, which can affect its stability and activity .

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