HAT1 Human

Histone Acetyltransferase 1 Human Recombinant
Cat. No.
BT8474
Source
Escherichia Coli.
Synonyms
EC 2.3.1.48, KAT1, histone acety ltransferase 1, Histone acetyltransferase type B catalytic subunit, HAT1.
Appearance
Sterile Filtered clear 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

HAT1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (20-341 a.a.) and having a molecular mass of 40.1 kDa. The HAT1 is fused to a 21 amino acid His Tag and purified by proprietary chromatographic techniques.

Product Specs

Introduction
HAT1, a type B histone acetyltransferase, plays a crucial role in the acetylation of newly synthesized histones in the cytoplasm. These acetylated histones are then transported into the nucleus for deposition onto newly formed DNA strands. Primarily, HAT1 acetylates soluble histone H4 at lysine residues 5 and 12 and, to a lesser extent, histone H2A at lysine 5. This enzyme is involved in replication-dependent chromatin assembly. Notably, HAT1 exhibits specificity for soluble histone H4, acetylating it at lysines 5 and 12, and displays limited activity towards histone H2A at lysine 5. The enzyme's intrinsic substrate specificity targets lysine residues within the GXGKXG recognition sequence.
Description
Recombinant human HAT1, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 343 amino acids (residues 20-341). With a molecular weight of 40.1 kDa, this protein is fused to a 21 amino acid His tag and purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HAT1 solution is buffered in 20mM Tris-HCl at pH 8 and supplemented with 1mM DTT and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze the solution at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. It is advisable to minimize repeated freeze-thaw cycles.
Purity
The purity of HAT1 is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
EC 2.3.1.48, KAT1, histone acety ltransferase 1, Histone acetyltransferase type B catalytic subunit, HAT1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKKLAEYKCN TNTAIELKLV RFPEDLENDI RTFFPEYTHQ LFGDDETAFG YKGLKILLYY IAGSLSTMFR VEYASKVDEN FDCVEADDVE GKIRQIIPPG FCTNTNDFLS LLEKEVDFKP FGTLLHTYSV LSPTGGENFT FQIYKADMTC RGFREYHERL QTFLMWFIET ASFIDVDDER WHYFLVFEKY NKDGATLFAT VGYMTVYNYY VYPDKTRPRV SQMLILTPFQ GQGHGAQLLE TVHRYYTEFP TVLDITAEDP SKSYVKLRDF VLVKLCQDLP CFSREKLMQG FNEDMAIEAQ QKFKINKQHA RRVYEILRLL VTD.

Product Science Overview

Function and Mechanism

HAT1 specifically acetylates histone H4 at lysines 5 and 12, and to a lesser extent, histone H2A at lysine 5 . This acetylation is essential for replication-dependent chromatin assembly, as it facilitates the incorporation of histones into chromatin and supports chromatin replication . The acetylation of histones by HAT1 is also linked to various biological processes, including cell cycle progression, glucose metabolism, and DNA damage repair .

Biological Significance

Histone acetylation by HAT1 is crucial for the regulation of gene expression. Acetylation neutralizes the positive charge on lysine residues, reducing the affinity between histones and DNA, and making DNA more accessible to transcription factors . This process is associated with transcriptional activation and the formation of euchromatin, which is less densely packed and more transcriptionally active .

Evolutionary Conservation

HAT1 is evolutionarily conserved across species, highlighting its fundamental role in chromatin biology . The enzyme’s ability to acetylate newly synthesized histones before their assembly into nucleosomes is a key aspect of its function . This acetylation is removed by histone deacetylases (HDACs) once the histones are incorporated into chromatin .

Clinical Relevance

Mutations or dysregulation of HAT1 can have significant implications for human health. For example, alterations in histone acetylation patterns are associated with various diseases, including cancer . Understanding the function and regulation of HAT1 can provide insights into the mechanisms underlying these diseases and potentially lead to the development of therapeutic strategies.

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