SETD7 Human

Set7/9 Histone Methyltransferase Human Recombinant
Cat. No.
BT13567
Source
Escherichia Coli.
Synonyms
Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.
Appearance

Sterile Filtered clear solution.

Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec'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

SETD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids & having a molecular mass of 40.7 kDa.
The SETD7 purified by proprietary chromatographic techniques.

Product Specs

Introduction
Set 7/9, in complex with S-adenosyl-L-methionine (AdoMet), functions as a histone methyltransferase (HMTase) that specifically catalyzes the transfer of methyl groups to the Lys4 residue of histone H3. The methylation of lysine residues on histones plays a crucial role in regulating chromatin structure and gene expression. Notably, acetylation, phosphorylation, and methylation of the amino-terminal tails of histones are believed to be involved in modulating chromatin structure and function. The enzymes responsible for methylating specific lysine residues on histones predominantly belong to the SET family, with Set7/9 being a notable exception. Unlike most SET proteins, Set7/9 exhibits exclusive mono-methylase activity.
Description
Recombinant Human SETD7, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 40.7 kDa, comprising 366 amino acids. The purification of SETD7 is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered clear solution.
Formulation
The protein is supplied in a buffer consisting of 50mM Tris-HCl (pH 7.5), 0.2M NaCl, 5mM DTT, and 20% glycerol.
Stability
For short-term storage (1-2 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of the protein is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Histone-lysine N-methyltransferase, H3 lysine-4 specific SET7, EC 2.1.1.43, Histone H3-K4 methyltransferase, H3-K4-HMTase, SET domain-containing protein 7, Set9, SET7/9, SETD7.
Source
Escherichia Coli.
Amino Acid Sequence
MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF QATQQK

Product Science Overview

Introduction

Set7/9, also known as SETD7, is a lysine-specific histone methyltransferase that plays a crucial role in the regulation of gene expression through the methylation of histone and non-histone proteins. This enzyme is involved in various cellular processes, including stemness, differentiation, and development.

Discovery and Structure

Set7/9 was first identified in 2001 when it was purified and characterized from the human cervical cancer cell line HeLa . The enzyme contains a SET domain, which is responsible for its methyltransferase activity. The SET domain is a conserved region found in many proteins across different species, indicating its evolutionary importance .

Function and Mechanism

Set7/9 specifically monomethylates lysine 4 on histone H3 (H3K4me1), a modification associated with transcriptional activation . The enzyme forms a complex with S-adenosyl-L-methionine (SAM), which serves as the methyl group donor. The active site of Set7/9 includes a binding pocket for SAM and a narrow substrate-specific channel that only allows unmethylated lysine residues to access .

In addition to histone methylation, Set7/9 also methylates several non-histone proteins, including p53, pRb, YAP, DNMT1, SOX2, and FOXO3 . These modifications play a significant role in regulating various cellular functions, such as cell cycle progression, apoptosis, and stem cell maintenance.

Biological Significance

The methylation of histones by Set7/9 is essential for the regulation of chromatin structure and gene expression. This process influences various biological processes, including embryogenesis, tissue development, and cellular differentiation . The balance between cellular stemness and differentiation is crucial for the development of multicellular organisms, and Set7/9 plays a pivotal role in maintaining this balance .

Pathological Implications

Aberrant activity of Set7/9 has been linked to several pathological conditions, including cancer. The enzyme’s role in regulating the methylation of non-histone proteins, such as p53 and pRb, suggests that it may contribute to the formation and maintenance of cancer stem cells . Understanding the function and regulation of Set7/9 could provide valuable insights into the development of therapeutic strategies for cancer and other diseases associated with abnormal cellular differentiation and self-renewal.

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