KMT5A Human
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
Greater than 85.0% as determined by SDS-PAGE.
Description
KMT5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 165 amino acids (195-352 a.a.) and having a molecular mass of 18.9kDa (Migrates at 18-28 kDa on SDS-PAGE under reducing conditions).
KMT5A is expressed with a 7 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Lysine Methyltransferase 5A (KMT5A), also known as SETD8 or SET8, is an enzyme that plays a crucial role in regulating various cellular processes. It catalyzes the addition of a methyl group to lysine residues on both histone and non-histone proteins. This methylation activity is essential for maintaining the structural integrity of DNA, especially during cell division. KMT5A is involved in controlling gene expression, particularly in silencing genes during specific cell cycle phases and mitosis. It acts as a safeguard against premature cellular aging by regulating metabolic processes through chromatin modifications. KMT5A directly influences the tumor suppressor protein p53 by mediating its monomethylation, which in turn suppresses the expression of genes regulated by p53. Loss of KMT5A can disrupt normal cellular functions, leading to increased nucleolar activity and alterations in mitochondrial metabolism regulated by the retinoblastoma protein.
This product consists of the recombinant human KMT5A protein, specifically amino acids 195 to 352, produced in Sf9 insect cells using baculovirus expression system. It is a single polypeptide chain with a 7 amino acid Histidine tag at the C-terminus to facilitate purification. The protein has a molecular weight of 18.9 kDa and appears as a band between 18-28 kDa on SDS-PAGE under reducing conditions due to glycosylation. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
The KMT5A protein is supplied in a solution containing 20mM Tris-HCl buffer at pH 8.0, 5mM DTT (reducing agent), 0.2M NaCl (salt), 1mM EDTA (chelating agent), and 50% glycerol (cryoprotectant). The protein concentration is 0.25mg/ml.
The purity of the KMT5A protein is greater than 85%, as determined by SDS-PAGE analysis.
KMT5A, PR-Set7, SET07, SET8, SETD8, H4-K20-HMTase KMT5A.
MKAELQSEER KRIDELIESG KEEGMKIDLI DGKGRGVIAT KQFSRGDFVV EYHGDLIEIT DAKKREALYA QDPSTGCYMY YFQYLSKTYC VDATRETNRL GRLINHSKCG NCQTKLHDID GVPHLILIAS RDIAAGEELL YDYGDRSKAS IEAHPWLKHH HHHHH.
Product Science Overview
KMT5A is unique in its ability to monomethylate lysine 20 on histone H4 (H4K20me1), a modification that is essential for various cellular processes . The enzyme uses S-adenosyl methionine (SAM) as a methyl group donor to transfer a methyl group to the ε-amine group of the lysine residue . This methylation increases the hydrophobic and basic nature of the lysine residue, allowing other proteins to recognize and bind to the methylated lysine .
The activity of KMT5A is implicated in several critical cellular functions, including:
- DNA Replication: KMT5A-mediated methylation of H4K20 is crucial for the proper progression of DNA replication .
- DNA Damage Response: The enzyme plays a role in the cellular response to DNA damage, helping to maintain genomic stability .
- Transcription Regulation: By modifying histones, KMT5A can influence the transcription of specific genes, either activating or repressing their expression .
- Cell Cycle Regulation: KMT5A is involved in the regulation of the cell cycle, ensuring proper cell division and proliferation .
Given its central role in essential cellular processes, dysregulation of KMT5A activity has been linked to various diseases, including cancer. Overexpression or mutations in the KMT5A gene can lead to aberrant cell proliferation and tumorigenesis . As a result, KMT5A is considered a potential target for therapeutic intervention in cancer treatment .
