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Histone H3 Tri-Methyl Lys9/H3K9Me3 Polyclonal

Product group: Primary
Monoclonal/ Polyclonal: Polyclonal
Host: Rabbit
Isotype: IgG
Application: Immunohistochemistry (IHC)
Application notes: 50-200
Conjugation Type: Unconjugated
Reactivity: Human
General notes: Localization: cytoplasm.
Buffer: proteinase K 5-10 min at 37°C
UNSPSC code: 12352203

The Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4). In contrast, a more diverse set of histone lysine methyltransferases have been identified, all but one of which contain a conserved catalytic SET domain origin

Lysozyme/Muramidase Polyclonal

Lysozyme is a ubiquitous enzyme defined as muraminidase catalyzing the hydrolysis of the beta glycosidic bond in bacterial peptidoglycan, a major component of the bacterial cell wall. Lysozyme in tissues and body fluids is associated with the monocyte-macrophage system and enhances the activity of immunoagents. Lysozyme C catalyzes the hydrolysis of certain mucopolysaccharides of bacterial cell walls. Specifically, it catalyzes the hydrolysis of the bacterial cell wall beta glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine. It is found in the spleen, lung, kidney, white blood cells, plasma, saliva, milk, and tears. Defects in Lysozyme C are a cause of amyloidosis type 8 (AMYL8), also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. Lysozyme immunoreactivity has been found in myeloid cells, histiocytes, granulocytes, macrophages, and monocytes. It is a good marker for macrophages that are activated in phagocytosis. Lysozyme has been useful in the identification of hitiocytoma.