Rabbit Polyclonal PNMT antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human PNMT aa 50 to C-terminus.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
IHC-P | WB | |
---|---|---|
Human | Tested | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes Suggested antigen retrieval using heat mediated 10mM Citrate buffer (pH6.0) or Tris-EDTA buffer (pH8.0) Perform heat-mediated antigen retrieval before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
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Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor (PubMed:20496117). Other substrates include phenylethanolamine and octopamine (PubMed:16277617, PubMed:16363801, PubMed:8812853). Also methylates normetanephrine (By similarity).
PENT, PNMT, Phenylethanolamine N-methyltransferase, PNMTase, Noradrenaline N-methyltransferase
Rabbit Polyclonal PNMT antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Human PNMT aa 50 to C-terminus.
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
The protein PNMT also known as Phenylethanolamine N-methyltransferase functions as an enzyme responsible for the methylation of norepinephrine to synthesize epinephrine. It belongs to the methyltransferase family and weighs approximately 30 kDa. PNMT is highly expressed in the adrenal medulla particularly in chromaffin cells but also found in smaller amounts in some parts of the brain such as the medulla oblongata and retina. This distribution supports its role in catecholamine biosynthesis and regulation.
The conversion of norepinephrine to epinephrine increases the functionality of PNMT in stress response mechanisms. PNMT plays an important role in the synthesis of catecholamines which are essential for modulating the fight-or-flight response. It does not form part of a larger protein complex but interacts with substrates and cofactors directly to catalyze its reactions. PNMT's activity is carefully regulated by factors including substrate availability and enzyme expression levels in tissues where it operates.
Norepinephrine to epinephrine synthesis conducted by PNMT marks the final step in the catecholamine biosynthetic pathway. This pathway is critical in managing cardiovascular and metabolic functions. The protein connects extensively with enzymes such as tyrosine hydroxylase and dopamine β-hydroxylase within this pathway which are involved in prior steps of catecholamine synthesis. PNMT's activity and regulation are therefore essential for maintaining homeostasis in stress and energy metabolism.
PNMT connects directly to conditions like hypertension and certain phaeochromocytomas which arise from catecholamine excess or imbalance. Elevated levels of PNMT can be found in tumors linked to the adrenal medulla affecting the production of epinephrine. PNMT's interaction with enzymes like dopamine β-hydroxylase is relevant in understanding these disorders since imbalances in enzyme activity can lead to disrupted catecholamine synthesis contributing to disease pathogenesis.
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Immunohistochemical analysis of formalin-fixed, paraffin-embedded U87 xenograft labeling PNMT with ab154282 at 1/500.
All lanes: Western blot - Anti-PNMT antibody (ab154282) at 1/1000 dilution
All lanes: HepG2 whole cell lysate at 30 µg
Predicted band size: 31 kDa
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