Recombinant Human PCMT1 protein is a Human Full Length protein, in the 1 to 227 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (PubMed:3167043, PubMed:6469980). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Protein-L-isoaspartate(D-aspartate) O-methyltransferase, PIMT, L-isoaspartyl protein carboxyl methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, Protein-beta-aspartate methyltransferase, PCMT1
Recombinant Human PCMT1 protein is a Human Full Length protein, in the 1 to 227 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl
ab95914 is purified using conventional chromatography techniques.
Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (PubMed:3167043, PubMed:6469980). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.
The PCMT1 protein also known as protein-L-isoaspartate (D-aspartate) O-methyltransferase catalyzes the repair of damaged proteins by recognizing and converting abnormal L-isoaspartyl residues to normal L-aspartyl residues. This enzymatic activity is important for maintaining protein integrity and function. The purified form of PCMT1 has a mass of approximately 24 kDa. It is ubiquitously expressed in various tissues with high levels found in the liver and brain emphasizing its essential role across different body systems.
The PCMT1 enzyme plays a significant role in cellular repair mechanisms by rejuvenating proteins that have been altered due to spontaneous deamidation or isomerization. This process is critical for preserving the longevity of proteins and preventing cellular aging and dysfunction. PCMT1 does not generally form part of a complex but works by interacting directly with protein substrates that contain abnormal isoaspartyl residues. It functions independently in its activity and this specificity highlights its importance in maintaining cellular homeostasis.
PCMT1 is an integral component of protein repair pathways specifically the pathways that manage protein maintenance and degradation. These pathways help prevent the accumulation of dysfunctional proteins thereby preserving cell function and survival. PCMT1 activity relates closely to proteins such as CHIP and ubiquitin-proteasome pathway elements which also manage protein quality control within the cell. Together these proteins ensure accurate protein folding and turnover.
PCMT1 activity connects to neurodegenerative disorders like Alzheimer's disease and demyelinating conditions such as multiple sclerosis. The deficiency or dysfunction in PCMT1 could lead to abnormal accumulation of damaged proteins causing cellular stress and contributing to disease pathology. In the context of these conditions PCMT1 has also been linked to other proteins like beta-amyloid in Alzheimer's illustrating the cascading effect that modified protein repair can have on disease development and progression.
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