Recombinant Human Protective protein/Cathepsin A (PPCA) is a Human Full Length protein, in the 29 to 480 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.
PPGB, CTSA, Lysosomal protective protein, Carboxypeptidase C, Carboxypeptidase L, Cathepsin A, Protective protein cathepsin A, Protective protein for beta-galactosidase, PPCA
Recombinant Human Protective protein/Cathepsin A (PPCA) is a Human Full Length protein, in the 29 to 480 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 7.4
Constituents: 99% Phosphate Buffer, 0.87% Sodium chloride
Purity greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.
Belongs to the peptidase S10 family.
Protective protein/Cathepsin A (PPCA) also known as cathepsin A or protective proteins is an enzyme with a molecular mass of approximately 54 kDa. The enzyme is expressed widely in different tissues including liver kidney and the central nervous system. Mechanically PPCA plays a role as a carboxypeptidase with serine-type protease activity important for the stabilization and activation of lysosomal enzymes such as beta-galactosidase and neuraminidase. This stabilization is vital for proper lysosomal function and the breakdown of glycoproteins within the cell.
In conjunction with these enzymes PPCA forms part of the lysosomal multienzyme complex. It regulates the degradation of sialylated glycoconjugates by ensuring the structural integrity and enzymatic activity of lysosomal enzymes. This regulation prevents the accumulation of substrate materials which can disrupt cellular homeostasis. PPCA's interaction with beta-galactosidase and neuraminidase enables the proper catabolism of glycoproteins and glycolipids which is essential for cellular functions.
PPCA functions within the lysosomal storage and sialic acid catabolism pathways. These pathways are significant for the degradation and recycling of macromolecules in the lysosome maintaining cellular health. In the sialic acid metabolism pathway PPCA pairs with neuraminidase to break down sialylated substrates while interacting closely with beta-galactosidase in glycoprotein catabolism. These interactions highlight its role in preserving the efficiency of lysosomal degradation processes.
Mutations in the PPCA gene can lead to diseases like galactosialidosis and neuraminidase deficiency. Galactosialidosis arises from defective cathepsin A activity disrupting normal glycoprotein breakdown and resulting in storage disorders. This condition involves both beta-galactosidase and neuraminidase which accumulate as a result of PPCA dysfunction. Similarly neuraminidase deficiency exhibits symptoms due to impaired degradation of sialic acids indicating the necessity of PPCA in disease prevention.
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