Recombinant Human Acid Phosphatase 2 protein (denatured)
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Recombinant Human Acid Phosphatase 2 protein (denatured) is a Human Fragment protein, in the 31 to 380 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
Lysosomal acid phosphatase, LAP, ACP2
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Acid Phosphatase 2 protein (denatured) (AB202151)
15% SDS-PAGE analysis of ab202151 (3 μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Acid Phosphatase 2 participates in the degradation of intracellular biomolecules and recycling of phosphate groups. It works in association with other lysosomal enzymes forming an important component of the lysosomal degradation complex. Within the lysosome it assists in processing macromolecules like nucleotides lipids and glycans contributing to cellular nutrient and energy homeostasis. By cleaving phosphate from a diverse range of substrates ACP2 aids in maintaining cellular function and growth.
Pathways
Acid phosphatases influence the lysosomal degradation pathway and play roles in phosphate metabolism. ACP2 interacts with enzymes involved in lysosomal functions like cathepsins and glucocerebrosidase which drive the breakdown of cellular debris. Furthermore ACP2 activity is intertwined with the mTOR signaling pathway impacting cellular growth and autophagy processes by regulating nutrient availability at the cellular level. This integration into metabolic pathways highlights its significance in regulating metabolic flux between degradation and biosynthesis.
Specifications
Form
Liquid
General info
Sequence similarities
Belongs to the histidine acid phosphatase family.
Post-translational modifications
The membrane-bound form is converted to the soluble form by sequential proteolytic processing. First, the C-terminal cytoplasmic tail is removed. Cleavage by a lysosomal protease releases the soluble form in the lysosome lumen.. N-glycosylated. The intermediates formed during enzymatic deglycosylation suggest that all eight predicted N-glycosylation sites are used.
Subcellular localisation
Lysosome membrane
Target data
Product promise
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