Recombinant Human Alkaline Phosphatase, Tissue Non-Specific protein
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Recombinant Human Alkaline Phosphatase, Tissue Non-Specific protein is a Human Full Length protein, in the 18 to 502 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
AP-TNAP, TNS-ALP, TNSALP, Alkaline phosphatase liver/bone/kidney isozyme, Phosphoamidase, Phosphocreatine phosphatase, ALPL
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
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
Alkaline phosphatase in tissues plays a pivotal role in bone mineralization and development. It functions to hydrolyze phosphate groups releasing inorganic phosphate necessary for bone and teeth formation. It forms part of a larger enzyme complex that interacts with extracellular substrates ensuring the continuous supply of phosphate ions. This enzyme in particular impacts cellular processes involving calcification and cellular differentiation.
Pathways
Alkaline phosphatase operates within phosphate metabolism and signaling pathways. Within the skeletal system it forms part of the regulatory mechanism for osteoblast activity and bone formation. It relates to proteins like osteopontin and bone sialoprotein which regulate the mineralization process. These pathways ensure the balance between phosphate ions and mineral deposition in bone tissue.
Specifications
Form
Liquid
Additional notes
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
General info
Function
Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed : 12162492, PubMed : 23688511, PubMed : 25982064). Has broad substrate specificity and can hydrolyze a considerable variety of compounds : however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates (PubMed : 12162492, PubMed : 2220817). Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate : it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration (PubMed : 23688511, PubMed : 25982064). Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization : while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (By similarity). Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner (By similarity). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters (PubMed : 20049532, PubMed : 2220817). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine : cytosine (poly I : C) (PubMed : 28448526). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle : localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N-phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity).
Sequence similarities
Belongs to the alkaline phosphatase family.
Post-translational modifications
N-glycosylated.
Target data
Product promise
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