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AB222955

Recombinant mouse Alkaline Phosphatase, Tissue Non-Specific protein (Active) (His tag C-Terminus)

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Recombinant mouse Alkaline Phosphatase, Tissue Non-Specific protein (Active) (His tag C-Terminus) is a Mouse Fragment protein, in the 19 to 503 aa range, expressed in Baculovirus infected insect cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.

View Alternative Names

Akp-2, Akp2, Alpl, AP-TNAP, TNAP, TNSALP, Alkaline phosphatase 2, Alkaline phosphatase liver/bone/kidney isozyme, Phosphoamidase, Phosphocreatine phosphatase

1 Images
SDS-PAGE - Recombinant mouse Alkaline Phosphatase, Tissue Non-Specific protein (Active) (AB222955)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant mouse Alkaline Phosphatase, Tissue Non-Specific protein (Active) (AB222955)

15% SDS-PAGE analysis of 3 μg ab222955.

MWt 50-70 kDa (SDS-PAGE under reducing conditions) .

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Baculovirus infected insect cells

Tags

His tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity is > 46,000 pmol/min/μg and is defined as the amount of enzyme that hydrolyze 1 pmole of 4-Methylumbelliferyl phosphate to phosphate and 4-Methylumbelliferone per minute at pH 8.8 at 25°C.

Accession

P09242

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

pH: 7.4 Constituents: PBS, 10% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"VPEKERDPSYWRQQAQETLKNALKLQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNTGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERTRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIKDIDVIMGGGRKYMYPKNRTDVEYELDEKARGTRLDGLDLISIWKSFKPRHKHSHYVWNRTELLALDPSRVDYLLGLFEPGDMQYELNRNNLTDPSLSEMVEVALRILTKNLKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDQAIGKAGAMTSQKDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVDGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHVMAYASCIGANLDHCAWAGSGLEHHHHHH","proteinLength":"Fragment","predictedMolecularWeight":"54.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":503,"aminoAcidStart":19,"nature":"Recombinant","expressionSystem":"Baculovirus infected insect cells","accessionNumber":"P09242","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alkaline Phosphatase Tissue Non-Specific also referred to as ALPL or alkaline phosphatase protein functions mechanically as a hydrolase enzyme. It catalyzes the dephosphorylation of molecules contributing to phosphate and mineral metabolism. This enzyme with a molecular mass of approximately 57 kDa exhibits expression in various tissues including liver bone and kidneys. Researchers can use techniques like alkaline phosphatase ELISA and immunohistochemistry to study its expression and localization.
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.

Alkaline phosphatase abnormalities correlate with hypophosphatasia and rickets. Hypophosphatasia results from mutations in the ALPL gene causing defective bone mineralization. In cases of rickets improper phosphate metabolism can occur due to dysfunctional enzyme activity. The imbalance in alkaline phosphatase activity also connects to disorders like hyperparathyroidism where calcium and phosphate homeostasis is disrupted involving proteins such as parathyroid hormone.

Specifications

Form

Liquid

Additional notes

Affinity purified

General info

Function

Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed : 10620060, PubMed : 11028439, PubMed : 14982838, PubMed : 23942722, PubMed : 33981039). 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 : 19874193, PubMed : 23942722, PubMed : 33981039). 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 : 10620060, PubMed : 11004006, PubMed : 11028439, PubMed : 12082181, PubMed : 14982838, PubMed : 32035618, PubMed : 9056646). 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 (PubMed : 20684022, PubMed : 26457330). 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 (PubMed : 23427088). 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 : 7550313). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (PubMed : 19874193, PubMed : 23825434, PubMed : 23942722, PubMed : 32028019). 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) (By similarity). 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 (PubMed : 33981039). 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 (PubMed : 33981039).

Sequence similarities

Belongs to the alkaline phosphatase family.

Post-translational modifications

N-glycosylated.

Product protocols

Target data

Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed : 10620060, PubMed : 11028439, PubMed : 14982838, PubMed : 23942722, PubMed : 33981039). 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 : 19874193, PubMed : 23942722, PubMed : 33981039). 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 : 10620060, PubMed : 11004006, PubMed : 11028439, PubMed : 12082181, PubMed : 14982838, PubMed : 32035618, PubMed : 9056646). 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 (PubMed : 20684022, PubMed : 26457330). 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 (PubMed : 23427088). 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 : 7550313). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (PubMed : 19874193, PubMed : 23825434, PubMed : 23942722, PubMed : 32028019). 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) (By similarity). 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 (PubMed : 33981039). 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 (PubMed : 33981039).
See full target information Alpl

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