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Rabbit anti-Mus musculus (Mouse) Alpl Polyclonal Antibody

The antibody against Alpl was raised in rabbit using the Recombinant Mouse Alkaline phosphatase, tissue-nonspecific isozyme protein (20-503AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.

ADC-50771A

The antibody against Alpl was raised in rabbit using the Recombinant Mouse Alkaline phosphatase, tissue-nonspecific isozyme protein (20-503AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA.

$299.00

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Specifications


Cat.No ADC-50771A ClonalityPolyclonal
Host SpeciesRabbitTarget NameALPL
FormLiquidSpecies ReactivityMouse
IsotypeIgGStorage Buffer0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4
Purification Method>95%, Protein G purifiedConjugateNon-conjugated
ApplicationELISAStorageUpon receipt

Immunogen Information


Immunogen DescriptionRecombinant Mouse Alkaline phosphatase, tissue-nonspecific isozyme protein (20-503AA)Target SpeciesMus musculus (Mouse)
Immunogen SequenceComplete sequences for the immunogen, target protein, and peptides are available upon request.Uniprot IDP09242
Background Information
  • Uniprot Id

    P09242

  • Target Species

    Mouse

  • Target Name

    ALPL

  • Target Full Name

    Alkaline phosphatase, tissue-nonspecific isozyme

  • Target Function

    Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis. 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. 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. 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. 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. 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. Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors. 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). 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. 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.

  • Target Subcellular Location

    Cell membrane; Lipid-anchor, GPI-anchor. Extracellular vesicle membrane; Lipid-anchor, GPI-anchor. Mitochondrion membrane; Lipid-anchor, GPI-anchor. Mitochondrion intermembrane space.

  • Target Protein Families

    Alkaline phosphatase family

  • Target Tissue Specificity

    Widely expressed. Expressed in DRG neurons and spinal cord neurons.

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