HRP-Labeled Alkaline Phosphatase/ALPL Protein, Human (HEK293, His)

HRP-Labeled Alkaline Phosphatase/ALPL Protein, Human (HEK293, His) is the recombinant human-derived HRP-Labeled Alkaline Phosphatase/ALPL protein, expressed by HEK293, with C-His tag.

Alkaline Phosphatase (ALP) is an enzyme that metabolizes various phosphate compounds and plays a crucial role in skeletal mineralization and adaptive thermogenesis. It exhibits broad substrate specificity, hydrolyzing a wide range of compounds, though its natural substrates primarily include diphosphate (inorganic pyrophosphate, PPi), pyridoxal 5’-phosphate (PLP), and N-phosphocreatine. By hydrolyzing extracellular diphosphate—a potent mineralization inhibitor—into phosphate, ALP promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration, thereby playing a vital role in skeletal and dental mineralization (By similarity). It functions non-redundantly with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 initiates hydroxyapatite crystallization in matrix vesicles (MVs), ALPL/TNAP facilitates its propagation. Additionally, ALP catalyzes the dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, ensuring sufficient PLP availability in the brain as a cofactor for neurotransmitter-synthesizing enzymes. The enzyme also mediates stepwise ATP degradation to adenosine, regulating purinergic receptor ligand availability (By similarity), and dephosphorylates microbial products (e.g., lipopolysaccharides, LPS) and phosphorylated small molecules (e.g., poly-inosine:cytosine, poly I:C). In adaptive thermogenesis, ALP acts as a key regulator in the futile creatine cycle by hydrolyzing N-phosphocreatine to initiate a cycle of creatine dephosphorylation and phosphorylation, dissipating energy as heat without performing mechanical or chemical work (By similarity).

Human

HEK293

C-His

P05186-1 (L18-S502)

249

Partial

Approximately 40-43 kDa,60-65 kDa & 180 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.