Enzymes
Product List
ALPL Mouse
Alkaline Phosphatase Liver/Bone/Kidney Mouse Recombinant
ALPP Human
Alkaline Phosphatase Placental Human Recombinant
ALPP Human, Active
Alkaline Phosphatase Placental Human Recombinant, BioActive
Human ALPP, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain with a molecular weight of 53.9 kDa. It consists of 494 amino acids (23-506 a.a.) and includes a 10 amino acid His tag at the C-terminus. Purification is achieved through proprietary chromatographic methods.
Alkaline Phosphatase Bovine
Alkaline Phosphatase Bovine Intestinal
ALPL Human
Alkaline Phosphatase Human Recombinant
HEK293.
Introduction
Alkaline Phosphatase (ALP) is an enzyme that catalyzes the hydrolysis of phosphate esters, releasing inorganic phosphate and alcohol. It operates optimally at an alkaline pH, typically around 10. ALP is classified into several isoenzymes based on their tissue of origin, including liver, bone, kidney, and intestinal ALP.
Key Biological Properties: ALP is a homodimeric enzyme with each subunit containing a zinc ion crucial for its catalytic activity. It is a membrane-bound glycoprotein.
Expression Patterns: ALP is expressed in various tissues, with the highest levels found in the liver, bone, kidney, and intestines.
Tissue Distribution: The distribution of ALP isoenzymes varies, with liver ALP predominantly found in hepatocytes, bone ALP in osteoblasts, and intestinal ALP in the brush border of enterocytes.
Primary Biological Functions: ALP plays a critical role in dephosphorylation processes, which are essential for various metabolic pathways. It is involved in the mineralization of bones and teeth by hydrolyzing pyrophosphate, an inhibitor of hydroxyapatite formation.
Role in Immune Responses: ALP is implicated in modulating immune responses by dephosphorylating lipopolysaccharides (LPS) on bacterial surfaces, reducing their toxicity and inflammatory potential.
Pathogen Recognition: By dephosphorylating LPS, ALP aids in the recognition and neutralization of pathogens, contributing to the body’s defense mechanisms.
Mechanisms with Other Molecules and Cells: ALP interacts with various substrates, including nucleotides, proteins, and alkaloids, facilitating their dephosphorylation.
Binding Partners: ALP binds to zinc and magnesium ions, which are essential for its structural integrity and catalytic activity.
Downstream Signaling Cascades: The dephosphorylation activity of ALP can influence downstream signaling pathways, such as those involved in bone formation and immune responses.
Regulatory Mechanisms: The expression and activity of ALP are tightly regulated at multiple levels, including transcriptional and post-translational modifications.
Transcriptional Regulation: ALP gene expression is regulated by various transcription factors, including Runx2 and Osterix, which are critical for osteoblast differentiation and bone formation.
Post-Translational Modifications: ALP undergoes glycosylation, which is essential for its stability, localization, and activity. Phosphorylation and proteolytic cleavage also modulate its function.
Biomedical Research: ALP is widely used as a marker for osteoblast activity and bone formation in research studies.
Diagnostic Tools: Elevated levels of ALP in the blood are indicative of liver or bone diseases, making it a valuable diagnostic marker for conditions such as hepatitis, cirrhosis, and bone disorders.
Therapeutic Strategies: ALP has potential therapeutic applications in treating conditions like hypophosphatasia, a rare genetic disorder characterized by defective bone mineralization.
Development: ALP is crucial during development for proper bone and teeth formation.
Aging: Changes in ALP activity are associated with aging, with elevated levels often observed in elderly individuals due to bone turnover and liver function changes.
Disease: Abnormal ALP levels are linked to various diseases, including liver disease, bone disorders, and certain cancers, highlighting its importance in health and disease.
