Technical Data
ALPP (Alkaline Phosphatase, Placental Type, Alkaline Phosphatase Regan Isozyme, Placental Alkaline Phosphatase 1, PLAP-1, PLAP)
Alkaline phosphatases are dimeric metalloenzymes which catalyses the hydrolysis of phosphomonoesters with release of inorganic phosphate and alcohol. In humans, three (placental, PLAP; germ cell, GCAP; and intestinal, IAP) out of the four alkaline phosphatases isozymes are tissue-specific. These three are 90-98% homologous and their genes are clustered on chromosome 2 while the fourth isoenzyme is tissue non-specific and is located on chromosome 1. The placental isoenzyme (PLAP), the most stable of the isoenzymes has attracted much interest because it is structurally related to some of the tumor-associated alkaline phosphatases. The crystal structure of human PLAP revealed three additional domains compared to the bacterial enzyme which correspond to an interfacial crown domain, an N-terminal alpha-helix and a peripheral calcium-binding domain. The enzyme is heat labile and is enzymatically inefficient, with a lower catalytic constant (kcat 460 s-1). It plays a role in transfer of maternal IgG to the fetus. More recently, it was reported that PLAP stimulates DNA synthesis and cell proliferation in fibroblasts in concert with insulin, zinc and calcium ions.

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

AA Sequence:

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ug-20CBlue IceHumanRabbit
As reported
Full length human ALPP, aa1-535 (NP_001623.3).
Purified by Protein A affinity chromatography.
Supplied as a liquid in PBS, pH 7.2.
Recognizes human ALPP.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.