Human ALPL Protein, His Tag, low endotoxin (active enzyme, MALS verified)

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ALL-H52H3-100ug
$390.00
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ALL-H52H3-1mg
$2,680.00
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ALL-H52H3
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Synonyms

AP-TNAP, APTNAP, HOPS, HPPA, HPPC, HPPI, HPPO, TNALP, TNAP, TNS-ALP, TNSALP

Source

Human ALPL Protein, His Tag (ALL-H52H3) is expressed from human 293 cells (HEK293). It contains AA Leu 18 - Ser 502 (Accession # P05186-1).

Predicted N-terminus: Leu 18

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 55.3 kDa. The protein migrates as 65-70 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

The protein is designed as a dimer.

Endotoxin

Less than 0.01 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

Formulation

Supplied as 0.2 μm filtered solution in 20 mM Tris, 150 mM NaCl, Glycerol, pH7.5 with trehalose as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.

Background

This gene encodes a member of the alkaline phosphatase family of proteins. There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate the mature enzyme. This enzyme may play a role in bone mineralization. Mutations in this gene have been linked to hypophosphatasia, a disorder that is characterized by hypercalcemia and skeletal defects.