Research Grade Asfotase alfa

Description: Asfotase alfa (BS11493) is a research-grade recombinant antibody targeting Alkaline phosphatase liver/bone/kidney isozyme. Produced in mammalian cells with native-like glycosylation.
Highlights:
• Research Grade — For PK/PD studies, assay development, and ADA research.
• Native Glycosylation — Mammalian expression ensures native-like patterns.
Host species: Human
Isotype: Fusion-[ALPL(alkalinephosphatase,TNSALP,tissuenon-specificalkalinephosphatase)18-502]2-IGHG1Fc(Fragmentconstant)-Asp-Ile-deca-aspartate
Species reactivity: Human
Immunogen:
Form: Liquid
Storage instructions:
Storage buffer: 0.01M PBS, pH7.4.
Concentration: 0.5mg/ml
Purity: >95% as determined by SDS-PAGE.
Clonality:
Applications: Research Grade Biosimilar
Target: Alkalinephosphataseliver/bone/kidneyisozyme,AP-TNAP,TNSALP,Alkalinephosphatase,tissue-nonspecificisozyme,ALPL
Purification: Protein A/G purified from cell culture supernatant.
Endotoxin level: <1EU/mg, determined by LAL gel clotting assay
Expression system: Mammalian Cells
Stability and Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4°C short term (1-2 weeks). Store at -20°C 12 months. Store at -80°C long term.
Alternative Names: ENB-0040,STRENSIQâ„¢
Background: Alkaline phosphatase, tissue-nonspecific isozyme (ALPL) is a ~57 kDa protein. 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.
References:
1. Di Mauro, S. et al. (2002) Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research 17, 1383-91. PMID: 12162492
2. Sultana, S. et al. (2013) Molecular genetics and metabolism 109, 282-8. PMID: 23688511
3. Numa-Kinjoh, N. et al. (2015) Molecular genetics and metabolism 115, 180-5. PMID: 25982064
4. Fedde, KN. et al. (1990) American journal of human genetics 47, 767-75. PMID: 2220817
5. Balasubramaniam, S. et al. (2010) Journal of inherited metabolic disease 33 Suppl 3, S25-33. PMID: 20049532
6. Pettengill, M. et al. (2017) PloS one 12, e0175936. PMID: 28448526
Note: For research use only. Not suitable for clinical or therapeutic use.