SILu^™Prot AMBP Alpha-1 Microglycoprotein human

AMBP is synthesized by the liver, with approximately half of the circulating protein complexed to IgA. The free form is readily filtered by the glomerulus and reabsorbed by proximal tubule cells. AMBP has been found to be a sensitive biomarker for proximal tubular dysfunction even in the early phase of injury when no histologic damage is observable. In addition, urinary AMBP has been proposed to be a useful marker of tubular dysfunction even in low-gestational-age preterm infants, a population at high risk for AKI (Acute Kidney Injury).

SILu^™ Prot AMBP is a recombinant, stable isotope-labeled human AMBP which incorporates ^[13C6, ¹⁵N4]-Arginine and [¹³C6, ¹⁵N2]-Lysine. Expressed in human 293 cells, it is designed to be used as an internal standard for bioanalysis of AMBP in mass-spectrometry. SILu^™ Prot AMBP is a monomer of 204 amino acids (including C-terminal polyhistidine and flag tags), with a molecular weight of ~23 kDa.

GPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVDYKDDDDKGHHHHHHHHGGQ

Supplied as a lyophilized powder containing phosphate buffered saline.

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