| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 12.8 kDa, a single non-glycosylated polypeptide chain containing 116 amino acids. |
| AA Sequence: |
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN |
| Purity: |
> 98% by SDS-PAGE and HPLC analyses. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 μm filtered concentrated solution in 20 mM Tris-HCl, pH8.0, 150 mM NaCl. |
| Endotoxin: |
Less than 0.1 EU/μg of rHuPCT/Procalcitonin as determined by LAL method. |
| Background: |
Procalcitonin (PCT) belongs to a group of related proteins including calcitonin gene-related peptides I and II, amylin, adrenomodulin, and calcitonin (CAPA peptide family). PCT originates from a common precursor, pre-procalcitonin, which comprises 141 amino acids and undergoes enzymatic removal of 25 amino acids from the N-terminus. This precursor is then cleaved sequentially to generate three peptides: a 55 amino acid N-terminal fragment, a 32 amino acid calcitonin, and a 21 amino acid katacalcin. PCT serves as a peptide precursor to the hormone calcitonin, playing a role in calcium homeostasis. It is primarily produced by the parafollicular cells (C cells) of the thyroid, as well as by neuroendocrine cells of the lung and intestine. Importantly, PCT levels are correlated with the severity of bacterial sepsis, establishing it as one of the earliest and most specific biomarkers for this condition. |
