Recombinant Human Procalcitonin Protein, CF Summary
Details of Functionality |
Bioassay data are not available. |
Source |
E. coli-derived human Procalcitonin protein Pro27-Asn141, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Pro27 |
Protein/Peptide Type |
Innovator Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
14 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
14 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Procalcitonin Protein, CF
Background
Procalcitonin
(PCT) is encoded by a single CALCA gene, and can result in 2 alternatively
spliced products: calcitonin and calcitonin-gene related peptide (CGRP) (1). Mature
PCT is expressed as a 116 amino acid (aa) protein which is subsequently cleaved
into 3 parts: a 57 aa pro-region, a 32 aa Calcitonin peptide and a 21 aa Katacalcin
peptide (2, 3). PCT is moderately conserved among species, with human sharing
72% and 75% sequence identity with mouse and rat, respectively. In healthy adults,
PCT is expressed by thyroid C cells and promptly converted to calcitonin (3).
Calcitonin is directly involved in osteoclast activity and bone resorption (4). However, in states of inflammatory disease or
bacterial infection, PCT is over-expressed from multiple cell types and the
levels of unprocessed PCT rise significantly (3-5). These increased levels of
PCT in circulation have been used as a diagnostic marker of systemic bacterial
infection and sepsis and as a guide to antibiotic therapy (5, 6). More recently, the use of PCT as a disease
marker has been expanded to include acute heart failure and vasculitic
disorders (7, 8).
-
Russwurm, S. et al. (2005). Clin Chem and Lab Med, 37:789.
- Le Moullec, J.M. et al. (1984) FEBS Lett 167:93.
- Maruna P. et al. (2000) Physiol Res;49 Suppl 1:S57.
- Becker, KL et al. (2004). J Clin Endocrinol Metab 89:1512.
- Müller B. et al. (2001) Jan;86(1):396-404. J Clin Endocrinol Metab.
- Meisner, M. et al. (2014) Ann Lab Med. Jul; 34:263.
- Möckel, M. et al. (2017) ESC Heart Failure, 4:203.
- Lee NH, et al. (2017) Korean J of Peds 60:112.
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