| CRAMP

Cathelicidin antimicrobial peptide(CRAMP) is a member of an antimicrobial peptide family, characterized by a highly conserved N-terminal signal peptide containing a cathelin domain and a structurally variable cationic antimicrobial peptide, which is produced by extracellular proteolysis from the C-terminus. The protein plays an important role in innate immunity defense against viruses. In addition to its antibacterial, antifungal, and antiviral activities, the protein functions in cell chemotaxis, immune mediator induction, and inflammatory response regulation.

| Repeatability

Intra-assay Precision (Precision within an assay)：CV% < 10%; Inter-assay Precision (Precision between assays)：CV% < 10%
 

| Recovery

The recovery of Mouse CRAMP spiked at three different levels in samples throughout the range of the assay was evaluated in various matrices.

 

Sample Type	Range(%)	Average Recovery(%)
Serum(n=8)	84-101	95
Plasma(n=8)	92-106	103
Cell Culture Supernates(n=8)	96-109	105

 

| Linearity

Samples were spiked with high concentrations of Mouse CRAMP and diluted with Universal Diluent to produce samples with values within the range of the assay.

 

		Serum(n=4)	Plasma(n=4)	Cell Culture Supernates(n=4)
1 : 2	Range (%)	84-95	88-96	90-110
	Average (%)	91	93	96
1 : 4	Range (%)	89-103	87-108	105-114
	Average (%)	94	98	107