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Amino acids 132-170 form the expressed segment for recombinant Human CAMP. The theoretical molecular weight of the CAMP protein is 24.7 kDa. The CAMP protein was expressed in e.coli. The N-terminal 10xHis-SUMO tag and C-terminal Myc tag was fused into the coding gene segment of CAMP, making it easier to detect and purify the CAMP recombinant protein in the later stages of expression and purification.Cathelicidin antimicrobial peptide (CAMP) is a protein primarily studied in the fields of immunology and infectious diseases. Its pivotal role lies in the innate immune system, where it acts as a natural antibiotic, defending against microbial invaders. Researchers focus extensively on CAMP's involvement in combating bacterial, viral, and fungal infections, making it a key player in understanding host defense mechanisms. The most significant and widely explored area is its impact on antimicrobial activity, unveiling insights into potential therapeutic strategies against infectious diseases. Additionally, studies touch upon CAMP's contribution to inflammatory responses and its implications in various dermatological conditions, shedding light on skin immunity. While CAMP's main spotlight is on infection defense, its diverse roles across different immune processes hint at broader applications in medicine and immunotherapy.
Amino acids 132-170 form the expressed segment for recombinant Human CAMP. The theoretical molecular weight of the CAMP protein is 24.7 kDa. The CAMP protein was expressed in e.coli. The N-terminal 10xHis-SUMO tag and C-terminal Myc tag was fused into the coding gene segment of CAMP, making it easier to detect and purify the CAMP recombinant protein in the later stages of expression and purification.Cathelicidin antimicrobial peptide (CAMP) is a protein primarily studied in the fields of immunology and infectious diseases. Its pivotal role lies in the innate immune system, where it acts as a natural antibiotic, defending against microbial invaders. Researchers focus extensively on CAMP’s involvement in combating bacterial, viral, and fungal infections, making it a key player in understanding host defense mechanisms. The most significant and widely explored area is its impact on antimicrobial activity, unveiling insights into potential therapeutic strategies against infectious diseases. Additionally, studies touch upon CAMP’s contribution to inflammatory responses and its implications in various dermatological conditions, shedding light on skin immunity. While CAMP’s main spotlight is on infection defense, its diverse roles across different immune processes hint at broader applications in medicine and immunotherapy.
| Cat.No | ACP02681 | Target Name | CAMP |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 132-170aa | Mol Weight | 24.7kDa |
| Protein Length | Full Length of Mature Protein | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P49913 |
|---|
Uniprot Id
P49913
Target Species
Human
Target Name
CAMP
Target Full Name
Cathelicidin antimicrobial peptide
Target Function
Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.
Target Subcellular Location
Secreted.
Target Protein Families
Cathelicidin family
Target Tissue Specificity
Expressed in bone marrow and testis and neutrophils.
Target Research Area
others
Target Synonyms
18 kDa cationic antimicrobial protein; Antibacterial peptide LL-37; Antibacterial protein FALL-39; CAMP; CAMP_HUMAN; CAP 18; CAP-18; CAP18; Cathelicidin antimicrobial peptide; Cathelin-like protein; Cathelin-related antimicrobial peptide; CATHL3; Cationic antimicrobial protein; 18-KD; CLP; Cnlp; Cramp; CRAMP; mouse; homolog of; FALL 39 ; FALL-39 peptide antibiotic; FALL39 ; hCAP 18; hCAP-18; hCAP18; HSD26 ; LL37; MCLP; Peptide antibiotic; PR-39; porcine; homolog of
Target Background
This gene encodes 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 encoded protein functions in cell chemotaxis, immune mediator induction, and inflammatory response regulation.
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