Product Name	Cathelicidin/Camp
Chinese Name	抗菌肽CAMP抗体
Alias	CAMP_HUMAN; Cathelicidin antimicrobial peptide; 8 kDa cationic antimicrobial protein; CAP-18; CAP18; hCAP-18; Antibacterial peptide FALL-39; FALL39; HSD26; LL37; LL 37; CRAMP; FALL-39 peptide antibiotic; Antibacterial peptide LL-37; Antibacterial peptide KR-20; Antibacterial peptide LL-23; Antibacterial peptide LL-29; Antibacterial peptide KS-30; Antibacterial peptide RK-31; Antibacterial peptide FF-33;
Research Area	Cell biology  immunology  Microbiology  Bacteria and viruses
Immunogen Species	Rabbit
Clonality	Polyclonal
React Species	(predicted: Mouse, Rat, )
Applications	ELISA=1:5000-10000 IHC-P=1:100-500 IHC-F=1:100-500 ICC=1:100-500 IF=1:100-500 （Paraffin sections need antigen repair） not yet tested in other applications. optimal dilutions/concentrations should be determined by the end user.
Theoretical molecular weight	19kDa
Cellular localization	Secretory protein
Form	Liquid
Concentration	1mg/ml
immunogen	KLH conjugated synthetic peptide derived from mouse Camp: 101-170/170
Lsotype	IgG
Purification	affinity purified by Protein A
Buffer Solution	0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
Storage	Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.
Attention	This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
PubMed	PubMed
Product Detail	Cathelicidins are a family of antimicrobial proteins found in the peroxidase-negative granules of neutrophils. Along with the family of proteins known as defensins, cathelicidins participate in the first line of defense by preventing local infection and systemic invasion of microbes. FALL-39 precursor (FALL-39 peptide antibiotic, cationic anti-microbial protein, CAMP, CAP-18, HSD26) is a cathelicidin anti-microbial protein that contains the antibacterial peptide LL-37 (amino acids 134-170). In contrast to the defensins, which are cysteine-rich peptides that fold in ∫-pleated sheets, LL-37 is a cysteine-free peptide that can adopt an amphipathic å-helical conformation. LL-37 binds to bacterial lipopolysaccharides (LPS) and is a potent chemotactic factor for recruiting mast cells to sites of inflammation. LL-37 is present in inflammatory skin diseases that include psoriasis, sub-acute lupus erthematosus, dermatitis and nickel contact hypersensitivity. It is not found in normal skin epidermis. The secreted protein is expressed primarily in bone marrow, testis and neutrophils. The mouse and rat ortholog, CRAMP (cathelin-related antimicrobial peptide), is also part of the cathelicidin family of host defense peptides. These include precursors of potent antimicrobial peptides that direct antimicrobial activity against various microbial pathogens and also activate mesenchymal cells during wound repair. CRAMP is expressed in testis, spleen, stomach and intestine. 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. [provided by RefSeq, Sep 2021] Function: Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. Subcellular Location: Secreted. Tissue Specificity: Expressed in bone marrow and testis and neutrophils. Similarity: Belongs to the cathelicidin family. SWISS: P51437 Gene ID: 12796 Database links: Entrez Gene: 820 Human Entrez Gene: 12796 Mouse SwissProt: P51437 Mouse Unigene: 3834 Mouse

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