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Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY)

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Published Data
CBMAB-X0146-FY-1
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in IF
Detection of increased CRAMP in macrophages infected by E. coli O22H8 (MOI=10) for 4 h. Red, CRAMP; blue, DAPI. Scale bars: 30 µm. Right panel: quantitation of CRAMP-positive staining spots per macrophage (Mφ). The immunofluorescence intensity per macrophage is shown, n=20-22 macrophages per group. ***P<0.001 (paired, two-tailed Student's t-test). ...View More
Chen, K., Yoshimura, T., Gong, W., Tian, C., Huang, J., Trinchieri, G., & Wang, J. M. (2021). Requirement of CRAMP for mouse macrophages to eliminate phagocytosed E. coli through an autophagy pathway. Journal of Cell Science, 134(5), jcs252148.
CBMAB-X0146-FY-2
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in WB
Upregulation of CRAMP in macrophages stimulated with inactivated E. coli O22H8. Macrophages from BM of myeloid CRAMP+/+ control mice were stimulated with inactivated E. coli O22H8 (MOI=10) at 37°C then were lysed at the indicated time points. The cell lysates were measured for CRAMP by western blotting. β-actin is shown as a loading control. ...View More
Chen, K., Yoshimura, T., Gong, W., Tian, C., Huang, J., Trinchieri, G., & Wang, J. M. (2021). Requirement of CRAMP for mouse macrophages to eliminate phagocytosed E. coli through an autophagy pathway. Journal of Cell Science, 134(5), jcs252148.
CBMAB-X0146-FY-3
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in IHC
Immunohistochemical staining results showed CAMP expression in both the WT and VDR-KD mouse models in all groups mentioned above. CAMP expression increased after H. pylori infection, and VitD3 treatment promoted this expression in a dose-dependent manner. #p < 0.05, ###p < 0.001, **p < 0.01, ***p < 0.001. All values are presented as the means ± SEM from 5 independent experiments unless otherwise stated. Scale bar= 50 μm. ...View More
Zhou, A., Li, L., Zhao, G., Min, L., Liu, S., Zhu, S., ... & Li, P. (2020). Vitamin D3 inhibits Helicobacter pylori infection by activating the VitD3/VDR-CAMP pathway in mice. Frontiers in Cellular and Infection Microbiology, 10, 566730.
CBMAB-X0146-FY-4
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in WB
Western blot analyses were performed to assess CAMP expression in WT and VDR-KD mice in all groups, including the control, H. pylori infection alone and H. pylori infection plus VitD3 treatment groups. ...View More
Zhou, A., Li, L., Zhao, G., Min, L., Liu, S., Zhu, S., ... & Li, P. (2020). Vitamin D3 inhibits Helicobacter pylori infection by activating the VitD3/VDR-CAMP pathway in mice. Frontiers in Cellular and Infection Microbiology, 10, 566730.
CBMAB-X0146-FY-5
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in IHC and IF
Contribution of epithelial cell-derived CRAMP to Muc2 production in the colon. (A) Reduced Muc2 expression in the colon mucosa of epithelial Cnlp−/− mice. Left panel: representative images are shown. Green: Muc2; blue: DAPI. White arrow: Muc2+ materials released onto the surface of colonic mucosa. Scale bar = 50 μm. Right panel: measurement of Muc2 thickness on the surface of colon mucosa. n = 13 per group; ***p < 0.001. (B) Muc2 expression in the colonic mucosa of myeloid Cnlp−/− mice. Left panel: representative images are shown. Green: Muc2; blue: DAPI. White arrow: Muc2+ materials released onto the surface of the mucosa. Scale bar = 50 μm. Right panel: measurement of Muc2+ thickness on the surface of colonic mucosa, n = 20 per group. (C) Reduced PAS+ cells in the colon crypts of epithelial Cnlp−/− mice. Left panels: representative images are shown. Red arrow: PAS+ cells. Scale bar = 100 μm. Right panel: PAS+ cell number per colonic crypt. n = 21-30 per group; ***p < 0.001. (D) No change of PAS+ cell number in the colonic crypts of myeloid Cnlp−/− mice. Left panels: representative images are shown. Red arrow: PAS+ cells. Scale bar = 100 μm. Right panel: PAS+ cells per colon crypt. n = 15-21 per group. ...View More
Chen, K., Yoshimura, T., Yao, X., Gong, W., Huang, J., Dzutsev, A. K., ... & Wang, J. M. (2021). Distinct contributions of cathelin-related antimicrobial peptide (CRAMP) derived from epithelial cells and macrophages to colon mucosal homeostasis. The Journal of Pathology, 253(3), 339-350.
CBMAB-X0146-FY-6
Mouse Anti-CAMP Recombinant Antibody (CBFYA-0099) (CBMAB-X0146-FY) in IF
Neutrophil extracellular killing of S. aureus is mediated by CRAMP, and syndecan-1 ectodomain and 2-O-sulfated heparan compounds inhibit killing of S. aureus by CRAMP. ...View More
Hayashida, A., Amano, S., Gallo, R. L., Linhardt, R. J., Liu, J., & Park, P. W. (2015). 2-O-sulfated domains in syndecan-1 heparan sulfate inhibit neutrophil cathelicidin and promote Staphylococcus aureus corneal infection. Journal of Biological Chemistry, 290(26), 16157-16167.
Datasheet
SDS
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal
Mouse
Clone
CBFYA-0099
Application
WB, IP, IF, ELISA
Immunogen
Amino acids 6-175 mapping at the C-terminus of CAP-18 of rat origin.
Host Species
Mouse
Specificity
Mouse, Rat
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
ELISA1:100-1:1,000
IF(ICC)1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% BSA
Concentration
0.1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
More Infomation

Target

Full Name
Cathelicidin Antimicrobial Peptide
Introduction
CAMP (Cathelicidin Antimicrobial Peptide) is a Protein Coding gene. Diseases associated with CAMP include Rosacea and Mycobacterium Marinum. Among its related pathways are Innate Immune System and Defensins.
Entrez Gene ID
820
UniProt ID
P49913
Alternative Names
Cathelicidin Antimicrobial Peptide; 18 KDa Cationic Antimicrobial Protein; CAP-18; FALL39; CAP18; FALL-39
Function
Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.
Biological Process
Antibacterial humoral response Source: UniProtKB
Antifungal humoral response Source: UniProtKB
Antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
Antimicrobial humoral response Source: Reactome
Chronic inflammatory response Source: UniProtKB
Cytolysis by host of symbiont cells Source: UniProtKB
Defense response to bacterium Source: MGI
Defense response to Gram-negative bacterium Source: UniProtKB
Defense response to Gram-positive bacterium Source: UniProtKB
Innate immune response Source: UniProtKB
Innate immune response in mucosa Source: UniProtKB
Killing by host of symbiont cells Source: CACAO
Modulation of process of other organism Source: UniProtKB
Neutrophil degranulation Source: Reactome
Positive regulation of interleukin-8 production Source: UniProtKB
Response to yeast Source: UniProtKB
Cellular Location
Secreted
PTM
The N-terminus is blocked.

Hochberg, A., Patz, M., Karrasch, T., Schäffler, A., & Schmid, A. (2021). Serum levels and adipose tissue gene expression of cathelicidin antimicrobial peptide (CAMP) in obesity and during weight loss. Hormone and Metabolic Research, 53(03), 169-177.

Karrasch, T., Höpfinger, A., Schäffler, A., & Schmid, A. (2021). The adipokine C1q/TNF-related protein-3 (CTRP-3) inhibits Toll-like receptor (TLR)-induced expression of Cathelicidin antimicrobial peptide (CAMP) in adipocytes. Cytokine, 148, 155663.

Wang, G., Li, Y., Yang, G., Yang, T., He, L., & Wang, Y. (2021). Cathelicidin antimicrobial peptide (CAMP) gene promoter methylation induces chondrocyte apoptosis. Human Genomics, 15(1), 1-10.

Lowry, M. B., Guo, C., Zhang, Y., Fantacone, M. L., Logan, I. E., Campbell, Y., ... & Gombart, A. F. (2020). A mouse model for vitamin D-induced human cathelicidin antimicrobial peptide gene expression. The Journal of steroid biochemistry and molecular biology, 198, 105552.

Chen, X., Ji, S., Si, J., Zhang, X., Wang, X., Guo, Y., & Zou, X. (2020). Human cathelicidin antimicrobial peptide suppresses proliferation, migration and invasion of oral carcinoma HSC-3 cells via a novel mechanism involving caspase-3 mediated apoptosis. Molecular Medicine Reports, 22(6), 5243-5250.

Febriza, A., Hatta, M., Natzir, R., Kasim, V. N., & Idrus, H. H. (2019). Activity of antimicrobial peptide; cathelicidin, on bacterial infection. The Open Biochemistry Journal, 13(1).

Li, Y., Østerhus, S., & Johnsen, I. B. (2018). Human metapneumovirus infection inhibits cathelicidin antimicrobial peptide expression in human macrophages. Frontiers in immunology, 9, 902.

Thomi, R., Schlapbach, C., Yawalkar, N., Simon, D., Yerly, D., & Hunger, R. E. (2018). Elevated levels of the antimicrobial peptide LL‐37 in hidradenitis suppurativa are associated with a Th1/Th17 immune response. Experimental dermatology, 27(2), 172-177.

Chen, X., Qi, G., Qin, M., Zou, Y., Zhong, K., Tang, Y., ... & Zou, X. (2017). DNA methylation directly downregulates human cathelicidin antimicrobial peptide gene (CAMP) promoter activity. Oncotarget, 8(17), 27943.

Barksdale, S. M., Hrifko, E. J., & van Hoek, M. L. (2017). Cathelicidin antimicrobial peptide from Alligator mississippiensis has antibacterial activity against multi-drug resistant Acinetobacter baumanii and Klebsiella pneumoniae. Developmental & Comparative Immunology, 70, 135-144.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme-Linked Immunospot (ELISpot)
Proteogenomics
Other Protocols

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For research use only. Not intended for any clinical use.

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