Recombinant Mouse Cathelicidin antimicrobial peptide (Camp)

Code CSB-YP004476MO
MSDS
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Source Yeast
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Code CSB-EP004476MO
MSDS
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Source E.coli
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Code CSB-EP004476MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP004476MO
MSDS
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Source Baculovirus
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Code CSB-MP004476MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Camp
Uniprot No.
Alternative Names
Camp; Cnlp; CrampCathelicidin antimicrobial peptide; Cathelin-like protein; CLP) [Cleaved into: Cathelin-related antimicrobial peptide; Cramp)]
Species
Mus musculus (Mouse)
Expression Region
135-172
Target Protein Sequence
ISRLAGLLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Acts as a potent antimicrobial peptide.
Gene References into Functions
  1. Mice treated with BMMNCs pre-incubated with CRAMP had smaller scars, enhanced cardiac recovery and less adverse remodeling. Histologically, this group had higher capillary density. Similarly, sustained CRAMP release from hydrogels enhanced the therapeutic effect of SDF-1, leading to enhanced functional recovery PMID: 29948752
  2. LL-37/CRAMP represents an important mediator of platelet activation and thrombo-inflammation. PMID: 29670076
  3. CRAMP deficiency impairs phagocytosis in cultured microglia cells after exposure to N. meningitides. PMID: 28915816
  4. Immunoblotting, qPCR, ChIP and siRNA-mediated gene knockdown studies revealed that the activation of phosphatidylinositol 3-kinase/protein kinase C zeta pathways in poly(I:C)-stimulated cells underlies Sp1 phosphorylation and recruitment to the mCRAMP promoter, leading to enhanced transcription PMID: 28343946
  5. The effect on insulin resistance found in Cramp-/- mice is solely due to leukocyte infiltration and not due to inflammatory phenotype of macrophages. Therefore we conclude that cathelicidin causes insulin resistance by the recruitment of myeloid cells into the adipose tissue. PMID: 26939624
  6. Cathelicidin is required for innate resistance to M. tuberculosis in a relevant animal model and is a key mediator in regulation of the levels of pro-inflammatory cytokines by calcium and cyclic nucleotides. PMID: 28097645
  7. Histological examination confirmed that CRAMP deficiency worsened the pancreatic inflammatory condition. These results indicate that CRAMP may be considered a novel modulatory mediator in mouse experimental AP. PMID: 27035328
  8. promotes olfactory epithelium inflammation PMID: 26346056
  9. overexpressed CRAMP in prostate tumor initially chemoattracts early myeloid progenitors to tumor microenvironment and mediates differentiation and polarization of early myeloid progenitors into protumorigenic M2 macrophages during PCa progression PMID: 26856684
  10. critical role in prevention of RSV-mediated disease postinfection exogenously applied LL-37 is protective against RSV-mediated disease in vivo. PMID: 26873992
  11. The aim of this project was to examine the functional impact of the human cathelicidin LL-37 and the mouse cathelicidin-related AMP (CRAMP) on the pathogenesis of lupus and arthritis. PMID: 25535966
  12. pancreatic beta-cells' production is controlled by short-chain fatty acids produced by the gut microbiota, and is defective in non-obese diabetic (NOD) mice PMID: 26253786
  13. Data indicate the role of cathelicidin-related antimicrobial peptide (CRAMP) as part of the innate immune defense against pathogens in bacterial CNS infections. PMID: 23969854
  14. Hypoxia-inducible factor-1alpha (HIF-1alpha), a transcription factor important for activating innate immune effectors, and the antimicrobial peptide LL-37 (CRAMP in mice) are key determinants of C. albicans colonization resistance. PMID: 26053625
  15. Specific structural motifs in syndecan-1 HS promote Staphylococcus aureus corneal infection by inhibiting neutrophil CRAMP. PMID: 25931123
  16. these findings show that the production of an antimicrobial peptide Camp by adipocytes is an important element for protection against S. aureus infection of the skin PMID: 25554785
  17. Cathelicidin-deficient (Cnlp(-/-)) mice produce much less LTB4 and TXB2 in vivo in response to TNF-alpha compared with control mice. PMID: 24736410
  18. observations indicate a nonredundant role for Fpr2 and its agonist CRAMP in DC maturation in immune responses. PMID: 24808174
  19. Expression of the antimicrobial peptide cathelicidin in the context of inflammation and in non-tumorous cells is an important factor for lung tumor growth. PMID: 23812430
  20. Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced sepsis. PMID: 24771854
  21. visfatin enhances CAMP, hBD-2, hBD-3, and S100A7 production in human keratinocytes and their orthologs in murine imiquimod-treated psoriatic skin. PMID: 23499548
  22. These data demonstrated that Salmonella Typhimurium PhoQ can sense cationic antimicrobial peptides and CRAMP serves as a putative direct PhoPQ activation signal in the mouse intestine. PMID: 22919691
  23. suppresses osteoclastogenesis induced by LPS and flagellin PMID: 23826736
  24. Collectively, these findings indicate that cathelicidin protects against H. pylori infection and its associated gastritis in vivo. Our study also demonstrates the feasibility of using the transformed food-grade bacteria to deliver cathelicidin. PMID: 23254369
  25. this investigation revealed an indispensable role for BD3, BD4, and CRAMP in defense against F. solani-induced keratitis PMID: 23670560
  26. Neutrophil-derived cathelicidin promotes adhesion of classical monocytes. PMID: 23283724
  27. TLR9 can induce the expression of antimicrobial peptides such as CRAMP in response to bacterial DNA motifs in primary glial cells. PMID: 23141747
  28. LL-37 activates caspase-1 in murine macrophages, resulting in release of active IL-1beta & IL-18. LL-37 activation of the NLRP3 inflammasome utilizes P2X7 receptor-mediated potassium efflux. PMID: 23267025
  29. CRAMP may exert important immunomodulatory effects that regulate lung injury and Gram-negative bacterial dissemination. PMID: 22634613
  30. CRAMP promotes atherosclerosis by enhancement of the recruitment of inflammatory monocytes. PMID: 22394519
  31. The role of the Src family kinase Lyn in the immunomodulatory activities of cathelicidin peptide LL-37 on monocytic cells PMID: 22246800
  32. Cathelicidin signaling via the Toll-like receptor (TLR9) protects against colitis in mice. PMID: 21762664
  33. results suggest that mCRAMP differentially regulates B- and T-cell function and implicate mCRAMP in the regulation of adaptive immune responses. PMID: 21773974
  34. ER stress increases CAMP expression via NF-kappaB-C/EBPalpha activation, independent of VDR, illuminating a novel VDR-independent role for ER stress in stimulating innate immunity. PMID: 21832078
  35. The presence of pronounced host inflammatory infiltration in lesions and lymph nodes of Leishmania-infected animals was CAMP-dependent. PMID: 21501359
  36. LL-37 induces apoptosis in CTLs via multiple different mechanisms, initiated by the LL-37-induced leakage of granzymes from cytolytic granules PMID: 21134367
  37. Data show that cathelicidin is highly produced during experimental pulmonary tuberculosis from diverse cellular sources and could have significant participation in its pathogenesis. PMID: 20636399
  38. Data show flagellin-induced protection was partially abrogated in cathelicidin-related antimicrobial peptide-deficient mice. PMID: 20566829
  39. CRAMP, the unique antimicrobial peptide derived from cathelin in mouse inhibited all the responses coupled to P2X(7) receptors in macrophages from wild type mice. PMID: 19913495
  40. an important native component of innate host defence in mice and provide protection against necrotic skin infection caused by Group A Streptococcus (GAS). PMID: 11719807
  41. solution structure in TFE/H2O solution determined by CD and NMR spectroscopy PMID: 12081622
  42. Cathelicidins are localized in the cytoplasmic granules of murine bone marrow-derived mast cells and directly participate in the mast cell immune response. PMID: 12594247
  43. cathelicidin expression (CRAMP) in the skin is 10- to 100-fold greater in the perinatal period than adult PMID: 12612195
  44. Intracellular reactive oxygen intermediates and proteases regulate macrophage CRAMP expression and activity to impair the replication of an intracellular bacterial pathogen. PMID: 14983025
  45. cathelicidin antimicrobial peptides are expressed in murine mammary glands PMID: 15531744
  46. Mig-14 and VirK inhibit binding of CRAMP to Salmonella typhimurium and thus promote bacterial resistance to CRAMP PMID: 15661016
  47. important component of innate antimicrobial defense in the colon PMID: 15814717
  48. CRAMP functions as both a chemoattractant for phagocytic leukocytes and an enhancer of adaptive immune response. PMID: 15879124
  49. role of cathelicidin in host susceptibility to HSV infection PMID: 16630942
  50. Data describe the production and function of the cathelicidin antimicrobial peptides LL-37, its precursor hCAP-18 and its ortholog CRAMP in epithelial cells of human and mouse urinary tract, respectively. PMID: 16751768

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Subcellular Location
Secreted.
Protein Families
Cathelicidin family
Tissue Specificity
Expressed in testis, spleen, stomach, and intestine. Very low expression found in heart, lung and skeletal muscle. No expression in brain, kidney or liver.
Database Links
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