Recombinant Human Cathelicidin Antimicrobial Peptide (CAMP) Protein (His-SUMO&Myc)

Name: Recombinant Human Cathelicidin Antimicrobial Peptide (CAMP) Protein (His-SUMO&Myc)
Brand: Beta LifeScience
SKU: BLC-03479P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Cathelicidin Antimicrobial Peptide (CAMP) Protein (His-SUMO&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49913
Target Symbol	CAMP
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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO&C-Myc
Target Protein Sequence	FALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
Expression Range	132-170aa
Protein Length	Full Length of Mature Protein
Mol. Weight	24.7kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity.
Subcellular Location	Secreted.
Protein Families	Cathelicidin family
Database References	HGNC: 1472 OMIM: 600474 KEGG: hsa:820 STRING: 9606.ENSP00000458149 UniGene: Hs.51120
Tissue Specificity	Expressed in bone marrow and testis and neutrophils.

Gene Functions References

The correlation between serum LL-37 and high-density lipoprotein cholesterol levels suggests that LL-37 may play a key role in regulation of cholesterol levels in hypercholesterolemia. PMID: 29644526
LL-37/CRAMP represents an important mediator of platelet activation and thrombo-inflammation. PMID: 29670076
Low vitamin D3 status and higher systemic levels of LL-37 may be a consequence of reduced TB control and enhanced pathological inflammation. PMID: 29867045
these data show that LL-37 affects surface and intracellular Toll-Like Receptor expression in tissue mast cells PMID: 29670923
This review describes novel advances involving the roles and mechanisms of human cathelicidin LL-37 in cancer. PMID: 29843147
this study shows that LL-37 serum level correlates with healing of venous leg ulcers PMID: 27663530
Elevated serum levels of LL-37 in bipolar patients may suggest the role of this peptide in the pathomechanism of BD. PMID: 29239826
LL-37 serum levels are not affected by body composition in elderly women with unipolar depression. PMID: 28959904
The findings support a role for STAT3 and HIF-1A in the regulation of LL-37 expression. PMID: 27633343
In silico docking study have confirmed the high binding affinities of multiple 9-mer peptides derived from LL-37 to the HLA-C*06:02 molecule proposed a mechanism of the interaction between this LL-37-HLA-C*06:02 complex and T cells via TCRs. PMID: 27189829
IL-33 down-regulates the induction of hCAP-18/LL-37 production in human gingival epithelial cells. PMID: 28637951
in teens with positive recto-vaginal group B streptococcus colonization, placental mRNA expression of cathelicidin is lower compared to those who tested negative for this infection PMID: 28622535
Serum levels of LL-37 were found to be higher in elderly patients with major depressive disorder compared to controls. PMID: 28550757
these results suggested that human CAMP/LL-37 might act as a tumor-suppressor in OSCC and DNA methylation might play roles during carcinogenesis via directly downregulating human CAMP promoter activity. PMID: 28427192
omoted epithelial and smooth-muscle-like differentiation of Adipose-derived stem cells through activating the Wnt/beta-catenin and NF-kappaB pathways, respectively PMID: 29223160
Patients with type 1 diabetes and presence of microangiopathy characterize higher level of serum cathelicidin. PMID: 28964758
The expression of LL-37 was up-regulated in the inflamed mucosa of IBD patients. LL-37 was induced by TLR-3 stimulation and exhibited an anti-microbial effect via interaction with lipopolysaccharide (LPS). PMID: 28872665
the mean level of LL-37 was statistically significantly higher in TB patients than that in patients with Gram-positive bacteria-induced pneumonia (p < 0.001), in patients with Gram-negative bacteria-induced pneumonia (p < 0.001), and in healthy controls (p < 0.001). PMID: 28956425
data suggest that cathelicidin LL-37 is an important element of host defense in the course of bacterial diseases within the respiratory tract, particularly when the infection is caused by an intracellular pathogen. PMID: 28218580
This review summarizes the current knowledge on molecular mechanisms underlying LL-37-induced receptor activation. PMID: 27609777
L-CATH-2, D-CATH-2 and LL-37 can modulate the immune response of primary chicken immune cells by increasing mannose receptor expression, antigen presentation, endocytosis and neutralizing LPS-induced cytokine production and as a result augment activation of the adaptive immune system. PMID: 28715682
study demonstrated a substantial loss of antimicrobial function when the peptide was exposed to low concentrations of nanomaterials, and further showed that the nanomaterial-peptide interaction resulted in a significant change in the structure of the peptide PMID: 28814602
cathelicidin selectively modulated synthesis of TLR4 and 9 in intestinal epithelium, but only when cells were exposed to virulence factors, mostly from apical surfaces. PMID: 28988039
Autologous endothelial progenitor cells transfected by lentiviral vectors expressing antibiotic peptide LL37, as well as urothelial and smooth muscle cells from New Zealand white male rabbits, were cultured and seeded onto preconfigured acellular collagen-based tubular matrices PMID: 28739721
this study shows that LL-37 may aid clearance of influenza A virus by promoting monocyte uptake of the virus, while reducing viral replication and virus-induced TNF-a responses in these cells PMID: 27856789
Male placental cotyledons showed reduced basal CYP27B1 and cathelicidin gene expression compared to females. PMID: 27210415
Study demonstrates high levels of serum hBD2 and LL-37 levels in paediatric post- infectious bronchiolitis obliterans patients. These antimicrobial peptides may have important roles in immune systems and the pathogenesis of these patients. PMID: 26073571
the expression of CAMP, vitamin D receptor (VDR), and the retinoid X receptor (RXR) isoforms in human skin and gingival tissue biopsies and investigated the signaling pathways involved in 1alpha,25-dihydroxyvitamin D3-induced upregulation of CAMP. PMID: 27357804
A positive correlation was found between vitamin D and urine cathelicidin levels in the vitamin D sufficient group, however, there was no correlation between vitamin D and urine cathelicidin levels in the vitamin D insufficient group. PMID: 27180947
LL37 induced YB1 expression, and increased tumor cell proliferation, migration and invasion of A375 and A875 malignant melanoma cell lines. PMID: 27922666
this study shows that serum cathelicidin levels of acute asthma group are higher than controlled asthma group, and can be used to predict viral-induced acute asthma PMID: 27955890
Our results suggest that calcitriol anti-cancer therapy is more likely to induce higher levels of CAMP in ERalpha- breast cancer cells, when compared to ERa + breast cancer cells. PMID: 27832772
These findings highlight the role of cathelicidin in the pathogenesis of allergic rhinitis. PMID: 26777417
expressions of LL-37 mRNA and protein in the lesions of cutaneous tuberculosis and tuberculids were similar to that of normal skin PMID: 26960373
this study shows that carbamylation has profound and diverse effects on the structure and biological properties of LL-37. In some cases, anti-inflammatory LL-37 was rapidly converted to pro-inflammatory LL-37 PMID: 26878866
In rhinovirus infected cystic fibrosis patients, LL37 was inversely correlated with viral load in bronchoalveolar lavage fluid. PMID: 26585423
we discuss 1,25D3-induced down-regulation of cytokine/chemokine production and stimulation of hCAP-18/LL-37 gene expression which represent two very important pathways for 1,25D3-evoked regulation of the innate immune response--{REVIEW} PMID: 26433491
this study provides evidence for the ability of LL37 to bind and internalize viral or endogenous DNA into non-immune cells. PMID: 26297208
The human cathelicidin LL-37--A pore-forming antibacterial peptide and host-cell modulator. PMID: 26556394
higher nasal levels are associated with protection against RSV infection, directly damages viral envelopes and disrupts viral particles PMID: 26873992
Data indicate that endoplasmic reticulum (ER) stress increase sphingosine-1-phosphate (S1P) production, in turn activating nuclear factor kappa B (NF-kappaB)-mediated cathelicidin antimicrobial peptide (CAMP) synthesis. PMID: 26903652
The authors show that the group A Streptococcus surface-associated M1 protein sequesters and neutralizes LL-37 antimicrobial activity through its N-terminal domain. PMID: 26468750
Cathelicidin appears to play different roles in the development of pulmonary sarcoidosis and tuberculosis. PMID: 26422567
Neonates with congenital pneumonia had significantly higher serum cathelicidin and lower serum 25(OH)D compared to controls. PMID: 25354286
Taken together, these observations suggest that activation of human mast cells by LL-37 could be modified by TLR2 ligands and the function of human mast cells could be switched from allergic reactions to innate immune response. PMID: 26778002
the use of hCAP-18 levels in blood plasma for differential diagnosis of neutropenic patients, was assessed. PMID: 26119962
LL37, HMGB1 and S100A9 are increased in serum during exacerbation in COPD patients PMID: 25931489
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
LL-37 interacts with negatively charged membranes forming a stable aggregate, which may produce toroidal pores. There is also an aggregate with a higher oligomeric degree for interaction of LL-37 with neutral membranes. PMID: 26502164
Chlamydial plasmid-encoded virulence factor Pgp3 neutralizes the antichlamydial activity of human cathelicidin LL-37. PMID: 26416907

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.