ll 37, human

LL-37, Human is a 37-residue, amphipathic, cathelicidin-derived antimicrobial peptide, which exhibits a broad spectrum of antimicrobial activity.

LL-37, Human acetate is a 37-residue, amphipathic, cathelicidin-derived antimicrobial peptide, which exhibits a broad spectrum of antimicrobial activity.

Human LL-37 is a 37 amino acid cationic (6+) peptide and has been widely studied. LL-37 penetrates the bacterial membrane and forms pores in the membrane.

LL-37, human acetate, is a 37-residue amphipathic peptide derived from cathelicidin, known for its broad-spectrum antimicrobial properties. This compound not only plays a crucial role in safeguarding the cornea against infection but also modulates wound healing [1] [2] [3].

LL-37 (18-37), an antimicrobial peptide fragment of LL-37, exhibits activity against S. aureus and C. albicans, with minimum lethal concentrations of 4 µM and 10 µM, respectively. Additionally, it inhibits E. histolytica trophozoites growth at concentrations between 10 to 50 µM.

Citrullinated LL-37 1cit, a modified LL-37 peptide, retains the antiviral properties of its parent compound against human rhinovirus and exhibits antibacterial activity against S. aureus. Furthermore, it diminishes the RV1B-induced expression of pro-inflammatory cytokines, including IL-8, CCL5, and IL-6 mRNA [1].

Citrullinated LL-37 2cit, a modified version of the LL-37 peptide, attenuates the antiviral efficacy of LL-37 against Human Rhinovirus (HRV) at a concentration of 10 μg/mL and diminishes its antibacterial properties. Furthermore, the compound diminishes RV1B-induced mRNA expression of pro-inflammatory cytokines IL-8, CCL5, and IL-6, and demonstrates a moderate decline in suppressing HRV-stimulated CCL5 secretion [1].

Citrullinated LL-37 3cit is a host defense peptide with notable immunomodulatory and antimicrobial properties, which exhibits direct antiviral activity against human rhinoviruses (HRV) [1].

LL-37(17-32) is a biologically active peptide fragment derived from the C-terminal domain of human cathelicidin antimicrobial peptide. This segment reverses ABCG2-mediated multidrug resistance in cancer cell lines, highlighting its potential therapeutic role against drug resistance.

Amylin (8-37), human, derived from human Amylin, possesses direct vasodilator effects in isolated mesenteric resistance arteries of rats. Human Amylin is a small pancreatic β-cell hormone that forms aggregates in the absence of insulin and is a key pathological feature of type II diabetes mellitus.

Glucagon-like peptide 1 (1-37), human, is a highly potent agonist of the GLP-1 receptor and a pancreatic hormone synthesized by post-translational processing of proglucagon. Unlike truncated forms of GLP-1, it neither affects food intake in rats nor enhances pancreatic insulin secretion.

Glucagon-like peptide 1 (1-37), human (TFA), is a highly potent agonist of the GLP-1 receptor and is a pancreatic hormone synthesized through post-translational processing of proglucagon.

Amylin (1-37) (human) (hIAPP (1-37)), a peptide hormone located in pancreatic beta-cell secretory granules, is characterized by an amidated C-terminus and a disulfide bond between cysteine residues 2 and 7 [1].

LL-37 GKE, an active domain of LL-37, exhibits antibacterial activity and possesses potential for antibiotic applications [1] [2].

Glucagon-like peptide 1 (1-37), human acetate is a highly potent the GLP-1 receptor agonist.

This LL-37 peptide is acetylated on the N-terminus and amidated on the C-terminus.It plays a key role in the first line of defense against local infection and systemic invasion of pathogens at sites of inflammation and wounds.

Citrullinated LL-37 3cit, a modified form of the LL-37 peptide, exhibits no antiviral activity at a concentration of 10 μg/mL while maintaining partial efficacy against HRV at 30 μg/mL. Furthermore, this citrullinated variant demonstrates diminished immunomodulatory properties compared to the native LL-37 and a moderate reduction in its capacity to decrease HRV-induced CCL5 secretion [1].

PTH-Related Protein (1-37) (human, mouse, rat) is a peptide analog of parathyroid-hormone-related protein (pTHrP), which plays a role in the physiological regulation of bone formation [1].

LL-37 amide, a positively charged antimicrobial peptide, exhibits anticancer activity, making it valuable for cancer research [1] [2].

pTH (1-37) (human), a fragment of parathyroid hormone (PTH), promotes cAMP formation and enhances alkaline phosphatase activity. Additionally, it fosters growth, elevates bone calcium content, and augments bone mineral density (BMD) in uremic animals. This compound shows promise for osteoporosis research [1] [2] [3].

Lactoferricin H, Lactotransferrin (37-61), human, is a bioactive peptide with antimicrobial properties, derived from amino acid residues 37-61 of human lactotransferrin.

LL-37 scrambled peptide acetate, a scrambled version of the cathepsin antimicrobial peptide LL-37, is commonly used as a negative control in experiments involving the LL-37 peptide.

β-Amyloid (1-37) (human) is potentially associated with mental status in Alzheimer's disease.

Pancreastatin (37-52), human, is a biologically active fragment of CgA-derived peptide (residues 250–301) that inhibits insulin release from islet beta cells [1][2].

LL-37 FKR, the C-terminal fragment of LL-37, plays a crucial role in antibacterial activity [1] [2].

Amylin (8-37) (human) (hIAPP (8-37)) is the 8-37 fragment of human islet amyloid polypeptide (IAPP) and exhibits a duplex folding with a hairpin structure [1].

Acetyl-Amylin (8-37) (human) is a specific amylin antagonist [1].

LL-37 scrambled peptide is a rearranged version of the cathelicidin anti-microbial peptide (LL-37).

β-Defensin-2 is a peptide with antimicrobial properties that protects the skin and mucosal membranes of the respiratory, genitourinary, and gastrointestinal tracts.1It inhibits the growth of periodontopathogenic and cariogenic bacteria, includingP. gingivalisandS. salivarius.2β-Defensin-2 (30 μg/ml) stimulates gene expression and production of IL-6, IL-10, CXCL10, CCL2, MIP-3α, and RANTES by keratinocytes.3It also stimulates calcium mobilization, migration, and proliferation of keratinocytes when used at concentrations of 30, 10, and 40 μg/ml, respectively. β-Defensin-2 induces IL-31 production by human peripheral blood-derived mast cellsin vitrowhen used at a concentration of 10 μg/ml and by rat mast cellsin vivofollowing a 500 ng intradermal dose.4Expression of β-defensin-2 is increased in psoriatic skin and chronic wounds.5,6 1.Lehrer, R.I.Primate defensinsNat. Rev. Microbiol.2(9)727-738(2004) 2.Ouhara, K., Komatsuzawa, H., Yamada, S., et al.Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, β-defensins and LL37, produced by human epithelial cellsJ. Antimicrob. Chemother.55(6)888-896(2005) 3.Niyonsaba, F., Ushio, H., Nakano, N., et al.Antimicrobial peptides human β-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokinesJ. Invest. Dermatol.127(3)594-604(2007) 4.Niyonsaba, F., Ushio, H., Hara, M., et al.Antimicrobial peptides human β-defensins and cathelicidin LL-37 induce the secretion of a pruritogenic cytokine IL-31 by human mast cellsJ. Immunol.184(7)3526-3534(2010) 5.Huh, W.-K., Oono, T., Shirafuji, Y., et al.Dynamic alteration of human β-defensin 2 localization from cytoplasm to intercellular space in psoriatic skinJ. Mol. Med. (Berl.)80(10)678-684(2002) 6.Butmarc, J., Yufit, T., Carson, P., et al.Human β-defensin-2 expression is increased in chronic woundsWound Repair Regen.12(4)439-443(2004)

CRAMP (140-173) (mouse), the ortholog of the human LL-37 antimicrobial peptide, inhibits LPS-induced responses and does not colocalize with TLR3 in BEAS-2B cells [1].

Lugdunin is an antibiotic peptide that disrupts membrane potential in bacteria, demonstrating activity against Gram-positive species including S. aureus, and effectively reducing skin and nasal colonization of this pathogen. Moreover, Lugdunin stimulates the production of LL-37 and CXCL8/MIP-2 in human keratinocytes and mouse skin [1].