Spantide I TFA

Spantide I TFA, a selective NK1 receptor antagonist and a substance P analog, exhibits K(i) values of 230 nM for NK1 and 8150 nM for NK2 receptors, respectively. It offers a method to decrease type 1 while increasing type 2 cytokine IL-10 in the infected cornea, significantly reducing corneal perforation [1] [2] [3].

[D-Pro2] Spantide I TFA is an analog of Spantide I, a selective antagonist of the NK1 receptor [1].

Stressin I (Cyclo(31-34)[DPhe12, Nle21, 38, Glu31, Lys34]Ac-hCRF(4-41)) TFA, with a K i of 1.7 nM, is a potent and selective agonist of the CRF1 receptor. It has been shown to elevate adrenocorticotropic hormone (ACTH) levels in rats [1].

IGF-I (30-41) (TFA) is amino acids 30 to 41 fragment of Insulin-like Growth Factor I (IGF-I).

Parasin I (TFA) is a 19-amino acid histone H2A-derived peptide isolated from the skin of the catfish, and shows antimicrobial activity[1].

Insulin-like Growth Factor I (24-41) TFA, a fragment comprising amino acids 24 to 41 of the full IGF-I TFA molecule, is a variant of IGF-I TFA, which itself is a 70 amino acid polypeptide hormone. This hormone serves as a trophic factor beneficial for both neurons and glial cells, playing a significant role in mediating the effects of growth hormone (GH) on systemic growth. Additionally, IGF-I TFA exhibits anabolic, antioxidant, anti-inflammatory, and cytoprotective properties. The specific fragment IGF-I (24-41) TFA is involved in regulating somatic growth as well as behavioral development [1] [2] [3].

Parasin I, a peptide fragment derived from the N-terminal region of histone H2A in catfish (P. asotus), plays a critical role in host defense. This antimicrobial peptide is produced through the action of cathepsin D on histone H2A within the skin mucosa of injured P. asotus. Demonstrating efficacy against a spectrum of Gram-positive and Gram-negative bacteria, as well as fungi, Parasin I exhibits minimum inhibitory concentrations (MICs) of 1-2 µg/ml, 1-4 µg/ml, and 1-2 µg/ml, respectively.

Mini Gastrin I, human (TFA) is a truncated form of the human gastrin peptide, encompassing amino acids 5-17 of the original sequence.

IGF-I is partly responsible for systemic GH activities although it possesses a wide number of own properties (anabolic, antioxidant, anti-inflammatory and cytoprotective actions).IGF-I (24-41) (TFA) is amino acids 24 to 41 fragment of Insulin-like Growth

Spantide antagonizes both bombesin & substance P. It is also tachykinin receptor antagonist.

Gastrin I (1-14), human TFA is 1-14 fragment of human gastrin I peptide.

IGF-I (30-41) (TFA) is a fragment consisting of amino acids 30 to 41 from Insulin-like Growth Factor I (IGF-I), a compound responsible in part for systemic GH (Growth Hormone) activities. It exhibits an array of properties including anabolic, antioxidant, anti-inflammatory, and cytoprotective actions [1].

Urotensin I (Catostomus urotensin I) TFA is a CRF-like neuropeptide that functions as an agonist for CRF receptors, demonstrating efficacy through pEC50 values of 11.46 for human CRF1, 9.36 for human CRF2, and 9.85 for rat CRF2α receptors in CHO cells. It also exhibits binding affinities (Ki) of 0.4 nM for hCRF1, 1.8 nM for rCRF2α, and 5.7 nM for mCRF2β receptors, respectively [1] [2].

Angiotensin I/II (1-6) TFA is a chemical compound comprising amino acids 1-6. It is derived from the Angiotensin I/II peptide, which is formed by the cleavage of the precursor angiotensinogen by renin. The resulting Angiotensin I is then hydrolyzed by angiotensin-converting enzyme (ACE) to produce biologically active Angiotensin II. Angiotensin II has been extensively studied for its potential applications in the treatment of Hypertension, Renin Angiotensin System, and Idiopathic Membranous Nephropathy[1][2][3].

Mini Gastrin I, human (TFA) is short for human Gastrin. It is a mother peptide composed of 5-17 amino acids.