Leptin (93-105), human

Product Name: Leptin (93-105), human

Sequence One Letter Code: NVIQISNDLENLR

Sequence Three Letter Code: H-Asn-Val-Ile-Gln-Ile-Ser-Asn-Asp-Leu-Glu-Asn-Leu-Arg-OH

Cas No: 200436-43-7

Chemical Formula:C64H110N20O23

Molecular Weight: 1527.8

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Endocrinology Disease Research

SMILES: CC[C@H](C)[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(=O)N)N

IUPAC: (4S)-4-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-5-amino-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2,4-diamino-4-oxobutanoyl]amino]-3-methylbutanoyl]amino]-3-methylpentanoyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-4-oxobutanoyl]amino]-3-carboxypropanoyl]amino]-4-methylpentanoyl]amino]-5-[[(2S)-4-amino-1-[[(2S)-1-[[(1S)-1-carboxy-4-(diaminomethylideneamino)butyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-5-oxopentanoic acid

INCHIKEY: OFDBWUQCFOBTMQ-BPVWZOJZSA-N

INCHI:

InChI=1S/C64H110N20O23/c1-11-30(9)49(83-53(96)33(15-17-42(66)86)74-61(104)50(31(10)12-2)84-60(103)48(29(7)8)82-51(94)32(65)22-43(67)87)62(105)81-41(26-85)59(102)79-39(24-45(69)89)57(100)80-40(25-47(92)93)58(101)77-36(20-27(3)4)54(97)73-34(16-18-46(90)91)52(95)78-38(23-44(68)88)56(99)76-37(21-28(5)6)55(98)75-35(63(106)107)14-13-19-72-64(70)71/h27-41,48-50,85H,11-26,65H2,1-10H3,(H2,66,86)(H2,67,87)(H2,68,88)(H2,69,89)(H,73,97)(H,74,104)(H,75,98)(H,76,99)(H,77,101)(H,78,95)(H,79,102)(H,80,100)(H,81,105)(H,82,94)(H,83,96)(H,84,103)(H,90,91)(H,92,93)(H,106,107)(H4,70,71,72)/t30-,31-,32-,33-,34-,35-,36-,37-,38-,39-,40-,41-,48-,49-,50-/m0/s1

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: This peptide corresponds to amino acids 93–105 of human leptin, an adipocyte-derived hormone that regulates appetite, energy expenditure, and body weight homeostasis. Leptin signals nutritional status to the hypothalamus and modulates neuroendocrine pathways controlling feeding behavior and metabolism. The 93–105 region contributes to structural and receptor-interaction properties of the hormone. This fragment is used in structure–function analyses, receptor-binding studies, and investigations of leptin-mediated signaling pathways. It supports research focused on obesity, metabolic syndrome, endocrine regulation, and energy balance, as well as studies exploring mechanisms of leptin resistance and metabolic dysregulation.

Current Research: Leptin is a hormone primarily produced by adipocytes that plays a central role in regulating appetite, energy expenditure, and body weight homeostasis. Acting as a key signal of nutritional status, leptin communicates the body’s energy reserves to the central nervous system, particularly the hypothalamus. Through this signaling pathway, leptin influences feeding behavior, metabolic rate, and neuroendocrine functions. Synthetic peptide fragments derived from leptin provide valuable tools for dissecting the structural and functional elements of this hormone. The Leptin (93–105) peptide, corresponding to amino acids 93–105 of human leptin, represents a region involved in receptor interactions and structural stability, making it useful for biochemical and signaling studies related to metabolic regulation. Leptin and Energy Homeostasis Leptin was originally identified as a hormone that links adipose tissue mass to the regulation of appetite and energy balance. As fat stores increase, leptin levels in circulation rise, signaling the brain that sufficient energy reserves are available. Conversely, reduced fat stores lead to decreased leptin levels, which stimulate appetite and reduce energy expenditure. This hormone acts primarily on the hypothalamus, where it interacts with specific neuronal populations that regulate feeding behavior. By modulating the activity of appetite-regulating neuropeptides, leptin helps maintain long-term stability of body weight and metabolic balance. Beyond its role in appetite control, leptin also influences glucose metabolism, endocrine signaling, immune responses, and reproductive function, highlighting its importance as a systemic metabolic regulator. Structure and Receptor Interaction Leptin is a protein hormone composed of several α-helical regions that form a compact structure required for interaction with its receptor, the leptin receptor (Ob-R). Binding of leptin to its receptor initiates intracellular signaling pathways that regulate gene expression and neuronal activity. The 93–105 region of leptin lies within a segment of the hormone that contributes to its structural integrity and receptor interaction properties. Although it represents only a small portion of the full protein, this sequence participates in the overall folding and functional conformation required for receptor engagement. Studying this fragment allows researchers to explore how specific regions of leptin contribute to receptor recognition and signaling activation. Leptin Receptor Signaling Pathways When leptin binds to its receptor in the hypothalamus and other tissues, it activates several intracellular signaling cascades. One of the primary pathways involves the JAK–STAT signaling system, which regulates transcription of genes involved in appetite suppression and energy metabolism. Additional pathways, including MAPK and PI3K signaling, also contribute to leptin-mediated cellular responses. These pathways influence neuronal activity, glucose metabolism, and lipid utilization, integrating leptin signaling with broader metabolic networks. Because disruptions in leptin signaling can significantly affect metabolic regulation, detailed studies of receptor interaction regions—such as the 93–105 sequence—help clarify the molecular basis of leptin function. Applications in Structure–Function Studies The Leptin (93–105) peptide is frequently used in structure–function analyses designed to determine how individual regions of the hormone contribute to its biological activity. By studying peptide fragments separately from the full protein, researchers can evaluate how specific amino acid sequences influence receptor binding, protein folding, and signaling efficiency. Such studies help identify critical residues involved in leptin–receptor interactions and provide insight into the structural requirements for effective signaling. Investigating Receptor Binding Mechanisms Synthetic fragments like the 93–105 peptide are also useful in receptor-binding experiments. Researchers can examine how peptide sequences interact with components of the leptin receptor or influence receptor activation. These experiments contribute to understanding the molecular interface between leptin and its receptor and help identify structural features that control signaling strength and specificity. Insights gained from these studies are valuable for understanding how leptin communicates metabolic information to target tissues. Relevance to Obesity and Metabolic Disorders Leptin signaling is critically involved in maintaining metabolic balance, and disturbances in this pathway can contribute to obesity and metabolic syndrome. In many cases of obesity, circulating leptin levels are elevated, yet the body fails to respond appropriately to the hormone—a condition known as leptin resistance. Understanding the molecular mechanisms underlying leptin resistance is a major focus of metabolic research. Peptide fragments derived from leptin help investigators examine how receptor interactions and signaling pathways may be altered in metabolic disorders. Research involving leptin fragments therefore contributes to broader efforts aimed at understanding metabolic dysregulation, insulin resistance, and obesity-related diseases. Supporting Studies of Endocrine Regulation In addition to metabolic effects, leptin participates in neuroendocrine regulation, influencing hormone release and physiological processes such as reproduction and stress responses. Because leptin signaling integrates nutritional status with endocrine control systems, detailed investigation of leptin structure and receptor interactions is important for understanding how energy balance affects hormonal regulation. The Leptin (93–105) peptide provides a simplified system for exploring these mechanisms at the molecular level. Conclusion The Leptin (93–105) peptide represents a defined fragment of the human leptin hormone involved in structural stability and receptor interaction. By isolating this region, researchers can investigate the molecular features that contribute to leptin signaling and metabolic regulation. Its applications include structure–function analyses, receptor-binding studies, and investigations of leptin-mediated signaling pathways. Through these studies, the peptide supports research into the biological mechanisms underlying energy balance, endocrine regulation, and metabolic disorders such as obesity and leptin resistance.