COLIVELIN - 100mg
Colivelin is a humanin-family peptide that has been extensively investigated in preclinical research models for its involvement in neuronal stress-response pathways. Experimental studies conducted in vitro and in vivo indicate that Colivelin may influence mechanisms associated with amyloid-related aggregation processes, neuronal apoptosis, and synaptic plasticity regulation under neurodegenerative conditions.
Description
SPECIFICATIONS
Product Code: COL100
Sequence: H-Ser-Ala-Leu-Leu-Arg-Ser-Ile-Pro-Ala-Pro-Ala-Gly-Ala-Ser-Arg-Leu-Leu-Leu-Leu- Thr-Gly-Glu-Ile-Asp-Leu-Pro-OH
Molecular Formula: C119H206N32O35
Molecular Weight: 2645.13 g/mol
CAS: 867021-83-8
Purity: Technical / Research Grade 98%
Other details: No TFA Salt
Form: Lyophilized powder
Color: White
Storage temperature: -20°C
Source: Synthetic
Safety classification: Standard handling
DESCRIPTION
Colivelin is a 26–amino-acid synthetic hybrid peptide belonging to the humanin (HN) peptide family, originally described in the mid-2000s. Peptides of the humanin family have been extensively investigated in preclinical neuroscience research for their involvement in neuronal survival signaling and resistance to amyloid-associated cellular stress under experimental conditions.
Humanin-derived hybrid peptide design
Colivelin was developed as a next-generation humanin derivative by combining two neuroactive peptide motifs: a modified segment of humanin and a fragment derived from activity-dependent neurotrophic factor (ADNF). This hybrid design has been used in laboratory studies to explore whether convergent neuroprotective signaling pathways can be engaged simultaneously within a single peptide construct.
Amyloid-associated neurotoxicity research
In cell culture systems, Colivelin has been examined for its ability to modulate amyloid-associated neuronal stress responses, including resistance to beta-amyloid–induced toxicity and other experimentally induced apoptotic stimuli. Comparative in vitro studies have evaluated its activity relative to parent humanin peptides, focusing on cell viability, apoptotic markers, and synaptic integrity–related parameters.
STAT3 and JAK/STAT pathway investigations
Colivelin has been investigated as an experimental modulator of STAT3-associated signaling pathways. In neuronal cell models, activation of JAK/STAT3 signaling has been linked to altered expression of anti-apoptotic and survival-associated genes, providing a mechanistic framework for studying how STAT3 activation influences neuronal resilience and axonal maintenance under stress conditions.
Neurodegeneration and synaptic plasticity research
In animal models expressing amyloid-related genetic alterations, Colivelin has been explored for its effects on synaptic plasticity, learning- and memory-associated signaling, and neuroinflammatory markers. Experimental outcomes have been assessed using behavioral paradigms, biochemical analyses, and histological evaluation, focusing on pathway modulation rather than functional restoration.
Ischemia and neuronal stress models
Colivelin has also been included in preclinical cerebral ischemia research to study neuronal survival, axonal integrity, and stress-responsive gene expression following experimentally induced ischemic insults. Observations from these systems have been used to examine how anti-apoptotic gene regulation, STAT3 signaling, and cytoskeletal remodeling interact during post-ischemic neuronal adaptation.
Extracellular and intracellular signaling mechanisms
Experimental evidence suggests that peptides of the humanin family, including Colivelin, may exert biological activity through both extracellular receptor-mediated mechanisms and intracellular signaling interactions. Laboratory studies have investigated peptide binding to cell-surface receptors as well as downstream activation of intracellular signaling cascades, including JAK2/STAT3-related pathways, under controlled experimental conditions
REFERENCES
All information presented above is derived from in vitro experiments, animal studies, and other preclinical research models. These data are intended solely for basic scientific investigation of biological mechanisms and do not imply any therapeutic, diagnostic, preventive, or clinical use in humans or animals.
M. Kostomoiri et al., "New labeled derivatives of the neuroprotective peptide colivelin: Synthesis, characterization, and first in vitro and in vivo applications" ScienceDirect[]
M. Yamada et al., "Nasal Colivelin Treatment Ameliorates Memory Impairment Related to Alzheimer's Disease" [Nature]
M. Matsuoka et al., "Humanin and colivelin: neuronal-death-suppressing peptides for Alzheimer's disease and amyotrophic lateral sclerosis" [PubMed]
T. Vhiba et al., "Development of a Femtomolar-Acting Humanin Derivative Named Colivelin by Attaching Activity-Dependent Neurotrophic Factor to Its N Terminus: Characterization of Colivelin-Mediated Neuroprotection against Alzheimer's Disease-Relevant Insults In Vitro and In Vivo" [The Journal of Neuroscience]
K. Oikawa ert al., "P2-328: The role of colivelin, a novel neuroprotective peptide, on hippocampal synaptic plasticity" [The Journal of the Alzheimer's Association]
H. Zhao et al., "Colivelin Rescues Ischemic Neuron and Axons Involving JAK/STAT3 Signaling Pathway" [PubMed]
DISCLAIMER
This product is intendend for lab research and development use only. These studies are performed outside of the body. This product is not medicines or drugs and has not been approved by the FDA or EMA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law. This product should only be handled by licensed, qualified professionals.
All product information provided on this website is for informational and educational purposes only.
Data sheet
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