biotin-Neurogranin (48-76), human

Product Name: biotin-Neurogranin (48-76), human

Sequence One Letter Code: Biotin-SGERGRKGPGPGGPGGAGVARGGAGGGPS-OH

Sequence Three Letter Code: biotin-Ser-Gly-Glu-Arg-Gly-Arg-Lys-Gly-Pro-Gly-Pro-Gly-Gly-Pro-Gly-Gly-Ala-Gly-Val-Ala-Arg-Gly-Gly-Ala-Gly-Gly-Gly-Pro-Ser-OH

Chemical Formula:C107H175N41O36S1

Molecular Weight: 2644.1

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Neurological Disease Research

Source / Species: human

Conjugation: Conjugated

Conjugation Type: Biotins

Code Nacres: NA.26

Application: Biotin-Neurogranin (48–76), human is an N-terminally biotinylated peptide derived from residues 48–76 of human neurogranin, a postsynaptic protein involved in calcium-mediated signaling and synaptic plasticity. This fragment represents a major endogenous neurogranin peptide detected in the human brain and has been associated with elevated cerebrospinal fluid levels in Alzheimer’s disease. The biotin tag enables sensitive detection, pull-down assays, ELISA development, and affinity-based biomarker research applications. This peptide supports investigations into synaptic dysfunction, cognitive decline mechanisms, and neurodegenerative disease progression. It is particularly useful in studies examining neurogranin as a biomarker for Alzheimer’s disease and related neurological disorders.

Current Research: Neurogranin is a postsynaptic, calmodulin-binding protein highly enriched in dendritic spines, where it modulates calcium–calmodulin signaling and contributes to long-term potentiation (LTP) and synaptic plasticity. Increasing evidence positions neurogranin as a sensitive marker of synaptic integrity, with cerebrospinal fluid (CSF) levels strongly correlated with synaptic loss in Alzheimer’s disease (AD). Among the endogenous fragments detected in human brain and CSF, the 48–76 region represents a prominent proteolytic product associated with disease-related synaptic degeneration. Current research focuses on neurogranin as a fluid biomarker reflecting early synaptic dysfunction preceding overt neuronal loss. Elevated CSF neurogranin levels have been reported in prodromal and mild cognitive impairment stages of AD, often correlating with amyloid burden and cognitive decline rates. Defined peptide fragments such as Neurogranin (48–76) are increasingly used to develop and validate immunoassays capable of distinguishing disease-specific proteoforms. The N-terminal biotin label enables affinity capture, sandwich ELISA optimization, and calibration of mass spectrometry–based quantification workflows. Mechanistically, studies investigating calcium dysregulation in AD highlight the importance of neurogranin cleavage and altered calmodulin binding in disrupted synaptic signaling. The 48–76 fragment provides a controlled reagent for mapping antibody epitopes, characterizing protease processing events, and analyzing fragment-specific interactions. Pull-down assays using the biotinylated peptide support identification of binding partners and evaluation of modification-dependent interactions within postsynaptic signaling complexes. Beyond Alzheimer’s disease, neurogranin alterations have been explored in other neurological conditions, including traumatic brain injury, Parkinson’s disease, and schizophrenia. Standardized peptide reagents facilitate cross-study comparison and biomarker assay harmonization. In translational research settings, reproducible synthetic fragments are essential for assay calibration, inter-laboratory validation, and development of diagnostic platforms integrating neurogranin with other synaptic and amyloid-related markers. Collectively, current research underscores neurogranin as a dynamic indicator of synaptic health and cognitive decline. Biotin-Neurogranin (48–76), human provides a well-defined tool for biomarker assay development, interaction studies, and mechanistic investigations into calcium-dependent synaptic dysfunction. Its utility spans basic neuroscience, translational biomarker validation, and therapeutic research targeting early synaptic pathology in neurodegenerative disease.