Bcl-2-like protein 1
Bcl-2-like protein 1 (173-182) is a synthetic peptide fragment corresponding to amino acids 173 through 182 of the Bcl-2-like protein 1 sequence, a member of the Bcl-2 family of apoptosis-regulating proteins. As a segment derived from a key region of this protein, it is of significant interest in the study of programmed cell death mechanisms, protein-protein interactions, and the modulation of apoptotic pathways. Researchers utilize such peptide fragments to dissect the structural and functional roles of specific motifs within the larger Bcl-2-like protein 1 molecule, enabling deeper understanding of mitochondrial integrity, cellular stress responses, and the regulation of cell survival and death across various biological systems.
Peptide-based apoptosis research: The 173-182 fragment of Bcl-2-like protein 1 is widely used in apoptosis research to probe the functional domains responsible for anti-apoptotic activity. By introducing this peptide into in vitro systems, investigators can assess its ability to mimic or disrupt native protein interactions within the Bcl-2 family, thereby elucidating the molecular determinants of apoptosis inhibition. Such studies are crucial for mapping the sequence-specific effects on mitochondrial outer membrane permeabilization and for identifying residues essential for binding to pro-apoptotic partners.
Protein-protein interaction mapping: The synthetic peptide serves as a valuable tool for characterizing the interaction interfaces between Bcl-2-like proteins and their binding partners, such as BH3-only proteins or other regulatory factors. Through techniques like pull-down assays, surface plasmon resonance, or fluorescence polarization, the fragment enables detailed analysis of binding affinities and specificities. These insights help clarify the conformational dynamics and competitive interactions that govern apoptotic signaling cascades.
Structural biology and conformational studies: Researchers employ the 173-182 peptide in structural investigations, including NMR spectroscopy and X-ray crystallography, to determine secondary structure propensities and conformational preferences of this functional region. Such studies inform on the peptide's ability to adopt helical or loop conformations, providing foundational data for modeling the full-length protein and for understanding structure-function relationships in Bcl-2 family members. This information is instrumental in the rational design of peptide mimetics or inhibitors.
Peptide synthesis and assay development: The defined sequence of this Bcl-2-like protein 1 fragment makes it a useful standard in the optimization of solid-phase peptide synthesis protocols and in the calibration of analytical techniques such as HPLC and mass spectrometry. Laboratories can utilize the peptide to validate synthesis yields, assess purity, and establish assay sensitivity, supporting broader applications in peptide chemistry and analytical method development.
Screening of modulators and inhibitor design: The peptide fragment is frequently incorporated into high-throughput screening platforms to identify small molecules, peptides, or other agents capable of modulating Bcl-2 family protein interactions. By serving as a target or competitor in binding assays, it facilitates the discovery and characterization of novel compounds that may alter apoptotic signaling pathways. Such applications are integral to early-stage research in chemical biology, enabling the exploration of structure-activity relationships and the evaluation of candidate modulators for further study.
2. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. High fat diet and GLP-1 drugs induce pancreatic injury in mice
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