ALX 40-4C Trifluoroacetate

ALX 40-4C Trifluoroacetate is a small peptide inhibitor of the chemokine receptor CXCR4, inhibits SDF-1 from binding CXCR4 with a Ki of 1 μM, and suppresses the replication of X4 strains of HIV-1; ALX 40-4C Trifluoroacetate also acts as an antagonist of the APJ receptor, with an IC50 of 2.9 μM.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1183

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M.F/Formula
C₅₈H₁₁₄F₃N₃₇O₁₂
M.W/Mr.
1578.76
Sequence
One Letter Code: Ac-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-NH2
three Letter Code: Ac-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-d-Arg-NH2

ALX 40-4C Trifluoroacetate is a synthetic peptide compound widely recognized for its utility in biochemical and molecular research, particularly in studies related to chemokine receptor interactions and immune cell signaling. Structurally, it is a peptide antagonist designed to selectively inhibit the function of the CXCR4 chemokine receptor, a key player in cellular migration, immune surveillance, and various pathological processes. Its trifluoroacetate salt form enhances solubility and stability, making it suitable for a range of in vitro and ex vivo applications. As a research tool, ALX 40-4C Trifluoroacetate facilitates precise interrogation of CXCR4-mediated pathways, enabling researchers to dissect complex signaling networks and cellular responses.

Receptor Antagonism Studies: ALX 40-4C Trifluoroacetate is extensively employed in the investigation of CXCR4 receptor function and inhibition. By competitively binding to the CXCR4 receptor, the peptide blocks the interaction with its natural ligand, stromal cell-derived factor 1 (SDF-1 or CXCL12). This antagonistic activity provides a robust platform for delineating the role of CXCR4 in cell signaling, migration, and downstream gene expression. Researchers utilize the compound to study receptor pharmacology, characterize ligand-receptor dynamics, and validate CXCR4 as a molecular target in diverse biological systems.

Cell Migration and Chemotaxis Assays: The peptide's ability to modulate chemokine-driven cellular movement makes it a valuable reagent in chemotaxis and cell migration assays. By inhibiting CXCR4-mediated chemotactic responses, ALX 40-4C Trifluoroacetate enables scientists to assess the contribution of this receptor to the directed movement of immune cells, stem cells, and other cell types. Such studies are critical for understanding mechanisms of immune cell trafficking, tissue homing, and cellular responses to microenvironmental cues in both physiological and pathological contexts.

Signal Transduction Analysis: In the context of intracellular signaling research, ALX 40-4C Trifluoroacetate serves as a selective probe for dissecting CXCR4-dependent pathways. Researchers leverage its specificity to inhibit receptor activation and monitor subsequent effects on intracellular signaling cascades, such as those involving G-protein coupled receptor (GPCR) mechanisms, calcium flux, and kinase activation. These studies provide mechanistic insights into how CXCR4 engagement translates into functional cellular outcomes and inform the design of targeted intervention strategies in cell biology.

Peptide Functional Studies: As a chemically defined peptide antagonist, ALX 40-4C Trifluoroacetate is integral to functional studies exploring peptide-receptor interactions. Its use allows for quantitative and qualitative assessment of peptide structure-activity relationships, receptor binding affinity, and antagonist potency. Such investigations are vital for the rational design of next-generation peptide modulators, optimization of pharmacological profiles, and the advancement of peptide-based research tools targeting chemokine receptors.

In vitro Model Development: The compound is also utilized in the development and validation of in vitro models that recapitulate CXCR4-dependent biological phenomena. By incorporating ALX 40-4C Trifluoroacetate into experimental systems, researchers can selectively block receptor function, thereby establishing controlled conditions for studying cell signaling, migration, and microenvironmental interactions. These models are instrumental in elucidating the molecular underpinnings of immune cell dynamics and in screening for novel modulators of chemokine receptor activity.

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