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Hepatitis A virus cellular receptor 1 (HAVCR1), also known as TIM-1 or KIM-1, is a single-pass transmembrane glycoprotein encoded by the HAVCR1 gene and expressed on selected epithelial and immune cell populations. Unlike soluble cytoplasmic proteins, HAVCR1 contains a single transmembrane segment and a large extracellular region comprising an N-terminal immunoglobulin variable (IgV)-like domain and a mucin-like domain. The IgV domain can recognize phosphatidylserine exposed on apoptotic cells and other membrane-derived structures, supporting cell-surface recognition and uptake-related processes. HAVCR1 can also participate in immune-related ligand interactions and cellular responses in a context-dependent manner.
The extracellular region of HAVCR1 is subject to proteolytic ectodomain shedding, including cleavage mediated by metalloproteases such as ADAM10 and ADAM17. This shedding can regulate the amount of receptor retained at the cell surface and generate soluble HAVCR1 ectodomain fragments. Different cell and tissue contexts may therefore influence HAVCR1 surface abundance, ligand engagement, and downstream biological effects. Rather than functioning as a general buffering receptor for intercellular adhesion, HAVCR1 is better characterized as a membrane-associated recognition molecule involved in phosphatidylserine binding, cellular uptake, and immune-related interactions.
HAVCR1 may also participate in intracellular signaling events initiated by extracellular ligand engagement. Sequence variants within the HAVCR1 gene may affect receptor expression, extracellular recognition, or other functional properties, although the consequences of individual variants require experimental validation. Variations in HAVCR1 expression and shedding can influence receptor availability at the cell surface, making HAVCR1 a useful research target for studies of membrane receptor biology, phosphatidylserine recognition, ectodomain processing, and immune-related cell interactions.
HAVCR1 localizes to the plasma membrane, where its extracellular IgV and mucin-like regions mediate interactions with extracellular ligands and membrane-associated targets. Its transmembrane topology distinguishes it from soluble intracellular proteins, while its ectodomain can undergo regulated proteolytic shedding. Changes in HAVCR1 expression, localization, ligand engagement, or shedding may alter cellular uptake and signaling responses, supporting its use in basic studies of single-pass transmembrane receptor function.
Fig. 1 Schematic domain topology of human HAVCR1 (TIM‑1) single‑pass transmembrane receptor, showing IgV‑like domain, mucine‑like domain, transmembrane region and cytoplasmic domain.1
The biological functions of integral membrane HAVCR1 receptor are focused on sustained surface ligand binding and cytoplasmic signal cascade transmission:
Creative Biolabs offers purified HAVCR1 membrane protein samples produced under unified preparation workflows, including full-length HAVCR1 constructs and isolated extracellular ligand-binding domain variants. Truncated receptor fragments cannot support complete surface ligand recognition and cytoplasmic signal coupling activity, while full-length constructs fit research focused on membrane receptor-ligand interaction and adhesion conformational analysis. All batches receive uniform quality screening. Functional assessments may only be performed on full-length membrane receptor under simulated lipid bilayer microenvironment setups. Consistent extracellular domain structural features are preserved across batches to support comparative laboratory analysis between experimental groups. Full-length HAVCR1 membrane samples retain intact extracellular ligand-binding pocket conformation after standardized purification, which supports reliable detection of weak and transient ligand-receptor binding events in comparative membrane functional analysis.
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Creative Biolabs provides cell research models with adjustable HAVCR1 expression levels, suitable for structural observation of single-pass transmembrane receptors and research into cell surface ligand interaction processing. Sample assessment covers sustained target membrane expression detection and preliminary ligand-receptor interaction analysis, enabling side-by-side comparison of receptor conformational behavior under varying membrane expression abundances. These cell models can be paired with diverse laboratory analysis schemes to track shifts in ligand response efficiency alongside changing target membrane protein levels.
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Anti-HAVCR1 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for plasma membrane localization mapping and identification of ligand-receptor complexes. The antibody series works with common laboratory detection reagents to support multi-dimensional observation of target membrane distribution within tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for HAVCR1 research:
HAVCR1 may act as an integral single-pass transmembrane receptor and participate in transmembrane transmission of extracellular adhesion molecular signals.
HAVCR1 expression status may alter membrane ligand response capacity and intracellular messenger cascade output, serving as a key mediator of tissue intercellular adhesion biological processes.
No, all HAVCR1 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material design and functional screening are optimized exclusively for basic laboratory research, without meeting clinical application criteria.
Offerings include full-length HAVCR1 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on membrane receptor-ligand interaction and intercellular adhesion signal transduction.
Laboratory analysis schemes may include surface ligand binding assays to assess its ligand recognition capacity under simulated lipid bilayer environments.