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TAS1R2

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All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

TAS1R2 (Taste 1 receptor member 2) encodes a multi‑pass transmembrane class‑C taste‑subfamily G‑protein‑coupled receptor protein predominantly localised to plasma‑membrane compartments, with minor protein fractions detected within intracellular vesicular membrane structures.This receptor protein occurs across multiple tissue populations and displays distinct, tissue‑biased expression profiles. Distinct from soluble intracellular polypeptides, it bears seven transmembrane helical segments together with sizable extracellular Venus‑flytrap and cysteine‑rich structural modules, alongside cytoplasmic coupling regions for downstream partner engagement.It acts as a membrane‑embedded receptor subunit, assembling with adjacent membrane‑resident partner components to form signal‑competent molecular assemblies under physiological states.Insufficient TAS1R2 protein abundance may impair normal membrane‑associated receptor‑partner complex assembly and disturb downstream cellular membrane‑adaptive behaviours. TAS1R2 may exert molecular buffering functions to sustain suitable receptor‑dependent molecular configurations within cell populations. Diverse cellular physiological and ligand‑responsive phases bring shifting membrane‑signal homeostasis demands, requiring varied transmembrane receptor proteins to maintain multicellular tissue physiological equilibrium. Membrane‑anchored TAS1R2 assembles with partner membrane‑resident protein units to counteract abnormal receptor‑complex rearrangements and preserve stable plasma‑membrane functional states.

Sequence‑level alterations to the TAS1R2 locus may compromise the structural organisation of assembled plasma‑membrane receptor‑partner complexes and alter readouts derived from cell‑surface molecular interaction events. Closely related members of class‑C taste receptor subfamily cannot fully replicate the complete set of TAS1R2‑dependent behaviours during heteromeric receptor‑complex formation and stable integration within plasma‑membrane assemblies.Shifts in TAS1R2 protein levels often align with cellular demands for membrane‑signal‑related activities, making this protein a useful research target to explore class‑C taste‑GPCR activities and membrane‑signal‑balance molecular dynamics. Predominantly distributed at plasma‑membrane together with minor intracellular membrane fractions, TAS1R2 contributes to heteromeric receptor‑complex formation and does not sustain constitutive persistent downstream signalling without appropriate ligand‑derived stimulation.Its multi‑modular seven‑transmembrane class‑C GPCR architecture equipped with large extracellular sensory domains distinguishes this glycoprotein from many other membrane‑embedded surface receptors; such structural features support the maintenance of membrane‑receptor complex arrangement and permit selective physical contacts with cell‑surface binding partners. Diminished functional performance of TAS1R2 may disturb the proper arrangement of plasma‑membrane receptor assemblies and weaken endogenous cellular adaptive buffering capacity, further supporting its research value for studies focused on taste‑sensing class‑C GPCR components.

Fig. 1 Cross-species taste receptor family diagram showing vertebrate T1R2/T1R3 sweet receptor architecture among other chemosensory receptors. (OA Literature)Fig. 1 Comparative schematic of taste receptor families in vertebrates and Drosophila, including the vertebrate T1R2/T1R3 sweet receptor.1

TAS1R2 Protein Function: Core Roles in Sweet-Receptor Heterodimer Formation and G-Protein-Coupled Signalling

The biological functions of transmembrane TAS1R2 receptor protein are focused on TAS1R2/TAS1R3 sweet-receptor heterodimer formation, ligand recognition and G-protein-coupled signalling:

  • Sweet-Receptor Heterodimer Formation: TAS1R2 associates with TAS1R3 to form the heterodimeric class-C GPCR that mediates sweet taste detection. Its Venus-flytrap domain, cysteine-rich domain and seven-transmembrane region support ligand recognition, intersubunit coupling and receptor activation.
  • Ligand-Dependent Signal Initiation: Sweet-ligand binding promotes conformational changes in the TAS1R2/TAS1R3 receptor and initiates downstream heterotrimeric G-protein signalling.
  • Class-C GPCR Domain Coupling: The extracellular sensory domains are coupled to the seven-transmembrane region, supporting propagation of ligand-induced conformational changes across the membrane.
  • Stimulus-Dependent Receptor Activation: Ligand-dependent activation of the TAS1R2/TAS1R3 complex modulates downstream sweet-taste signalling responses.
  • Research Model Relevance: Sequence variants of TAS1R2 may alter sweet-ligand recognition, TAS1R2/TAS1R3 receptor function or downstream signalling within laboratory research systems.

TAS1R2 Membrane Protein Product

Creative Biolabs offers purified TAS1R2 membrane samples produced under unified preparation workflows, including full-length TAS1R2 constructs and isolated domain variants. Truncated domain fragments cannot support complete surface-partner-complex assembly behaviours, while full-length constructs suit research focused on receptor-subunit-partner interaction and plasma-membrane anchoring functional observation. All batches receive uniform quality screening. Functional-relevant observation may only be carried out with full-length samples under simulated plasma-membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length TAS1R2 samples retain intact partner-interaction-domain conformation after standardized purification, which supports reliable detection of weak and transient subunit-partner contacts for comparative functional analysis.

TAS1R2 Membrane Protein Product

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TAS1R2 Stable Cell Line Product

Creative Biolabs provides adjustable TAS1R2 expression cell research models with varied expression levels, applicable to structural observation of multi-pass transmembrane class-C taste-GPCR-family receptor proteins and research into membrane-partner molecular interaction. Sample evaluation includes sustained target expression detection and preliminary partner-interaction observation, enabling side-by-side comparison of subunit-binding behaviours under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in partner-assembly efficiency alongside shifting target protein levels.

TAS1R2 Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

TAS1R2 Recombinant Antibody Product

Anti-TAS1R2 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for plasma-membrane localization mapping and identification of subunit-partner molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within membrane-enriched sample materials.

TAS1R2 Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • Partner Matching Structural Traits: Retains native membrane-receptor and partner-interaction-domain features, suited for laboratory observation of plasma-membrane-partner and transmembrane-receptor-subunit binding interactions.
  • Target Selective Recognition: Might bind distinct structural regions unique to TAS1R2, applicable to mechanistic research on class-C taste-GPCR proteins.
  • Plasma-Membrane Research Compatibility: Designed for routine laboratory analysis of regulatory pathways governing membrane-receptor-complex subunit-partner gradient balance.
  • Full Customization Support: Tailored TAS1R2 membrane protein, antibody and cell model development can be arranged to satisfy diversified taste-GPCR-receptor research demands.

Custom TAS1R2 Research Services

Beyond catalog products, Creative Biolabs offers specialized custom services for TAS1R2 research:

  • Custom TAS1R2 Protein Production: Tailored mutant and fluorescent-tagged TAS1R2 constructs for dual membrane-partner assembly analysis.
  • Custom Antibody Development: Generation of target-specific TAS1R2 antibodies for cell-membrane-subunit localization observation and subunit-partner complex detection.
  • Stable Cell Line Engineering: Construction of customized cell systems with tunable TAS1R2 expression levels.
  • Functional Assay Development: Custom design of detection workflows for observing membrane-partner and plasma-membrane-molecule binding activity.

Frequently Asked Questions (FAQ)

  1. What is the primary function of TAS1R2?

    TAS1R2 acts as a class-C GPCR subunit that heterodimerises with TAS1R3 to form the sweet taste receptor and supports ligand-dependent G-protein-coupled signalling.

  2. Why is TAS1R2 a significant research target?

    TAS1R2 is a key determinant of sweet-ligand recognition and TAS1R2/TAS1R3 receptor signalling, making it a useful target for studies of sweet taste receptor biology.

  3. Are Creative Biolabs' TAS1R2 products suitable for clinical use?

    No, TAS1R2-associated research reagents from Creative Biolabs are exclusively built for exploring membrane-receptor-dependent plasma-membrane signal-regulatory mechanisms, and shall not be deployed for any clinical-oriented workflows. These preparations are optimized for basic laboratory investigation and do not satisfy performance benchmarks required for clinical implementation.

  4. What types of TAS1R2 products does Creative Biolabs offer?

    Offerings include full-length TAS1R2 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on sweet-receptor assembly, ligand recognition and signalling.

  5. How to observe the partner-binding characteristics of TAS1R2 samples?

    Laboratory observation schemes may include subunit-partner interaction related tests to analyse molecular-binding associated behaviors under simulated plasma-membrane environments.

Reference
  1. Chen, Kejin, et al. "Ectopic taste receptors in animal physiology: Evolutionary conservation and functional diversification." Frontiers in Cell and Developmental Biology 13 (2025): 1660529. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fcell.2025.1660529
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