Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsCreative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
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Loading...All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
Guided entry of tail-anchored proteins factor 3, ATPase (GET3) is a soluble cytoplasmic ATPase encoded by the GET3 gene, distributed within cytoplasmic chaperone compartments across multiple somatic cell populations. Unlike integral membrane transporters with multi-spanning lipid helices, GET3 contains no transmembrane anchoring segments and functions as a soluble cytoplasmic sorting factor for tail-anchored polypeptide precursors. It appears to operate as a resident cytoplasmic ATP-dependent chaperone to coordinate controlled delivery of tail-anchored protein substrates to membrane insertion sites under physiological protein sorting conditions. Unbound tail-anchored polypeptides easily form misfolded aggregates without GET3-mediated chaperone buffering, and GET3 establishes moderate sorting balance to sustain steady precursor trafficking toward lipid bilayers. Different cytoplasmic translation zones produce distinct tail-anchored protein precursors, requiring coordinated soluble ATPase factors to maintain balanced membrane insertion rates. Cytosolic GET3 may continuously bind newly synthesized tail-anchored peptides and deliver them to target membrane sites, limiting cytoplasmic aggregation and preserving membrane insertion homeostasis. Sustained chaperone binding maintained by GET3 prevents aberrant aggregation of uninserted tail-anchored polypeptides, which could disrupt cytoplasmic sorting pathways and interfere with steady supply of membrane precursor substrates across cell populations.
GET3 may mediate ATP-powered precursor transport from ribosomal zones to membrane bilayers. Sequence variants within the GET3 gene alter polypeptide binding affinity and correlate with disrupted protein sorting states. No other cytoplasmic sorting ATPase fully recapitulates GET3’s dual capacity for tail-anchored peptide capture and ATP-driven trafficking. Variations in GET3 expression levels likely correspond to cellular membrane protein biogenesis status, rendering the enzyme a suitable research target for cytoplasmic chaperone and membrane insertion analysis. GET3 localizes freely within aqueous cytoplasm, without embedding into lipid bilayer structures. Its fully soluble cytosolic localization separates it from integral membrane transport proteins, carrying dual potential roles in preventing precursor aggregation and regulating ordered tail-anchored protein membrane loading. GET3-coupled ATP hydrolysis may adjust cytoplasmic levels of uninserted polypeptides and modify overall membrane protein biogenesis efficiency. Reduced functional GET3 elevates misfolded precursor accumulation and weakens cellular membrane insertion capacity, making GET a research subject for cytoplasmic sorting ATPase studies.
Fig. 1 Ribbon representation of Get3 monomer in two orthogonal views, showing nucleotide‑binding domain (NBD) and helical finger domain.1
The biological functions of soluble cytoplasmic GET3 ATPase are focused on sustained tail-anchored precursor binding and ATP-fueled cytoplasmic trafficking:
Creative Biolabs offers purified GET3 protein samples produced under unified preparation workflows, including full-length GET3 constructs and isolated ATPase core domain variants. Truncated fragments cannot support complete peptide capture and ATP-dependent trafficking activity, while full-length constructs fit research focused on tail-anchored protein sorting. All batches receive uniform quality screening. Functional assessments may only be performed under simulated cytoplasmic aqueous microenvironment setups. Consistent ATPase pocket structure is preserved across batches to support comparative laboratory analysis between experimental groups. Full-length GET3 samples retain intact peptide-binding cleft and ATP coordination conformation after purification, supporting stable detection of transient peptide-enzyme binding during sorting functional analysis.
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Creative Biolabs provides cell research models with adjustable GET3 expression levels, suitable for observation of cytoplasmic sorting ATPases and research into tail-anchored precursor trafficking. Sample assessment covers sustained cytoplasmic target detection and preliminary peptide binding analysis, enabling side-by-side comparison of sorting efficiency at different GET3 abundances. These cell models can be matched with multiple analytical schemes to track changes in membrane precursor supply rates.
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Anti-GET3 recombinant antibodies are generated via standardized workflows, compatible with common detection techniques for cytoplasmic localization and peptide-chaperone complex identification. The antibody series supports multi-dimensional observation of GET3 distribution in tissue cytoplasmic compartments.
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Beyond catalog products, Creative Biolabs offers specialized custom services for GET3 research:
GET3 may act as a soluble cytoplasmic ATPase and mediate ATP-dependent sorting of tail-anchored protein precursors toward membrane insertion sites.
GET3 expression status may alter cytoplasmic precursor aggregation levels and cellular membrane insertion efficiency, acting as a key mediator of tail-anchored protein biogenesis.
No, all GET3 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 GET3 protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on tail-anchored peptide cytoplasmic sorting.
Laboratory analysis schemes may include tail-anchored peptide binding assays to assess its precursor capture capacity under simulated cytoplasmic environments.
