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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CRB2(Crumbs) is a single transmembrane apical membrane protein encoded by CRB2 gene, which is specifically located in the apical plasma membrane region of polarized epithelial cells and is the key core protein of epithelial polarity regulation system. There are obvious functional and structural differences between the protein and soluble cytoplasmic enzymes, and its molecular structure contains conservative extracellular adhesion motifs and cytoplasmic polar complex docking fragments, but it does not have catalytic domains that mediate substrate metabolism and decomposition. Under physiological steady-state conditions, CRB2 mainly plays a biological role as the apical scaffold receptor, and can combine with the cytoplasmic polar complex subunit to assemble functional complexes. When the function of anchoring scaffold factor at the top of epithelial cells is missing or insufficient, it is easy to cause the disorder of polar structure at the top of cells, and CRB2 can maintain the orderly assembly of polar structures in various epithelial tissue microenvironments through stable structural buffering. Different epithelial tissue functional zones can be assembled to form differentiated polar complex subunit combinations, which require diverse top transmembrane scaffold proteins to cooperate to maintain the overall polar homeostasis of epithelial barrier system. Membrane-anchored CRB2 can continuously recruit cytoplasmic polar complex subunits, effectively inhibit the disordered rearrangement of apical membrane structure, and ensure the stable maintenance of the polar state of epithelial cells.
Sequence variation of CRB2 gene can change its binding affinity with polar complex subunits, resulting in disorder of polarity construction of epithelial cells, and other known apical transmembrane proteins do not have the dual functional characteristics of CRB2, which has both extracellular molecular adhesion and cytoplasmic polar complex recruitment. The expression abundance of CRB2 is highly adaptive and dynamically linked with the polarization state of epithelial cells, which is an important target for studying the epithelial apical junction structure and the mechanism of cell polarity regulation. From the localization and functional characteristics, CRB2 is embedded in the lipid bilayer at the top of epithelial cells, which can simultaneously bind extracellular adhesion ligands and cytoplasmic polar subunits, and the binding process will not activate the continuous intracellular signal cascade reaction. The unique localization mode of its apical transmembrane makes it different from cytoplasmic soluble proteins, and it has the dual regulatory potential of maintaining the order of apical membrane structure and supporting supramolecular assembly of polar complexes. The down-regulation or functional loss of functional CRB2 protein will directly lead to the disorder of apical-basal polarity distribution of epithelial cells and weaken the structural stability of epithelial barrier, which fully highlights the important scientific research value of this protein in the basic research field of apical scaffold protein.
Fig. 1 Domain‑organization comparison of mammalian CRB‑family transmembrane proteins. CRB2 possesses characteristic extracellular EGF‑like and Laminin‑G modules, a single transmembrane helix, and cytoplasmic FERM‑ and PDZ‑binding motifs for polarity‑complex subunit recruitment.1
The biological functions of transmembrane CRB2 polarity scaffold protein are focused on sustained cytoplasmic polarity-subunit recruitment and apical-membrane structural coordination:
Creative Biolabs offers purified CRB2 membrane samples produced under unified preparation workflows, including full-length CRB2 constructs and isolated extracellular domain variants. Truncated extracellular fragments cannot support complete polarity-complex-recruitment behaviors, while full-length constructs suit research focused on apical-scaffold anchoring and epithelial-polarity assembly. All batches receive uniform quality screening. Functional relevant observation may only be carried out with full-length samples under simulated membrane microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length CRB2 samples retain intact polarity-subunit docking-motif conformation after standardized purification, which supports reliable detection of weak and transient protein-subunit contacts for comparative functional analysis.
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Creative Biolabs provides adjustable CRB2 expression cell research models with varied expression levels, applicable to structural observation of apical transmembrane scaffold proteins and research into polarity-complex-subunit-binding interaction. Sample evaluation includes sustained target expression detection and preliminary subunit-interaction observation, enabling side-by-side comparison of scaffold-recruitment behaviors under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in subunit-recruitment efficiency alongside shifting target protein levels.
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Anti-CRB2 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for epithelial apical-membrane localization mapping and identification of multi-subunit polarity molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within epithelial tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for CRB2 research:
CRB2 might act as an apical transmembrane scaffold protein and participate in recruiting cytoplasmic polarity-complex subunits to sustain ordered epithelial apical-basal polarity.
CRB2 expression status could alter epithelial polarity‑complex assembly efficiency and apical‑membrane structural stability, serving as a major regulatory mediator of epithelial‑cell‑polarity biological processes.
No, all CRB2 related products and services are strictly for research use only, and cannot be applied in clinical workflows. All material designs and functional tests are optimized exclusively for basic laboratory research scenarios, without matching clinical application standards.
Offerings include full‑length CRB2 membrane protein, target‑specific recombinant antibodies and tunable expression cell research models, supporting research on epithelial polarity homeostasis and apical‑junction‑complex assembly.
Laboratory observation schemes may include protein-subunit interaction related tests to analyze scaffold-recruitment-associated behaviors under simulated membrane environments.
