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.
CD164 molecule (CD164) is a type I single-pass transmembrane mucin glycoprotein encoded by the CD164 gene, broadly expressed on hematopoietic progenitor, epithelial and mesenchymal cell plasma membranes across multiple tissue compartments. The polypeptide carries an extensively O-glycosylated extracellular mucin domain, a single hydrophobic transmembrane helix and short cytoplasmic terminal segments bearing conserved protein interaction motifs. As a surface glycoprotein, it participates in intercellular contact regulation and compartmental retention of progenitor cell populations under steady tissue development conditions. The abundant glycan chains distributed on the outer surface form a hydrated protective layer that limits excessive non-specific cell attachment events, while discrete protein epitopes support selective binding to matching cell-surface partner molecules. Without sufficient CD164 expression to balance adhesion intensity, progenitor cell pools tend to undergo premature detachment from supporting tissue stroma, which disturbs the ordered maintenance of undifferentiated cell reserves in tissue niches. Different tissue microenvironments form distinct adhesion gradient requirements; stromal and progenitor cell interfaces rely on CD164-mediated dual regulation of glycan shielding and specific protein-protein contacts to sustain balanced niche retention capacity across developmental stages. Extensive glycosylation modification patterns shift alongside cell differentiation status, and these glycan variations may adjust the relative strength of CD164-dependent intercellular binding without altering core transmembrane anchoring architecture.
Sequence variations within CD164 coding sequences could change the length of extracellular mucin regions or disrupt cytoplasmic binding motifs, which tends to interfere with normal progenitor cell niche retention observed in tissue model systems. No other type I mucin fully combines the dual functions of non-specific adhesion buffering and selective stromal partner recognition as seen in CD164, though other membrane mucins carry partial overlapping glycan barrier capacity. CD164 stably embeds within lipid bilayers and will not shed into free soluble fractions under physiological steady states, unless triggered by specialized proteolytic cleavage events. Its type I integral membrane topology separates extracellular glycan-rich domains from cytoplasmic regulatory motifs, granting the protein dual potential to modulate surface contact accessibility and transmit weak intracellular feedback signals linked to niche occupancy shifts. Reduced functional CD164 levels weaken the glycan shielding barrier and lower specific stromal binding affinity simultaneously, disrupting the equilibrium of progenitor cell retention and mobilization within tissue microenvironments, which makes this mucin a suitable research subject for cell niche and adhesion regulatory analysis.
Fig. 1 Domain and glycosylation‑site annotation of human CD164 primary sequence and membrane topology, illustrating signal peptide, dual mucin domains, transmembrane helix and short cytoplasmic tail.1
The biological functions of integral membrane CD164 mucin protein are focused on extracellular glycan shielding and selective intercellular partner interaction:
Creative Biolabs offers purified CD164 membrane protein samples produced under unified preparation workflows, including full-length CD164 constructs and isolated extracellular mucin domain variants. Truncated polypeptide fragments cannot support complete glycan barrier formation and stromal binding activity, while full-length constructs fit progenitor niche adhesion research. All batches receive uniform quality screening. Functional assessments may only be performed under simulated lipid bilayer microenvironment setups. Extracellular glycosylated domain structural features are preserved across batches to support comparative intercellular binding analysis between experimental groups. Full-length CD164 membrane samples retain intact glycan modification sites and cytoplasmic interaction motifs after standardized purification, which supports reliable detection of weak and transient cell partner binding events in comparative membrane functional analysis.
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Creative Biolabs provides cell research models with adjustable CD164 expression levels, suitable for structural observation of type I mucin transmembrane proteins and progenitor niche interaction research. Sample assessment covers sustained target membrane expression detection and preliminary stromal binding analysis, enabling side-by-side comparison of cell retention behavior under varying CD164 abundances. These cell models can be paired with tissue compartment observation schemes to track progenitor mobilization shifts linked to CD164 dosage changes.
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Anti-CD164 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for progenitor cell membrane localization mapping and cell contact complex identification. The antibody series works with common laboratory detection reagents to support multi-dimensional observation of CD164 distribution within stromal tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for CD164 research:
CD164 may act as type I transmembrane mucin to form extracellular glycan barriers and mediate selective binding with stromal cells for progenitor niche maintenance.
CD164 expression status tends to adjust progenitor cell retention efficiency, serving as a key mediator of tissue niche homeostasis biological processes.
No, all CD164 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 CD164 membrane protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on mucin-regulated cell adhesion.
Laboratory analysis schemes may include cell co-binding assays to assess intercellular interaction capacity under simulated lipid bilayer environments.
