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.
Olfactomedin 4 (OLFM4) is a completely secreted soluble glycoprotein encoded by OLFM4 gene, which is mainly synthesized by epithelial cells and myeloid cells and secreted into the extracellular space. The primary sequence of the protein does not contain hydrophobic transmembrane anchoring fragment and has no cell membrane anchoring ability; Its mature spatial structure is centered on the highly conserved C-terminal olfactory mediator folding structure, and many glycosylation modification sites are distributed on the protein surface, which provides an important structural basis for its extracellular function regulation. Biochemical studies indicate that OLFM4 can participate in extracellular protein-protein interactions, while its glycan moieties may also support lectin-mediated recognition at the cell surface, consistent with its role as a secreted extracellular regulatory glycoprotein.
Under physiological steady-state conditions, OLFM4 secretion is associated with epithelial homeostasis and extracellular cell-interaction processes. Different epithelial and myeloid contexts can show distinct OLFM4 expression and secretion levels. Glycosylation can influence extracellular recognition, and reported interactions include lectin-mediated binding to OLFM4-associated glycans and protein-protein contacts involving the olfactomedin domain. These observations support studying OLFM4 as a secreted interaction protein rather than as a direct glycan crosslinker or matrix-buffering factor.
Sequence variation within OLFM4 may affect protein folding, glycosylation, or extracellular interaction properties. OLFM4 remains a secreted extracellular glycoprotein rather than an integral membrane protein, and its olfactomedin domain provides a platform for protein-protein interactions. Changes in OLFM4 expression have been investigated in epithelial and immune-cell contexts, including processes related to adhesion and tissue homeostasis. Thus, OLFM4 is a useful target for studying secreted olfactomedin biology and extracellular interaction mechanisms.
Fig. 1 Schematic representation of olfactomedin secretion and extracellular localization. Olfactomedin is secreted into the extracellular space, where its conserved olfactomedin domain facilitates protein-protein interactions. OLFM4, as a member of this family, shares this secretory property as a soluble extracellular glycoprotein.1
The biological functions of soluble secreted OLFM4 olfactomedin glycoprotein are focused on extracellular protein interactions and epithelial response regulation:
Creative Biolabs offers purified OLFM4 protein samples produced under unified preparation workflows, including full-length OLFM4 constructs and isolated C-terminal olfactomedin domain variants. Full-length and domain constructs can support comparative studies of OLFM4 extracellular interactions and epithelial biology. All batches receive uniform quality screening. Functional assessments may only be performed under simulated extracellular aqueous microenvironment setups. Conserved olfactomedin-domain structural features are preserved across batches to support comparative protein-interaction analysis between experimental groups. Full-length OLFM4 samples retain intact olfactomedin-domain conformation after standardized purification, supporting detection of weak and transient extracellular protein complexes in comparative functional analysis.
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Creative Biolabs provides cell research models with adjustable OLFM4 expression levels, suitable for structural observation of secreted olfactomedin glycoproteins and interstitial matrix research. Sample assessment covers secreted protein quantification and extracellular partner-binding analysis, enabling side-by-side comparison of extracellular interaction profiles under varying OLFM4 abundances. These cell models can be paired with localization or adhesion-related readouts to track response changes linked to OLFM4 secretion levels.
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Anti-OLFM4 recombinant antibodies are generated via standardized workflows, compatible with extracellular fluid glycoprotein detection and extracellular protein-complex identification. The antibody series supports multi-dimensional observation of OLFM4 distribution within epithelial interstitial spaces.
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Beyond catalog products, Creative Biolabs offers specialized custom services for OLFM4 research:
OLFM4 may act as a secreted olfactomedin glycoprotein that participates in extracellular protein interactions and epithelial homeostasis; its glycan moieties can also support lectin-mediated recognition.
OLFM4 expression and secretion are associated with epithelial and myeloid cell states, making it a useful target for studying extracellular interaction and tissue-homeostasis mechanisms.
No, all OLFM4 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 OLFM4 protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on extracellular protein interactions and epithelial biology.
Laboratory analysis schemes may include protein-binding or lectin-binding assays to assess extracellular interaction characteristics under defined conditions.
