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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EPH receptor B2 (EPHB2) is a single pass transmembrane receptor tyrosine kinase encoded by EPHB2 gene. This protein localizes to plasma membrane of many cell populations. EPHB2 contains large extracellular ligand binding region, one transmembrane helix and an intracellular cytoplasmic segment with tyrosine kinase catalytic domain. Extracellular region includes globular ephrin binding domain together with additional cysteine rich and repeat modules exposed to extracellular environment. Cytoplasmic side houses kinase domain plus multiple tyrosine residues available for phosphorylation events. Newly synthesized EPHB2 folds inside endoplasmic reticulum compartments before trafficking toward cell surface. Extracellular domain folding requires formation of conserved disulfide bond arrangements. Different cell types show variable EPHB2 expression magnitude. Only properly folded molecules can accumulate at cell surface and participate in cell cell contact events. Correct formation of disulfide bonds is critical to maintain native conformation of extracellular ligand binding modules.
EPHB2 extracellular globular domain binds B class ephrin ligands presented on adjacent opposing cell surfaces. Ligand engagement driven by direct cell cell contact triggers receptor oligomerization at plasma membrane. Oligomer formation activates intrinsic cytoplasmic tyrosine kinase catalytic activity. Activated kinase domain carries out auto phosphorylation on multiple intracellular tyrosine sites, generating docking phosphotyrosine motifs for recruitment of cytosolic signal adaptor proteins. Other Eph family paralogs possess distinct ephrin binding preference and cannot fully recapitulate EPHB2 response profile. Variation in EPHB2 surface abundance changes number of available receptor units ready to respond to cell contact presented ephrin ligands. Mutation within extracellular ligand binding domain impairs ephrin recognition. Alteration of kinase domain residues can abolish catalytic turnover without preventing ligand driven receptor oligomerization. Changes to intracellular tyrosine sites modify spectrum of recruited cytosolic signalling partners after receptor activation, and adjust downstream signal output intensity without fully eliminating receptor oligomer formation.
Fig. 1 Schematic of EPHB2‑ephrin bidirectional juxtacrine signalling complex. Cell‑cell contact enables ligand‑receptor recognition. Transmembrane EPHB2 triggers forward signalling via intracellular tyrosine phosphorylation; ephrin mediates reverse signalling on the opposing cell, jointly driving downstream effector recruitment.1
The biological functions of EPHB2 are focused on ephrin ligand recognition, cell contact triggered receptor oligomerization and tyrosine kinase dependent intracellular signal propagation:
Creative Biolabs offers purified EPHB2 membrane samples via standardized preparation workflows, including full length EPHB2 constructs and isolated extracellular ligand binding domain variants. Isolated extracellular fragments may not support complete ephrin triggered oligomerization and intracellular kinase signalling related behaviours, while full length constructs may be suited for eph ephrin cell contact signalling associated research. All samples receive routine quality screening, and functional relevant observation may only be carried out with full length samples under simulated membrane environments. All sample batches follow unified processing standards to maintain consistent structural features for comparative laboratory analysis across separate test groups.
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Creative Biolabs provides adjustable EPHB2 expression cell models with varied expression levels, applicable to transmembrane receptor tyrosine kinase structural characteristic observation and ephrin dependent cell cell signalling related research. Sample evaluation includes sustained target expression detection and preliminary intermolecular interaction associated observation, which can support comparative analysis of receptor associated behaviours under different expression statuses. These cell systems can be matched with diverse laboratory analysis schemes to observe changes of ligand triggered signal output efficiency under different target expression abundances.
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Antibody reagents targeting EPHB2 are generated via mature protein preparation workflows, compatible with multiple routine laboratory detection methods for cellular localization profiling and molecular complex identification, to support systematic analysis of EPHB2 distribution and eph receptor associated molecular complexes across diverse laboratory research setups. The antibody series can cooperate with other common laboratory detection reagents to complete multi dimensional observation of target distribution inside tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for EPHB2 research:
EPHB2 may function as transmembrane Eph receptor tyrosine kinase and participate in B class ephrin ligand recognition, contact driven oligomerization and tyrosine kinase dependent intracellular signal propagation.
EPHB2 expression status may influence juxtacrine cell cell signal response capacity, serving as a major regulatory mediator of eph ephrin contact signalling related biological processes.
No, all EPHB2 related products and services are strictly for research use only, not intended for clinical related operations. All material designs and functional tests are only optimized for basic laboratory research scenarios, without matching clinical application standards.
Offerings include full length EPHB2 membrane protein, target specific recombinant antibodies and adjustable expression cell research models, supporting eph ephrin cell cell contact signalling research.
Laboratory observation schemes may include eph receptor ephrin ligand interaction related tests to analyse receptor associated behaviours under simulated cellular environments.
