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.
Structural characteristics and physiological matrix remodeling function: Lysyl oxidase-like protein 2(LOXL2) is a copper-dependent extracellular amine oxidase of Lysyl oxidase family, which is mainly synthesized by fibroblasts and epithelial cells and secreted into extracellular matrix. The protein is significantly different from intracellular soluble oxidase, and its protein structure contains multiple scavenger receptor cysteine-rich binding domains and highly conserved C-terminal catalytic core, and has no transmembrane anchoring sequence and membrane localization structure characteristics. As a key regulatory factor binding to extracellular matrix, LOXL2 can mediate the oxidative deamination of matrix protein lysine residues under physiological steady-state conditions and participate in the modification and remodeling of extracellular matrix. When the functional reserve of secretory oxidase is insufficient, extracellular matrix components are prone to disorderly aggregation and abnormal assembly, and LOXL2 can play a buffering role in matrix remodeling and maintain the dynamic balance of fiber network maturation in various connective tissue microenvironments. The composition of extracellular matrix in different tissues is specific, and the multicellular tissue system needs to rely on diversified secretory oxidases to maintain the steady state of matrix assembly, in which LOXL2 located in extracellular matrix can continuously bind to fibrous matrix substrate, inhibit the abnormal rearrangement of matrix supramolecular network, and ensure the stability and integrity of local tissue structure.
Mutation effect, regulation mechanism and research value: Mutation of LOXL2 gene can change the catalytic binding ability of protein to substrate, and cause abnormal remodeling of spatial structure and assembly mode of tissue extracellular matrix. Of all the members of the lysyl oxidase family, only LOXL2 has both the catalytic function of fiber matrix substrate and the molecular recognition mediated by scavenger receptor, and no other family protein can completely reproduce its unique biological function. The expression abundance of LOXL2 is highly matched with connective tissue remodeling activity, which is an important research target to study the function of secreted lysyl oxidase and analyze the regulation mechanism of extracellular matrix. At the level of molecular regulation, LOXL2 is located in the matrix region through extracellular secretion, which specifically completes the substrate catalytic reaction, and this process will not induce the continuous activation of intracellular signal cascade. Different from intracellular oxidase regulatory factors, its extracellular matrix settlement characteristics enable it to simultaneously mediate the cross-linking modification of extracellular fiber matrix and the recognition of specific molecular chaperones. When the function of LOXL2 protein is damaged or the expression of LOXL2 protein is down-regulated, the process of maturation and modification of matrix protein will be disordered, and the buffering regulation ability of tissue local structure remodeling will be significantly reduced, which further proves that loxl2 has high scientific research value in the basic research of lysyl oxidase family.
Fig. 1 Domain architecture of human full-length LOXL2 (774 aa). The schematic depicts N-terminal signal peptide, four SRCR substrate-recognition domains, and conserved C-terminal catalytic core. Post-translational modification sites including glycosylation are annotated.1
The biological functions of secreted LOXL2 oxidase protein are focused on sustained fibrous-substrate catalysis and extracellular-matrix network coordination:
Creative Biolabs offers purified LOXL2 recombinant protein samples produced under unified preparation workflows, including full-length LOXL2 constructs and isolated catalytic-domain variants. Truncated domain fragments cannot support complete fibrous-substrate catalysis behaviours, while full-length constructs suit research focused on extracellular matrix-substrate interaction and matrix-remodeling-related functional observation. All batches receive uniform quality screening. Functional relevant observation may only be carried out with full-length samples under simulated extracellular microenvironment setups. Consistent structural features are preserved across batches to support comparative laboratory analysis across separate test groups. Full-length LOXL2 samples retain intact copper-dependent catalytic-core conformation after standardized purification, which supports reliable detection of weak and transient enzyme-substrate contacts for comparative functional analysis.
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Creative Biolabs provides adjustable LOXL2 expression cell research models with varied expression levels, applicable to structural observation of secreted lysyl-oxidase family proteins and research into matrix-substrate molecular interaction. Sample evaluation includes sustained target expression detection and preliminary substrate-interaction observation, enabling side-by-side comparison of enzymatic catalytic behaviours under differing expression abundances. These cell systems can pair with diverse laboratory analysis schemes to track changes in substrate-processing efficiency alongside shifting target protein levels.
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Anti-LOXL2 recombinant antibodies are generated via standardized protein preparation workflows, compatible with routine laboratory detection techniques for extracellular-matrix localization mapping and identification of enzyme-substrate molecular complexes. The antibody series can work alongside common laboratory detection reagents to realize multi-dimensional observation of target distribution within connective-tissue related tissue samples.
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Beyond catalog products, Creative Biolabs offers specialized custom services for LOXL2 research:
LOXL2 might act as a secreted copper-dependent lysyl oxidase and participate in oxidative deamination of fibrous matrix substrates to modulate extracellular-matrix network maturation.
LOXL2 expression status could alter matrix-substrate catalysis efficiency and local extracellular-matrix structural balance, serving as a major regulatory mediator of connective-tissue remodeling biological processes.
No, all LOXL2 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 LOXL2 recombinant protein, target-specific recombinant antibodies and tunable expression cell research models, supporting research on extracellular matrix homeostasis and lysyl-oxidase-mediated fibrous-substrate processing.
Laboratory observation schemes may include enzyme-substrate interaction related tests to analyse catalytic-associated behaviors under simulated extracellular microenvironments.
