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The protein encoded by LOX is an extracellular copper enzyme that initiates the crosslinking of collagens and elastin. Additionally we are shipping LOX Kits (34) and LOX Proteins (15) and many more products for this protein.
Showing 10 out of 174 products:
Human Monoclonal LOX Primary Antibody for WB - ABIN1882261
Gao, Xiao, Ma, Li, Liu, Feng, Fang, Wu, Han, Zhang, Sun, Wu, Padera, Chen, Wong, Ge, Ji: LKB1 inhibits lung cancer progression through lysyl oxidase and extracellular matrix remodeling. in Proceedings of the National Academy of Sciences of the United States of America 2010
Show all 3 references for ABIN1882261
Human Monoclonal LOX Primary Antibody for WB - ABIN1882262
Santhanam, Baker, Hegamyer, Kirschmann, Colburn: Pdcd4 repression of lysyl oxidase inhibits hypoxia-induced breast cancer cell invasion. in Oncogene 2010
Show all 3 references for ABIN1882262
Human Polyclonal LOX Primary Antibody for EIA, FACS - ABIN953265
Mariani, Trackman, Kagan, Eddy, Shows, Boyd, Deak: The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene). in Matrix (Stuttgart, Germany) 1992
Partial knockdown of lysyl oxidase genes sensitizes the developing embryo to dithiocarbamate exposure.
Data reveal a role for lysyl oxidase in early morphogenesis, especially in muscle development and neurogenesis, and resume some aspects of physiopathology of copper metabolism.
LOX gene expression was approximately 2.5-fold higher in fetal membranes from preterm prelabor rupture of membranes (pPROM (show SERPINH1 Antibodies)) compared to preterm and term birth.
The data suggest a fibromodulin (show FMOD Antibodies)-modulated collagen cross-linking mechanism where fibromodulin (show FMOD Antibodies) binds to a specific part of the collagen domain and also forms a complex with lysyl oxidase, targeting the enzyme toward specific cross-linking sites.
Cu chaperone function of Atox1 (show ATOX1 Antibodies) mediated through Cu transporter ATP7A (show ATP7A Antibodies) is required for VEGF (show VEGFA Antibodies)-induced angiogenesis via activation of Cu enzyme lysyl oxidase.
Our study demonstrated that the LOX rs1800449 genotypes (AA and GA + AA) and allele (A) appears to confer risk for susceptibility to keratoconus.
Individuals with LOX variants had fusiform enlargement of the aortic root and ascending thoracic aorta, leading to ascending aortic dissections.
two LOX variants, rs2956540 and rs10519694, may affect individual susceptibility to keratoconus
LOX expression at the mRNA and protein level, and enzymatic activity were remarkably upregulated in the hypoxic A549 cells, compared with normoxic A549 cells.
Aortic tissue from Marfan syndrome patients and display enhanced expression of the members of the LOX family, LOX and LOX-like 1.
Evidence for association was found for both of the tested loci.It was strongest for rs3735520:G>A near HGF (show HGF Antibodies) with A allele being a risk factor and rs2956540:G>C within LOX with C allele having a protective effect
Using principal component analysis (PCA (show FLVCR1 Antibodies)), the authors identified a LOX/hypoxia signature associated with poor patient survival in resectable pancreatic ductal adenocarcinoma patients.
Statins normalize vascular lysyl oxidase (LOX) down-regulation induced by proatherogenic risk factors.
These results indicate that proLOX could be processed by two different mechanisms producing two forms of active LOX.
Lysyl oxidase enhances elastin (show ELN Antibodies) synthesis and matrix formation by vascular smooth muscle cells
Lysyl oxidase has a role in oxidizing basic fibroblast growth factor (show FGF2 Antibodies) and inactivating its mitogenic potential
In cases of vascular calcification, the decreased expression of LOX may be partially responsible for decreased vascular elasticity and also for the decreased formation of new elastic fibers.
Statins normalize vascular lysyl oxidase down-regulation induced by proatherogenic risk factors.
LOX family members contribute significantly to the detrimental effects of cardiac remodelling, highlighting LOX inhibition as a potential therapeutic strategy for post-infarction recovery
Findings suggest that the lysyl oxidase (LOX)-mediated organization of collagen fibers in the extracellular matrix is an important regulator of osteoblastogenesis.
Data suggest of pharmacologic targeting of lysyl oxidase (LOX) pathway to inhibit liver fibrosis and promote its resolution.
CTR1 (show SLC31A1 Antibodies), ATP7A (show ATP7A Antibodies), and lysyl oxidase were upregulated in the lung tissues and pulmonary arteries of mice with hypoxia-induced pulmonary hypertension and pulmonary arterial smooth muscle cells.
Inhibition of tissue transglutaminase (show TGM2 Antibodies) resulted in a reduced rate of compaction compared to controls during early remodeling (up to 2 days). In contrast, inhibition of lysyl oxidase did not alter the early compaction.
decreased expression of cross-linking enzymes (LOXs) and increased expression of ECM (show MMRN1 Antibodies)-degrading proteinases (MMP-1 (show MMP1 Antibodies), 2, 3) might be of great contribution to poor healing ability of PCL (show PKD2L1 Antibodies) ligament
LOX is indispensable for the progression of BLM-induced experimental lung fibrosis by aggravating the inflammatory response and subsequent fibrosis process after lung injury.
LOX and LOXL2 (show LOXL3 Antibodies) may play an important role in the pathogenesis of AMD (show AMD1 Antibodies). Targeting LOXL2 (show LOXL3 Antibodies) could have a broader efficacy than targeting LOX, by reducing angiogenesis and inflammation, as well as fibrosis.
The protein encoded by this gene is an extracellular copper enzyme that initiates the crosslinking of collagens and elastin. The enzyme catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. In addition to crosslinking extracellular matrix proteins, the encoded protein may have a role in tumor suppression. Defects in this gene are a cause of autosomal recessive cutis laxa type I (CL type I). Two transcript variants encoding different isoforms have been found for this gene.
, protein-lysine 6-oxidase-like
, protein-lysine 6-oxidase
, ras excision protein
, ras recision gene (rrg)
, Lysyl oxidase (an H-rev gene with its expression down-regulated in HRAS-transformed rat 208F fibroblasts)