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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 Antibodies (179) and LOX Kits (47) and many more products for this protein.
Showing 10 out of 14 products:
Human LOX Protein expressed in HEK-293 Cells - ABIN2712316
Baker, Bird, Welti, Gourlaouen, Lang, Murray, Reynolds, Cox, Erler: Lysyl oxidase plays a critical role in endothelial cell stimulation to drive tumor angiogenesis. in Cancer research 2013
Show all 5 Pubmed References
Mouse (Murine) LOX Protein expressed in Escherichia coli (E. coli) - ABIN2123209
Tsukasaki, Hamada, Okamoto, Nagashima, Terashima, Komatsu, Win, Okamura, Nitta, Yasuda, Penninger, Takayanagi: LOX Fails to Substitute for RANKL in Osteoclastogenesis. in Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research 2016
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 role in cancer stromal cells activation and promotion of gastric cancer progression
an association of LOX gene polymorphism (G473A) on diabetes and DFU patients
LOX expression was mildly but significantly upregulated in CD34 (show CD34 Proteins)+-derived primary myelofibrosis megakaryocytes and platelets compared with controls. These megakaryocytes showed a greater tendency to adhere and spread to monomeric collagen, and this was inhibited by the LOX-specific inhibitor BAPN (show ANPEP Proteins).
Data suggest that a missense mutation in lysyl oxidase (LOX) is associated with aortic disease.
Our findings suggest that LOX has a role in cancer cell mitosis
Our findings provide new evidence that LOX regulates SNAI2 expression and that SNAI2-mediated TIMP4 (show TIMP4 Proteins) secretion plays a role in cancer progression.
UXT (show UXT Proteins) Is a LOX-PP Interacting Protein That Modulates Estrogen Receptor Alpha (show ESR1 Proteins) Activity in Breast Cancer Cells.
LOX is a prognostic factor for poor progression free survival in patients with ER- breast cancer. LOX overexpression was positively correlated with resistance to radiation and drug therapy.
This preliminary study indicated that LOX gene polymorphisms, such as rs2303656, rs3900446, and rs763497, may play crucial roles in intracranial aneurysm formation in the Korean population.
Results show that CTGF (show CTGF Proteins) mediates the GDF8 (show MSTN Proteins)-induced up-regulation of LOX expression and increases in LOX activity in human granulosa cells.
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 Proteins) synthesis and matrix formation by vascular smooth muscle cells
Lysyl oxidase has a role in oxidizing basic fibroblast growth factor (show FGF2 Proteins) 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 up-regulation is associated with enhanced oxidative stress that promotes p38MAPK (show MAPK14 Proteins) activation, elastin (show ELN Proteins) structural alterations, and vascular stiffness.
These results suggest that LOX has the ability to induce RANKL (show TNFSF11 Proteins) expression on stromal cells; however, it fails to substitute for RANKL (show TNFSF11 Proteins) in osteoclastogenesis.
Data show that LOX-PP enhances adipogenesis at least partially through inhibition of FGF-2 (show FGF2 Proteins) receptor signaling.
LOX targeting reduces peritoneal fibrosis.
Absence of lysyl oxidase (Lox) causes thoracic aortic aneurysms. The aortic mechanical behavior of Lox(-/-) mice is consistent with reduced elastin (show ELN Proteins) and collagen cross-linking but demonstrates vascular location-specific differences. Lox(-/-) aortas show upregulation of matrix remodeling genes and location-specific differential expression of other matrix and smooth muscle cell gene sets.
Findings from this study indicate that preventing LOX overexpression may be protective against high glucose-induced apoptosis in retinal vascular cells associated with diabetic retinopathy.
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.
The data suggest a fibromodulin (show FMOD Proteins)-modulated collagen cross-linking mechanism where fibromodulin (show FMOD Proteins) 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.
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)