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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 (190) and LOX Proteins (17) and many more products for this protein.
Showing 10 out of 54 products:
Human LOX ELISA Kit for Sandwich ELISA - ABIN418267
Tadmor, Bejar, Attias, Mischenko, Sabo, Neufeld, Vadasz: The expression of lysyl-oxidase gene family members in myeloproliferative neoplasms. in American journal of hematology 2013
Show all 7 Pubmed References
Mouse (Murine) LOX ELISA Kit for Sandwich ELISA - ABIN425766
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
Show all 2 Pubmed References
Rat (Rattus) LOX ELISA Kit for Sandwich ELISA - ABIN432937
Wang, Wan, Li, Zhang, Wan, Ji, Li, Liu, Han: Lysyl oxidase is involved in synovial hyperplasia and angiogenesis in rats with collagen‑induced arthritis. in Molecular medicine reports 2017
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.
Our results indicate the involvement of LOX in the initiation of fibrous capsule formation which ultimately contributes towards the progression of capsular contracture
this study has revealed that IL-1beta (show IL1B ELISA Kits) may contribute to the rupture of fetal membranes by attenuating collagen crosslinking through downregulation of LOX expression in amnion fibroblasts
This study focused on the relationship between lysyl oxidase (LOX), LOX-like protein 1 (LOXL1 (show LOXL1 ELISA Kits)), and LOXL2 (show LOXL2 ELISA Kits) and pulmonary emphysema pathogenesis.
The aim was to examine if the serum concentrations of elastin (show ELN ELISA Kits)-related proteins correlate to signs of cardiovascular diseases in patients with Diabetes mellitus type 2.
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 ELISA Kits)+-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 ELISA Kits).
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 ELISA Kits) secretion plays a role in cancer progression.
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 ELISA Kits) synthesis and matrix formation by vascular smooth muscle cells
Lysyl oxidase has a role in oxidizing basic fibroblast growth factor (show FGF2 ELISA Kits) 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 over-expression in vascular smooth muscle cells was associated with a change in the structure of collagen and elastin (show ELN ELISA Kits) fibres; LOX could constitute a novel source of oxidative stress that might participate in elastin (show ELN ELISA Kits) changes and contribute to vascular remodelling
LOX up-regulation is associated with enhanced oxidative stress that promotes p38MAPK (show MAPK14 ELISA Kits) activation, elastin (show ELN ELISA Kits) structural alterations, and vascular stiffness.
These results suggest that LOX has the ability to induce RANKL (show TNFSF11 ELISA Kits) expression on stromal cells; however, it fails to substitute for RANKL (show TNFSF11 ELISA Kits) in osteoclastogenesis.
UXT Is a LOX-PP Interacting Protein That Modulates Estrogen Receptor Alpha (show ESR1 ELISA Kits) Activity in Breast Cancer Cells.
Data show that LOX-PP enhances adipogenesis at least partially through inhibition of FGF-2 (show FGF2 ELISA Kits) 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 ELISA Kits) 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 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)