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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 (194) and LOX Proteins (13) and many more products for this protein.
Showing 10 out of 45 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
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.
Results show that CTGF (show CTGF ELISA Kits) mediates the GDF8 (show MSTN ELISA Kits)-induced up-regulation of LOX expression and increases in LOX activity in human granulosa cells.
The LOXL1 (show LOXL1 ELISA Kits) SNPs, rs1048661 and rs3825942, are associated with PXF (show PEX19 ELISA Kits) in the South Indian population correlating with lowered LOX activity in the aqueous humor. The increased level of total TGF-beta (show TGFB1 ELISA Kits) in the aqueous humor of PXF (show PEX19 ELISA Kits) cases is possibly associated with LOX regulation which needs further investigation.
These findings suggest that LOX induces an age-dependent disturbance of diastolic function and aggravates Ang II (show AGT ELISA Kits)-induced hypertrophy, which provides novel insights into the role of LOX in cardiac performance.
LOX, a hypoxia-responsive gene that encodes lysyl oxidase, is activated by HIF-2-alpha (show EPAS1 ELISA Kits) more than HIF-1 (show HIF1A ELISA Kits). Two new hypoxia response elements identified in the LOX promoter mediate most HIF responsiveness.
our findings show that LOX supports colorectal cancer cell dissemination in the bone marrow
LOX G473A polymorphism apparently elevated human sensitivity to cigarette smoking carcinogens for eliciting cancers in the lung and colon only. Thus, LOX G473A polymorphism positively correlates with carcinogenesis and it may be used as an ideal intrinsic biomarker for prediction or diagnosis of carcinogenesis in humans.
increased cortisol and 11beta-HSD1 (show HSD11B1 ELISA Kits) abundance and decreased LOX abundance were observed in human amnion tissue after the labor-initiated spontaneous rupture of membranes
endogenous LOX is overexpressed in clear cell renal cell carcinoma, is involved in a positive-regulative loop with HIF-1alpha, and has a major action on clear cell renal cell carcinoma progression through cellular adhesion, migration, and collagen matrix stiffness increment
colorectal carcinoma perilesional extracellular matrix has increased content of lysyl oxidase
LOX affects the epithelial-mesenchymal transition of gastric cancer cells in hypoxic conditions.
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 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 data suggest a fibromodulin (show FMOD ELISA Kits)-modulated collagen cross-linking mechanism where fibromodulin (show FMOD ELISA Kits) 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.
Data suggest of pharmacologic targeting of lysyl oxidase (LOX) pathway to inhibit liver fibrosis and promote its resolution.
Cu chaperone function of Atox1 (show ATOX1 ELISA Kits) mediated through Cu transporter ATP7A (show ATP7A ELISA Kits) is required for VEGF (show VEGFA ELISA Kits)-induced angiogenesis via activation of Cu enzyme lysyl oxidase.
CTR1 (show SLC31A1 ELISA Kits), ATP7A (show ATP7A ELISA Kits), 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 ELISA Kits) 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.
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)