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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 Kits (45) 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.
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.
The LOXL1 (show LOXL1 Proteins) SNPs, rs1048661 and rs3825942, are associated with PXF (show PEX19 Proteins) in the South Indian population correlating with lowered LOX activity in the aqueous humor. The increased level of total TGF-beta (show TGFB1 Proteins) in the aqueous humor of PXF (show PEX19 Proteins) 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 Proteins)-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 Proteins) more than HIF-1 (show HIF1A Proteins). 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 Proteins) 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 (show MOK Proteins), is involved in a positive-regulative loop with HIF-1alpha (show HIF1A Proteins), and has a major action on clear cell renal cell carcinoma (show MOK Proteins) progression through cellular adhesion, migration, and collagen matrix stiffness increment
colorectal carcinoma perilesional extracellular matrix has increased content of lysyl oxidase
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.
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.
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 Proteins) mediated through Cu transporter ATP7A (show ATP7A Proteins) is required for VEGF (show VEGFA Proteins)-induced angiogenesis via activation of Cu enzyme lysyl oxidase.
CTR1 (show SLC31A1 Proteins), ATP7A (show ATP7A Proteins), 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.
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)