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LOXL2 encodes a member of the lysyl oxidase gene family. Additionally we are shipping Lysyl Oxidase-Like 2 Antibodies (102) and Lysyl Oxidase-Like 2 Kits (23) and many more products for this protein.
Showing 10 out of 28 products:
Dmloxl-1 and Dmloxl-2 are differentially expressed; active DmLOXL-1 influences gene expression and development
Results showed that LOXL2 was overexpressed in head and neck squamous cell carcinoma clinical specimens and that silencing of the LOXL2 gene significantly inhibited the migration and invasion of cancer cells.
ECM (show MMRN1 Proteins) crosslinking by EC-derived exosomes is mediated by LOXL2.
Results show that miR (show MLXIP Proteins)-26a and miR (show MLXIP Proteins)-26b were significantly downregulated in renal cell carcinoma (show MOK Proteins) clinical specimens and appeared to function as tumor suppressors through regulation of collagen cross-linking enzymes, LOXL2 and PLOD2 (show PLOD2 Proteins), both of which function as oncogenes in this disease.
Loss of tumor-suppressive miR29s enhanced cancer cell invasion in lung SCC (show CYP11A1 Proteins) through direct regulation of oncogenic LOXL2.
LOXL2 promotes tumor progression.
We identified LOXL2 to be associated with the outcome of colon cancer patients. Furthermore, it can be used to stratify patients at stages II and III for further therapeutic decisions.
Data suggest that restoration of MIRN29 (microRNA 29) synthesis silences expression of LOXL2 (lysyl oxidase-like 2) and inhibits cell proliferation, migration, and invasiveness of renal cell carcinoma (show MOK Proteins) cells.
Lysine oxidation of the transcription factor TAF10 (show TAF10 Proteins) by LOXL2 is a controlled protein modification and demonstrates a role for protein oxidation in regulating pluripotency genes.
Results show that LOXL2 is highly expressed and involved in clear cell renal cell carcinoma (show MOK Proteins) progression by regulating the levels of integrins a5 and b1.
identified novel alternative splicing isoform, LOXL2 Deltae13; data suggest it modulates effects of cancer cell migration and invasion through a different mechanism from full-length LOXL2 and may play an important role in tumor carcinogenesis and progression
LOX (show LOX Proteins) and LOXL2 (show LOXL3 Proteins) may play an important role in the pathogenesis of AMD (show AMD1 Proteins). Targeting LOXL2 (show LOXL3 Proteins) could have a broader efficacy than targeting LOX (show LOX Proteins), by reducing angiogenesis and inflammation, as well as fibrosis.
Loss and gain of function analyses combined with in vivo studies in syngeneic breast cancer models demonstrate the participation of LOXL2 (show LOXL3 Proteins) and E47 (show TCF3 Proteins) in tumor growth and their requirement for lung metastasis.
Findings reveal new insight into the mechanisms of fibroblast activation, a novel function of LOXL2 (show LOXL3 Proteins), and further highlight the importance of generating LOXL2 (show LOXL3 Proteins)-targeted therapies for the prevention of tumor progression and metastasis.
The Snail1 (show SNAI1 Proteins) transcription factor represses mouse pericentromeric transcription, acting through the H3K4 deaminase LOXL2 (show LOXL3 Proteins).
The enzymatic activity of lysyl oxidas-like-2 (LOXL2 (show LOXL3 Proteins)) is not required for LOXL2 (show LOXL3 Proteins)-induced inhibition of keratinocyte differentiation.
This study provides the first evidence for the role of LOXL2 (show LOXL3 Proteins) in regulating angiogenesis through collagen IV (show COL4 Proteins) scaffolding.
LOXL2 (show LOXL3 Proteins) promotes chondrocyte differentiation by mechanisms that are likely to include roles as both a regulator and an effector of chondrocyte differentiation
The efficacy and safety of LOXL2 (show LOXL3 Proteins)-specific monoclonal antibody represents a new therapeutic approach with broad applicability in oncologic and fibrotic diseases.
LoxL2 (show LOXL3 Proteins) is not expressed in MC3T3-E1 cells.
This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family.
, lysyl oxidase-like 2
, Lysyl oxidase-like protein 2
, lysyl oxidase homolog 2
, lysyl oxidase homolog 2-like
, lysyl oxidase related 2
, lysyl oxidase-like protein 2
, lysyl oxidase-related protein 2
, lysyl oxidase-related protein WS9-14
, Lysyl oxidase homolog 2