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The protein encoded by PLOD2 is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. Additionally we are shipping PLOD2 Antibodies (40) and PLOD2 Kits (4) and many more products for this protein.
Showing 6 out of 7 products:
The finding that LH2 modifies collagen in the extracellular space challenges the current view that LH2 functions solely on the endoplasmic reticulum and could also have important implications for cancer biology.
Authors propose that lysyl hydroxylase 2, and the subsequent increase in pyridinoline cross-links, is responsible for the persistent fibrosis in experimental osteoarthritis.
Lysyl hydroxylase-2b directs collagen cross-linking pathways through its action on telopeptidyl lysine residues.
LH2b (show LHX9 Proteins) catalyzes post-translational modification of collagen in collagen matrix formation and mineralization in bone.
analysis of the specific regulation for the expression of LH isoforms as well as for alternative splicing of LH2 during embryogenesis and in different tissues
TIA1 (show TIA1 Proteins) and TIAL1 (show TIAL1 Proteins) regulate the alternate splicing of lysyl hydroxylase 2
This study reports for the first time the expression of PLOD2 in Brain Arteriovenous Malformations and suggests a potential role of PLOD2 in brain Arteriovenous Malformations pathophysiology.
FKBP65 (show FKBP10 Proteins) is linked to pyridinoline cross-linking by specifically mediating the dimerization of LH2.
PLOD2, which is associated with the stiffness of the extracellular matrix, was directly regulated by miR (show MLXIP Proteins)-26a-5p and miR (show MLXIP Proteins)-26b-5p and may be a good prognostic marker in patients with BC
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 (show LOXL2 Proteins) and PLOD2, both of which function as oncogenes in this disease.
findings reveal that TGFbeta1 (show TGFB1 Proteins) induces a SP1 (show PSG1 Proteins)- and SMAD3 (show SMAD3 Proteins)-dependent recruitment of histone modifying enzymes to the PLOD2 promoter other than the currently known TGFbeta1 (show TGFB1 Proteins) downstream co-activators and epigenetic modifications
LH2 enhances the metastatic properties of tumor cells and functions as a regulatory switch that controls the relative abundance of biochemically distinct types of collagen cross-links in the tumor stroma.
TGFbeta (show TGFB1 Proteins) induced PLOD2/LH2 expression in human synovial osteoarthritic fibroblasts through ALK5 (show TGFBR1 Proteins) signaling.
data indicate that HIF-1alpha (show HIF1A Proteins) controls sarcoma metastasis through PLOD2-dependent collagen modification and organization in primary tumors
Infrapatellar fat pad (show PADI4 Proteins) contributeS to the development of synovial fibrosis in the knee joint by increasing collagen production, PLOD2 expression, cell proliferation, and cell migration.
The protein encoded by this gene is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. The enzyme (cofactors iron and ascorbate) catalyzes the hydroxylation of lysyl residues in collagen-like peptides. The resultant hydroxylysyl groups are attachment sites for carbohydrates in collagen and thus are critical for the stability of intermolecular crosslinks. Some patients with Ehlers-Danlos syndrome type VIB have deficiencies in lysyl hydroxylase activity. Mutations in the coding region of this gene are associated with Bruck syndrome. Alternative splicing results in multiple transcript variants encoding different isoforms.
lysyl hydroxylase 2
, procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
, Procollagen-lysine 2-oxoglutarate 5-dioxygenase (Lysine hydroxylase) 2
, Procollagen-lysine, 2-oxoglutarate 5-dioxygenase (Lysine hydroxylase) 2
, lysine hydroxylase 2
, lysyl hydroxlase 2
, telopeptide lysyl hydroxylase
, procollagen-lysine 2-oxoglutarate 5-dioxygenase 2