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The protein encoded by PLOD3 is a membrane-bound homodimeric enzyme that is localized to the cisternae of the rough endoplasmic reticulum. Additionally we are shipping PLOD3 Antibodies (52) and PLOD3 Proteins (5) and many more products for this protein.
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LH3 directs target-selective motor axon regeneration.
Together these data suggest that Lh3-Collagen18A1 dependent ECM (show MMRN1 ELISA Kits) modifications regulate the transition of trunk neural crest cells from a non-segmental sheet like migration mode to a segmental stream migration mode
diwanka (lh3) acts through myotomal type XVIII collagen, a ligand for neural-receptor protein tyrosine phosphatases that guide motor axons
Data indicate that lysyl hydroxylase 3 is essential for the glucosyltion of mannan-binding lectin MBL (show MBL2 ELISA Kits)-A (show Mbl1 ELISA Kits).
LH3 is an important regulator of adiponectin biosynthesis, secretion and activity.
LH3-mediated glucosylation occurs at the specific molecular loci in the type I collagen molecule and plays critical roles in controlling collagen cross-linking, fibrillogenesis, and mineralization.
the major function of LH3 in osteoblasts is to glucosylate galactosylhydroxylysine residues in type I collagen and that an impairment of this LH3 function significantly affects type I collagen fibrillogenesis.
results demonstrate that LH3 is indispensable for biosynthesis of type IV collagen (show COL4 ELISA Kits) and for basement membrane stability during early development and that loss of LH3's functions leads to embryonic lethality
LH3 is present and active in the extracellular space
LH3 has lysyl hydroxylase and galactosylhydroxylysyl glucosyltransferase T activities in vivo, and is essential for the formation of the basement membrane
Results report an important role for lysyl hydroxylase 3 in the organization of the extracellular matrix (ECM (show MMRN1 ELISA Kits)) and cytoskeleton.
VIPAR, with its partner proteins, regulate sorting of lysyl hydroxylase 3 (LH3, also known as PLOD3) into newly identified post-Golgi collagen IV (show COL4 ELISA Kits) carriers
Proteomic analysis revealed that PLOD3, which is the gene encoding for collagen-modifying lysyl hydroxylase 3 (LH3), is regulated by miR (show MLXIP ELISA Kits)-663a.
The study shows that lysyl hydroxylase 3 localizes to epidermal basement membrane and is reduced in patients with recessive dystrophic epidermolysis bullosa.
MMP-9 (show MMP9 ELISA Kits) recruitment to the fibroblast cell surface by Lysyl Hydroxylase 3 (LH3) triggers TGF-beta (show TGFB1 ELISA Kits) activation and fibroblast differentiation
LH3 molecules found in the cell medium are secreted through the Golgi complex, and the secretion is dependent on LH3 glycosyltransferase activity; LH3 found on the cell surface bypasses the Golgi complex
Dimerization of human lysyl hydroxylase 3 is mediated by the amino acids 541-547
Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity
Manipulation of the gene for LH3 can be used to selectively alter glycosylation and hydroxylation reactions, and provides new tool to clarify functions of unique hydroxylysine linked carbohydrates in collagens and other proteins.
The deficiency of LH3 glycosyltransferase activities, especially in the extracellular space, causes growth arrest.
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.
procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3
, procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
, procollagen-lysine,2-oxoglutarate 5-dioxygenase 3-like
, lysyl hydroxylase 2
, lysyl hydroxylase 3
, bone protein I (BP-I)
, lysine hydroxylase 3
, lysyl hydroxlase 3