Rabbit anti-Human PLOD3 Polyclonal Antibody

Uniprot Id

O60568

Target Species

Human

Target Name

PLOD3

Target Full Name

Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3

Target Function

Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine. Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes.

Target Involvement

Lysyl hydroxylase 3 deficiency (LH3 deficiency)

Target Subcellular Location

Rough endoplasmic reticulum. Endoplasmic reticulum lumen. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Secreted. Secreted, extracellular space.

Target Tissue Specificity

Ubiquitous. Detected in heart, placenta and pancreas and at lower levels in lung, liver and skeletal muscle.

Target Research Area

Others

Target Synonyms

2-oxoglutarate 5-dioxygenase 3; bone protein I; BP-I; LH3; Lysine hydroxylase 3; Lysyl hydroxylase 3; Plod3; PLOD3_HUMAN; Procollagen lysine,2 oxoglutarate 5 dioxygenase 3 precursor; Procollagen-lysine

Target Background

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.