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Lysyl hydroxylase is a membrane-bound homodimeric protein localized to the cisternae of the endoplasmic reticulum. Additionally we are shipping Procollagen-Lysine,2-Oxoglutarate 5-Dioxygenase 1 Kits (18) and Procollagen-Lysine,2-Oxoglutarate 5-Dioxygenase 1 Proteins (6) and many more products for this protein.
Showing 10 out of 28 products:
Human Polyclonal PLOD1 Primary Antibody for FACS, IHC (p) - ABIN656585
Wågsäter, Paloschi, Hanemaaijer, Hultenby, Bank, Franco-Cereceda, Lindeman, Eriksson: Impaired collagen biosynthesis and cross-linking in aorta of patients with bicuspid aortic valve. in Journal of the American Heart Association 2013
Human Polyclonal PLOD1 Primary Antibody for IHC, IHC (p) - ABIN4346298
Heard, Besio, Weis, Rai, Hudson, Dimori, Zimmerman, Kamykowski, Hogue, Swain, Burdine, Mackintosh, Tackett, Suva, Eyre, Morello: Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation. in PLoS genetics 2016
Data show that homozygous and compound heterozygous changes found in PLOD1 and SLC2A10 (show SLC2A10 Antibodies) may confer autosomal recessive effects, and three MYH11 (show MYH11 Antibodies), ACTA2 (show ACTA2 Antibodies) and COL3A1 (show COL3A1 Antibodies) heterozygous variants were considered as putative pathogenic gene alterations.
Common polymorphisms in four candidate genes (COL11A1 (show COL11A1 Antibodies), COL18A1 (show COL18A1 Antibodies), FBN1 (show FBN1 Antibodies) and PLOD1) were unlikely to play important roles in the genetic susceptibility to high myopia.
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
Results indicate that a C-terminal 40 amino acid segment of lysyl hydroxylase confers endoplasmic reticulum residency in a KDEL-receptor (show KDELR Antibodies)-independent manner.
Lysyl hydroxylase is a membrane-bound homodimeric protein localized to the cisternae of the 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 VI have deficiencies in lysyl hydroxylase activity.
, lysyl hydroxylase 1
, procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase 1
, procollagen-lysine 2-oxoglutarate 5-dioxygenase (lysine hydroxylase Ehlers-Danlos syndrome type VI)
, procollagen-lysine, 2-oxoglutarate 5-dioxygenase (lysine hydroxylase, Ehlers-Danlos syndrome type VI)
, procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
, lysine hydroxylase
, lysyl hydroxlase 1
, 2-oxoglutarate 5-dioxygenase 1
, procollagen-lysine 5-dioxygenase
, procollagen-lysine 2-oxoglutarate 5-dioxygenase 1