|Application ||WB, FC|
|Other Accession||Q9R0E2, NP_000293.2|
|Calculated MW||H=84,88;M=84;R=84 KDa|
|Antigen Region||66-94 aa|
|Other Names||Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1, Lysyl hydroxylase 1, LH1, PLOD1, LLH, PLOD|
|Target/Specificity||This PLOD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 66-94 amino acids from the N-terminal region of human PLOD1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PLOD1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.|
|Cellular Location||Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side|
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Provided below are standard protocols that you may find useful for product applications.
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.
Johnatty, S.E., et al. PLoS Genet. 6 (7), E1001016 (2010) :
Huang, Q.Y., et al. Bone 44(5):984-988(2009)
Yamada, Y., et al. Int. J. Mol. Med. 19(5):791-801(2007)
Tasker, P.N., et al. Osteoporos Int 17(7):1078-1085(2006)
Giunta, C., et al. Mol. Genet. Metab. 86 (1-2), 269-276 (2005) :
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