PLOD1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 3
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, FC, E |
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Primary Accession | Q02809 |
Other Accession | Q9R0E2, NP_000293.2 |
Reactivity | Human |
Predicted | Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 83550 Da |
Antigen Region | 66-94 aa |
Gene ID | 5351 |
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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. |
Dilution | WB~~1:1000-1:2000 IHC-P~~1:25 FC~~1:25 |
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. |
Name | PLOD1 |
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Synonyms | LLH, PLOD |
Function | Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys- Gly- sequences in collagens (PubMed:10686424, PubMed:15854030, PubMed:8621606). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable). |
Cellular Location | Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side |
Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
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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