PLOD3 Antibody (N-term) 精选
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
- 背景知识
Application
| WB, E |
|---|---|
| Primary Accession | O60568 |
| Other Accession | NP_001075.1 |
| Reactivity | Human |
| Predicted | Mouse, Rat, Bovine, Canine, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 84785 Da |
| Antigen Region | 78-105 aa |
| Gene ID | 8985 |
|---|---|
| Other Names | Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3, Lysyl hydroxylase 3, LH3, PLOD3 |
| Target/Specificity | This PLOD3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 78-105 amino acids from the N-terminal region of human PLOD3. |
| Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
| 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 | PLOD3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | PLOD3 |
|---|---|
| Function | Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812, PubMed:9582318, PubMed:9724729). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues (PubMed:10934207, PubMed:11896059, PubMed:11956192, PubMed:12475640, PubMed:18298658, PubMed:18834968, PubMed:30089812). Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen- like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5- hydroxylysine residues (PubMed:25419660). Essential for normal biosynthesis and secretion of type IV collagens (Probable) (PubMed:18834968). Essential for normal formation of basement membranes (By similarity). |
| Cellular Location | Rough endoplasmic reticulum. Endoplasmic reticulum lumen. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R0E1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R0E1}; Lumenal side {ECO:0000250|UniProtKB:Q9R0E1}. Secreted Secreted, extracellular space {ECO:0000250|UniProtKB:Q9R0E1}. Note=The majority of the secreted protein is associated with the extracellular matrix. {ECO:0000250|UniProtKB:Q9R0E1} |
| Tissue Location | Ubiquitous (PubMed:9724729). Detected in heart, placenta and pancreas and at lower levels in lung, liver and skeletal muscle (PubMed:9582318, PubMed:9724729). |
Provided below are standard protocols that you may find useful for product applications.
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.
REFERENCES
Wang, C., et al. J. Cell. Mol. Med. 13(3):508-521(2009)
Salo, A.M., et al. Am. J. Hum. Genet. 83(4):495-503(2008)
Salo, A.M., et al. J. Cell. Physiol. 207(3):644-653(2006)
Wang, C., et al. Matrix Biol. 21(7):559-566(2002)
Rautavuoma, K., et al. J. Biol. Chem. 277(25):23084-23091(2002)
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