LOXL3 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
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Primary Accession | P58215 |
Other Accession | Q9Z175, NP_115992.1 |
Reactivity | Human |
Predicted | Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 83166 Da |
Antigen Region | 715-744 aa |
Gene ID | 84695 |
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Other Names | Lysyl oxidase homolog 3, 143-, Lysyl oxidase-like protein 3, LOXL3, LOXL |
Target/Specificity | This LOXL3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 715-744 amino acids from the C-terminal region of human LOXL3. |
Dilution | WB~~1:2000 IHC-P~~1:10~50 |
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 | LOXL3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | LOXL3 {ECO:0000303|PubMed:11386757, ECO:0000312|HGNC:HGNC:13869} |
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Function | Protein-lysine 6-oxidase that mediates the oxidation of peptidyl lysine residues to allysine in target proteins (PubMed:17018530, PubMed:28065600). Catalyzes the post-translational oxidative deamination of peptidyl lysine residues in precursors of elastin and different types of collagens, a prerequisite in the formation of cross-links between collagens and elastin (PubMed:17018530). Required for somite boundary formation by catalyzing oxidation of fibronectin (FN1), enhancing integrin signaling in myofibers and their adhesion to the myotendinous junction (MTJ) (By similarity). Acts as a regulator of inflammatory response by inhibiting differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acts by interacting with STAT3 in the nucleus and catalyzing both deacetylation and oxidation of lysine residues on STAT3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). Also able to catalyze deacetylation of lysine residues on STAT3 (PubMed:28065600). |
Cellular Location | Secreted, extracellular space {ECO:0000250|UniProtKB:Q9Z175}. Cytoplasm. Nucleus Note=It is unclear how LOXL3 is both intracellular (cytoplasmic and nuclear) and extracellular: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, the intracellular location is clearly reported and at least another protein of the family (LOXL2) also has intracellular and extracellular localization despite the presence of a signal sequence (PubMed:28065600). [Isoform 2]: Cytoplasm. Secreted, extracellular space |
Tissue Location | Isoform 1: Predominantly detected in the heart, placenta, lung, and small intestine (PubMed:17018530). Isoform 2: Highly detected in the kidney, pancreas, spleen, and thymus, and is absent in lung (PubMed:17018530). In eye, present in all layers of corneas as well as in the limbus and conjunctiva (at protein level) (PubMed:26218558). |
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Background
This gene encodes a member of the lysyl oxidase gene family. The prototypic member of the family is essential to the biogenesis of connective tissue, encoding an extracellular copper-dependent amine oxidase that catalyses the first step in the formation of crosslinks in collagens and elastin. A highly conserved amino acid sequence at the C-terminus end appears to be sufficient for amine oxidase activity, suggesting that each family member may retain this function. The N-terminus is poorly conserved and may impart additional roles in developmental regulation, senescence, tumor suppression, cell growth control, and chemotaxis to each member of the family. Alternatively spliced transcript variants of this gene have been reported but their full-length nature has not been determined.
References
Kim, Y., et al. Oncol. Rep. 22(4):799-804(2009)
Sebban, S., et al. Virchows Arch. 454(1):71-79(2009)
Akagawa, H., et al. Hum. Genet. 121 (3-4), 377-387 (2007) :
Lee, J.E., et al. J. Biol. Chem. 281(49):37282-37290(2006)
Peinado, H., et al. EMBO J. 24(19):3446-3458(2005)
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