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Mouse Anti-LOXL2 Recombinant Antibody (5D2) (CBMAB-A5051-LY)

The product is antibody recognizes LOXL2. The antibody 5D2 immunoassay techniques such as: WB, ELISA.
See all LOXL2 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human
Clone
5D2
Antibody Isotype
IgG2b, κ
Application
WB, ELISA

Basic Information

Immunogen
LOXL2 (NP_002309, 675 a.a. ~ 773 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2b, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
lysyl oxidase-like 2
Introduction
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. [provided by RefSeq]
Entrez Gene ID
UniProt ID
Alternative Names
LOR2; WS9-14
Function
Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137).
Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (PubMed:27735137).
Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (PubMed:27735137).
Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (PubMed:25959397).
LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (By similarity).
Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3 (PubMed:16096638, PubMed:27735137, PubMed:24414204).
During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292).
SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292).
Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (PubMed:28332555).
Involved in E-cadherin repression following hypoxia, a hallmark of EMT believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression (PubMed:20026874).
When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:20306300).
Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952).
Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity).
Biological Process
AgingManual Assertion Based On ExperimentTAS:ProtInc
Cell adhesionManual Assertion Based On ExperimentTAS:ProtInc
Cellular protein modification processManual Assertion Based On ExperimentIDA:UniProtKB
Collagen fibril organizationManual Assertion Based On ExperimentIMP:UniProtKB
Endothelial cell migrationManual Assertion Based On ExperimentIMP:UniProtKB
Endothelial cell proliferationManual Assertion Based On ExperimentIMP:UniProtKB
Epithelial to mesenchymal transitionManual Assertion Based On ExperimentIDA:UniProtKB
Heterochromatin organizationManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of stem cell population maintenanceISS:UniProtKB
Negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:UniProtKB
Negative regulation of transcription, DNA-templatedManual Assertion Based On ExperimentIDA:UniProtKB
Peptidyl-lysine oxidationManual Assertion Based On ExperimentIDA:UniProtKB
Positive regulation of chondrocyte differentiationISS:UniProtKB
Positive regulation of epithelial to mesenchymal transitionManual Assertion Based On ExperimentIMP:UniProtKB
Response to copper ionManual Assertion Based On ExperimentIDA:UniProtKB
Response to hypoxiaISS:UniProtKB
Sprouting angiogenesisManual Assertion Based On ExperimentIMP:UniProtKB
Cellular Location
Secreted, extracellular space, extracellular matrix, basement membrane
Nucleus
Chromosome
Endoplasmic reticulum
Associated with chromatin (PubMed:27735137).
It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted (PubMed:23319596).
However, a number of reports confirm its intracellular location and its key role in transcription regulation (PubMed:22204712, PubMed:22483618).
PTM
The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.
N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core.

Cano, A., Eraso, P., Mazón, M. J., & Portillo, F. (2023). LOXL2 in Cancer: A Two-Decade Perspective. International Journal of Molecular Sciences, 24(18), 14405.

Lu, X., Xin, D. E., Du, J. K., Zou, Q. C., Wu, Q., Zhang, Y. S., ... & Chinn, Y. E. (2022). Loss of loxl2 promotes uterine hypertrophy and tumor progression by enhancing H3K36ac-dependent gene expression. Cancer Research, 82(23), 4400-4413.

Li, R., Li, H., Zhu, L., Zhang, X., Liu, D., Li, Q., ... & Jiang, S. H. (2021). Reciprocal regulation of LOXL2 and HIF1α drives the Warburg effect to support pancreatic cancer aggressiveness. Cell Death & Disease, 12(12), 1106.

Ferreira, S., Saraiva, N., Rijo, P., & Fernandes, A. S. (2021). LOXL2 inhibitors and breast cancer progression. Antioxidants, 10(2), 312.

Wu, S., Xing, X., Wang, Y., Zhang, X., Li, M., Wang, M., ... & Cui, J. (2021). The pathological significance of LOXL2 in pre-metastatic niche formation of HCC and its related molecular mechanism. European Journal of Cancer, 147, 63-73.

Wen, B., Xu, L. Y., & Li, E. M. (2020). LOXL2 in cancer: regulation, downstream effectors and novel roles. Biochimica et Biophysica Acta (BBA)-Reviews on Cancer, 1874(2), 188435.

Matsuoka, K., Bakiri, L., Wolff, L. I., Linder, M., Mikels-Vigdal, A., Patiño-García, A., ... & Wagner, E. F. (2020). Wnt signaling and Loxl2 promote aggressive osteosarcoma. Cell research, 30(10), 885-901.

Klepfish, M., Gross, T., Vugman, M., Afratis, N. A., Havusha-Laufer, S., Brazowski, E., ... & Sagi, I. (2020). LOXL2 inhibition paves the way for macrophage-mediated collagen degradation in liver fibrosis. Frontiers in Immunology, 11, 480.

Puente, A., Fortea, J. I., Cabezas, J., Arias Loste, M. T., Iruzubieta, P., Llerena, S., ... & Crespo, J. (2019). LOXL2—A new target in antifibrogenic therapy?. International journal of molecular sciences, 20(7), 1634.

Zhan, X. H., Jiao, J. W., Zhang, H. F., Xu, X. E., He, J. Z., Li, R. L., ... & Li, E. M. (2019). LOXL2 upregulates phosphorylation of ezrin to promote cytoskeletal reorganization and tumor cell invasion. Cancer Research, 79(19), 4951-4964.

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For research use only. Not intended for any clinical use.

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