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Mouse Anti-LOX Recombinant Antibody (9G2) (CBMAB-L1929-YJ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
9G2
Antibody Isotype
IgG1
Application
FC, IHC, WB

Basic Information

Immunogen
LOX antibody was raised in mouse using a human recombinant protein fragment corresponding to amino acids 22-168 of human LOX (NP_002308) produced in HEK293T cells, as the immunogen.
Specificity
Human
Antibody Isotype
IgG1
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!]

Buffer
PBS, pH 7.3, 1% BSA, 50% Glycerol
Preservative
0.02% Sodium Azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 22-168

Target

Full Name
lysyl oxidase
Introduction
LOX is a member of the lysyl oxidase family of proteins. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate a regulatory propeptide and the mature enzyme. The copper-dependent amine oxidase activity of this enzyme plays a role in the crosslinking of collagens and elastin, while the propeptide may play a role in tumor suppression. In addition, defects in this gene have been linked with predisposition to thoracic aortic aneurysms and dissections.
Entrez Gene ID
4015
UniProt ID
P28300
Alternative Names
AAT10; protein-lysine 6-oxidase; EC 1.4.3.13
Function
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787).
Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity).
Biological Process
Ascending aorta developmentIEA:Ensembl
Blood vessel morphogenesisISS:UniProtKB
Bone mineralizationIEA:Ensembl
Cell chemotaxisIEA:Ensembl
Cellular protein modification processManual Assertion Based On ExperimentTAS:ProtInc
Cellular response to chemokineIEA:Ensembl
Collagen fibril organizationManual Assertion Based On ExperimentIBA:GO_Central
Connective tissue developmentIEA:Ensembl
Descending aorta developmentIEA:Ensembl
DNA biosynthetic processIEA:Ensembl
Elastic fiber assemblyIEA:Ensembl
Heart developmentIEA:Ensembl
Lung developmentIEA:Ensembl
Muscle cell cellular homeostasisIEA:Ensembl
Muscle cell developmentIEA:Ensembl
Osteoblast differentiationIEA:Ensembl
Peptidyl-lysine oxidationManual Assertion Based On ExperimentIDA:UniProtKB
Platelet-derived growth factor receptor-beta signaling pathwayIEA:Ensembl
Protein kinase B signalingIEA:Ensembl
Regulation of apoptotic processIEA:Ensembl
Regulation of bone developmentIEA:Ensembl
Regulation of gene expressionIEA:Ensembl
Regulation of megakaryocyte differentiationIEA:Ensembl
Regulation of platelet-derived growth factor receptor-beta signaling pathwayIEA:Ensembl
Regulation of protein phosphorylationIEA:Ensembl
Regulation of receptor bindingIEA:Ensembl
Regulation of striated muscle tissue developmentIEA:Ensembl
Regulation of transforming growth factor beta receptor signaling pathwayIEA:Ensembl
Response to steroid hormoneIEA:Ensembl
Response to xenobiotic stimulusIEA:Ensembl
Wound healingIEA:Ensembl
Cellular Location
Secreted
Secreted, extracellular space
Involvement in disease
Aortic aneurysm, familial thoracic 10 (AAT10):
A form of thoracic aortic aneurysm, a disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
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.
Proteolytically cleaved by BMP1 which removes the propeptide (PubMed:31152061).
Also proteolytically cleaved by ADAMTS2 and ADAMTS14, but not by ADAMTS3, at an additional cleavage site downstream of the BMP1 cleavage site (PubMed:31152061).
The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin (By similarity).
Cleavage by BMP1 to remove the propeptide does not increase enzymatic activity but increases binding to collagen (PubMed:31152061).
Cleavage by ADAMTS2 produces a form with reduced collagen-binding activity (PubMed:31152061).By Similarity1 Publication
Sulfated at Tyr-187 and also at either Tyr-183 or Tyr-184 which enhances binding to collagen.
More Infomation

Ye, M., Zhou, J., Gao, Y., Pan, S., & Zhu, X. (2020). The prognostic value of the lysyl oxidase family in ovarian cancer. Journal of Clinical Laboratory Analysis, 34(12), e23538.

Saatci, O., Kaymak, A., Raza, U., Ersan, P. G., Akbulut, O., Banister, C. E., ... & Sahin, O. (2020). Targeting lysyl oxidase (LOX) overcomes chemotherapy resistance in triple negative breast cancer. Nature communications, 11(1), 2416.

Wei, S., Gao, L., Wu, C., Qin, F., & Yuan, J. (2020). Role of the lysyl oxidase family in organ development. Experimental and Therapeutic Medicine, 20(1), 163-172.

Laczko, R., & Csiszar, K. (2020). Lysyl oxidase (LOX): functional contributions to signaling pathways. Biomolecules, 10(8), 1093.

Chen, W., Yang, A., Jia, J., Popov, Y. V., Schuppan, D., & You, H. (2020). Lysyl oxidase (LOX) family members: rationale and their potential as therapeutic targets for liver fibrosis. Hepatology, 72(2), 729-741.

Vallet, S. D., & Ricard-Blum, S. (2019). Lysyl oxidases: from enzyme activity to extracellular matrix cross-links. Essays in biochemistry, 63(3), 349-364.

Al-u’datt, D. A., Allen, B. G., & Nattel, S. (2019). Role of the lysyl oxidase enzyme family in cardiac function and disease. Cardiovascular Research, 115(13), 1820-1837.

Rodríguez, C., & Martínez-González, J. (2019). The role of lysyl oxidase enzymes in cardiac function and remodeling. Cells, 8(12), 1483.

Vallet, S. D., Guéroult, M., Belloy, N., Dauchez, M., & Ricard-Blum, S. (2019). A three-dimensional model of human lysyl oxidase, a cross-linking enzyme. ACS omega, 4(5), 8495-8505.

Leung, L., Niculescu-Duvaz, D., Smithen, D., Lopes, F., Callens, C., McLeary, R., ... & Springer, C. (2019). Anti-metastatic inhibitors of lysyl oxidase (LOX): design and structure–activity relationships. Journal of medicinal chemistry, 62(12), 5863-5884.

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

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