L4794

Anti-Lysyl Oxidase antibody produced in rabbit

Name: Anti-Lysyl Oxidase antibody produced in rabbit
Brand: SIGMA

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Lysyl Oxidase Antibody, Lysyl Oxidase Antibody - Anti-Lysyl Oxidase antibody produced in rabbit, Anti-LOX, Anti-Protein lysine 6-oxidase

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About This Item

NACRES:

NA.41

UNSPSC Code:

12352203

Product Name

Anti-Lysyl Oxidase antibody produced in rabbit, ~1 mg/mL, affinity isolated antibody, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

human

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1 mg/mL

technique(s)

western blot: 1.5-3.0 μg/mL using HEK-293T cells expressing human LOX

UniProt accession no.

P28300

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

Rabbit polyclonal anti-Lysyl Oxidase antibody specifically recognizes human lysyl oxidase (LOX). Detection of the LOX band by immunoblotting is specifically inhibited by the LOX immunizing peptide.

The gene LOX (lysyl oxidase) encodes an extracellular matrix remodeling enzyme that catalyzes the oxidation of primary amino group of peptidyl lysine to reactive peptidyl aldehydes. It is mainly involved in the oxidation of lysine residues in elastin and collagen, resulting in the formation of covalent cross-linkages, which stabilize these fibrous proteins. It also plays a role in several cellular processes such as developmental regulation, tumor suppression, cell motility, and cellular senescence. It is involved in hypoxia-induced metastasis and serves as a therapeutic target for the treatment of metastases.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

General description

The gene LOX (lysyl oxidase) encodes a copper-dependent amine oxidase that belongs to LOX family of proteins. These proteins contain highly conserved C- terminal mature catalytic domains that include the copper binding site, the lysyl tyrosyl quinine (LTQ) cofactor residues, and the cytokine receptor like (CRL) domain. It is present in both intercellular and intracellular locations.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

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Lysyl oxidase is downregulated by the EWS/FLI1 oncoprotein and its propeptide domain displays tumor supressor activities in Ewing sarcoma cells.

Noelia Agra et al.

PloS one, 8(6), e66281-e66281 (2013-06-12)

Ewing sarcoma is the second most common bone malignancy in children and young adults. It is driven by oncogenic fusion proteins (i.e. EWS/FLI1) acting as aberrant transcription factors that upregulate and downregulate target genes, leading to cellular transformation. Thus, identificating

Lysyl oxidase, extracellular matrix remodeling and cancer metastasis.

Xiao Q and Ge G

Cancer Microenvironment, 5, 261-273 (2012)

Lysyl oxidases: a novel multifunctional amine oxidase family.

Csiszar K

Prog. Nucleic Acids Res. Mol. Biol., 70, 1-32 (2001)

Lysyl oxidase is essential for hypoxia-induced metastasis.

Erler JT

Nature, 440, 1222-1226 (2006)

Lysyl oxidase: properties, specificity, and biological roles inside and outside of the cell.

Kagan HM and Li W

Journal of Cellular Biochemistry, 88, 660-672 (2003)

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