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L4794

Sigma-Aldrich

Anti-Lysyl Oxidase antibody produced in rabbit

enhanced validation

~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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

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.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... LOX(4015)
mouse ... Lox(16948) , Lox(24914)

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.

Specificity

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.

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

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.

Physical form

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

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.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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 oxidases: a novel multifunctional amine oxidase family.
Csiszar K
Prog. Nucleic Acids Res. Mol. Biol., 70, 1-32 (2001)
Lysyl oxidase, extracellular matrix remodeling and cancer metastasis.
Xiao Q and Ge G
Cancer Microenvironment, 5, 261-273 (2012)
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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