LOX Protein (Myc-DYKDDDDK Tag)

N° du produit ABIN2712316

Détail du produit

Antigène: LOX (Lysyl Oxidase (LOX))

Type de proteíne: Recombinant

Origine: Humain

Source: HEK-293 Cells

Purification/Conjugué: Cette LOX protéine est marqué à la Myc-DYKDDDDK Tag.

Application: Antibody Production (AbP), Standard (STD)

Attributs du produit:

• Recombinant human Lysyl oxidase protein expressed in HEK293 cells.
• Produced with end-sequenced ORF clone

Pureté: > 80 % as determined by SDS-PAGE and Coomassie blue staining

Information d'application

Indications d'application: Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays

Commentaires:

The tag is located at the C-terminal.

Restrictions: For Research Use only

Stockage

Concentration: 50 μg/mL

Buffer: 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10 % glycerol.

Stock: -80 °C

Stockage commentaire: Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.

Référence

Pilecki, Holm, Schlosser, Moeller, Wohl, Zuk, Heumüller, Wallis, Moestrup, Sengle, Holmskov, Sorensen: "Characterization of Microfibrillar-associated Protein 4 (MFAP4) as a Tropoelastin- and Fibrillin-binding Protein Involved in Elastic Fiber Formation." dans: The Journal of biological chemistry, Vol. 291, Issue 3, pp. 1103-14, (2016) (PubMed).

Kondala, Puri, Banka, Sachdeva, Sakhuja: "Short-term prognosis of potential celiac disease in Indian patients." dans: United European gastroenterology journal, Vol. 4, Issue 2, pp. 275-80, (2016) (PubMed).

Cox, Rumney, Schoof, Perryman, Høye, Agrawal, Bird, Latif, Forrest, Evans, Huggins, Lang, Linding, Gartland, Erler: "The hypoxic cancer secretome induces pre-metastatic bone lesions through lysyl oxidase." dans: Nature, Vol. 522, Issue 7554, pp. 106-10, (2015) (PubMed).

Miller, Morton, Pinese, Saturno, Jamieson, McGhee, Timpson, Leach, McGarry, Shanks, Bailey, Chang, Oien, Karim, Au, Steele, Carter, McKay, Anderson, Evans, Marais, Springer, Biankin, Erler, Sansom: "Targeting the LOX/hypoxia axis reverses many of the features that make pancreatic cancer deadly: inhibition of LOX abrogates metastasis and enhances drug efficacy." dans: EMBO molecular medicine, Vol. 7, Issue 8, pp. 1063-76, (2015) (PubMed).

Richter, Dayaram, Gilmartin, Ganji, Pemmasani, Van Der Key, Shohet, Donehower, Kumar: "WIP1 phosphatase as a potential therapeutic target in neuroblastoma." dans: PLoS ONE, Vol. 10, Issue 2, pp. e0115635, (2015) (PubMed).

Zhao, Sagare, Ma, Halliday, Kong, Kisler, Winkler, Ramanathan, Kanekiyo, Bu, Owens, Rege, Si, Ahuja, Zhu, Miller, Schneider, Maeda, Maeda, Sugawara, Ichida, Zlokovic: "Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance." dans: Nature neuroscience, Vol. 18, Issue 7, pp. 978-87, (2015) (PubMed).

Arnold, Kent, Hogarth, Schlatt, Prasad, Haenisch, Walsh, Muller, Griswold, Amory, Isoherranen: "Importance of ALDH1A enzymes in determining human testicular retinoic acid concentrations." dans: Journal of lipid research, Vol. 56, Issue 2, pp. 342-57, (2015) (PubMed).

Wilson, Bradley, Shaw, Wagenmakers: "Paxillin and focal adhesion kinase colocalise in human skeletal muscle and its associated microvasculature." dans: Histochemistry and cell biology, Vol. 142, Issue 3, pp. 245-56, (2014) (PubMed).

Nandhu, Hu, Cole, Erdreich-Epstein, Rodriguez-Gil, Viapiano: "Novel paracrine modulation of Notch-DLL4 signaling by fibulin-3 promotes angiogenesis in high-grade gliomas." dans: Cancer research, Vol. 74, Issue 19, pp. 5435-48, (2014) (PubMed).

Divakaran, Hines, McCarver: "Human hepatic UGT2B15 developmental expression." dans: Toxicological sciences : an official journal of the Society of Toxicology, Vol. 141, Issue 1, pp. 292-9, (2014) (PubMed).

Tansley, Betteridge, Gunawardena, Jacques, Owens, Pilkington, Arnold, Yasin, Moraitis, Wedderburn, McHugh: "Anti-MDA5 autoantibodies in juvenile dermatomyositis identify a distinct clinical phenotype: a prospective cohort study." dans: Arthritis research & therapy, Vol. 16, Issue 4, pp. R138, (2014) (PubMed).

Baker, Bird, Welti, Gourlaouen, Lang, Murray, Reynolds, Cox, Erler: "Lysyl oxidase plays a critical role in endothelial cell stimulation to drive tumor angiogenesis." dans: Cancer research, Vol. 73, Issue 2, pp. 583-94, (2013) (PubMed).

Détail du antigène

Antigène: LOX (Lysyl Oxidase (LOX))

Autre désignation: Lysyl Oxidase (LOX Produits)

Synonymes: LOX Protein, Xlox Protein, MGC146507 Protein, lox Protein, zgc:77447 Protein, AI893619 Protein, TSC-160 Protein, H-rev142 Protein, Rrg1 Protein, lysyl oxidase Protein, lysyl oxidase a Protein, lysyl oxidase L homeolog Protein, LOX Protein, lox Protein, loxa Protein, lox.L Protein, Lox Protein

Sujet: Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression. [UniProtKB/Swiss-Prot Function]

Poids moléculaire: 46.8 kDa

NCBI Accession: NP_002308

Pathways: SARS-CoV-2 Protein Interactome