LOX Protein (Myc-DYKDDDDK Tag)

Produktnummer ABIN2712316

Produktdetails

Target: LOX (Lysyl Oxidase (LOX))

Protein-Typ: Recombinant

Spezies: Human

Quelle: HEK-293 Cells

Aufreinigungstag / Konjugat: Dieses LOX Protein ist gelabelt mit Myc-DYKDDDDK Tag.

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

Produktmerkmale:

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

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

Anwendungsinformationen

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

Kommentare:

The tag is located at the C-terminal.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Konzentration: 50 μg/mL

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

Lagerung: -80 °C

Informationen zur Lagerung: 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.

Referenzen

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." in: 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." in: 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." in: 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." in: 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." in: 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." in: 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." in: 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." in: 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." in: Cancer research, Vol. 74, Issue 19, pp. 5435-48, (2014) (PubMed).

Divakaran, Hines, McCarver: "Human hepatic UGT2B15 developmental expression." in: 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." in: 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." in: Cancer research, Vol. 73, Issue 2, pp. 583-94, (2013) (PubMed).

Antigendetails

Target: LOX (Lysyl Oxidase (LOX))

Andere Bezeichnung: Lysyl Oxidase (LOX Produkte)

Synonyme: 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

Hintergrund: 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]

Molekulargewicht: 46.8 kDa

NCBI Accession: NP_002308

Pathways: SARS-CoV-2 Protein Interaktom