product summary
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company name :
Novus Biologicals
other brands :
IMGENEX
product type :
antibody
product name :
LOX propeptide Antibody - BSA Free
catalog :
NB110-41568
quantity :
0.1 ml (also 0.025 ml)
price :
409 USD
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
clone name :
SMP14
reactivity :
human, mouse, rat
application :
western blot, immunohistochemistry, immunocytochemistry, immunohistochemistry - paraffin section
more info or order :
citations: 26
Reference
Chandrakumar S, Santiago Tierno I, Agarwal M, Lessieur E, Du Y, Tang J, et al. Mechanical Regulation of Retinal Vascular Inflammation and Degeneration in Diabetes. Diabetes. 2024;73:280-291 pubmed publisher
Chandrakumar S, Santiago Tierno I, Agarwal M, Matisioudis N, Kern T, Ghosh K. Subendothelial Matrix Stiffening by Lysyl Oxidase Enhances RAGE-Mediated Retinal Endothelial Activation in Diabetes. Diabetes. 2023;72:973-985 pubmed publisher
Neff L, Zhang Y, Van Laer A, Baicu C, Karavan M, Zile M, et al. Mechanisms that limit regression of myocardial fibrosis following removal of left ventricular pressure overload. Am J Physiol Heart Circ Physiol. 2022;323:H165-H175 pubmed publisher
Chu Q, Xiao Y, Song X, Kang Y. Extracellular matrix remodeling is associated with the survival of cardiomyocytes in the subendocardial region of the ischemic myocardium. Exp Biol Med (Maywood). 2021;246:2579-2588 pubmed publisher
Kaczorowski A, Tolstov Y, Falkenstein M, Vasioukhin V, Prigge E, Geisler C, et al. Rearranged ERG confers robustness to prostate cancer cells by subverting the function of p53. Urol Oncol. 2020;38:736.e1-736.e10 pubmed publisher
Ilatovskaya D, Pitts C, Clayton J, Domondon M, Troncoso M, Pippin S, et al. CD8+ T-cells negatively regulate inflammation post-myocardial infarction. Am J Physiol Heart Circ Physiol. 2019;317:H581-H596 pubmed publisher
Shearer D, Mervis M, Manley E, Reddy A, Alford A. TSP1 and TSP2 deficiencies affect LOX protein distribution in the femoral diaphysis and pro-peptide removal in marrow-derived mesenchymal stem cells in vitro. Connect Tissue Res. 2019;60:495-506 pubmed publisher
Kielosto M, Eriksson J, Nummela P, Yin M, Hölttä E. Divergent roles of lysyl oxidase family members in ornithine decarboxylase- and RAS-transformed mouse fibroblasts and human melanoma cells. Oncotarget. 2018;9:37733-37752 pubmed publisher
Breton Y, Desrosiers V, Ouellet M, Deshiere A, Torresilla C, Cohen E, et al. Expression of MDM2 in Macrophages Promotes the Early Postentry Steps of HIV-1 Infection through Inhibition of p53. J Virol. 2019;93: pubmed publisher
Varona S, Orriols M, Galán M, Guadall A, Cañes L, Aguiló S, et al. Lysyl oxidase (LOX) limits VSMC proliferation and neointimal thickening through its extracellular enzymatic activity. Sci Rep. 2018;8:13258 pubmed publisher
Ramos G, Cruz A, Silva W, Rozanski A, Baptista I, Silvestre J, et al. Thyroid hormone upregulates MDM2 in rat type i fiber: implications for skeletal muscle mass regulation. Acta Physiol (Oxf). 2017;: pubmed publisher
Voorhees A, DeLeon Pennell K, Ma Y, Halade G, Yabluchanskiy A, Iyer R, et al. Building a better infarct: Modulation of collagen cross-linking to increase infarct stiffness and reduce left ventricular dilation post-myocardial infarction. J Mol Cell Cardiol. 2015;85:229-39 pubmed publisher
Joshi Y, Sória M, Quadrato G, Inak G, Zhou L, Hervera A, et al. The MDM4/MDM2-p53-IGF1 axis controls axonal regeneration, sprouting and functional recovery after CNS injury. Brain. 2015;138:1843-62 pubmed publisher
Inaba H, Kuboniwa M, Sugita H, Lamont R, Amano A. Identification of signaling pathways mediating cell cycle arrest and apoptosis induced by Porphyromonas gingivalis in human trophoblasts. Infect Immun. 2012;80:2847-57 pubmed publisher
de Freitas M, Ramalho L, Xavier F, Moreira A, Reis S. p53 and MDM2 protein expression in actinic cheilitis. J Appl Oral Sci. 2008;16:414-9 pubmed
Chen D, Zhang Z, Li M, Wang W, Li Y, Rayburn E, et al. Ribosomal protein S7 as a novel modulator of p53-MDM2 interaction: binding to MDM2, stabilization of p53 protein, and activation of p53 function. Oncogene. 2007;26:5029-37 pubmed
Stevenson L, Sparks A, Allende Vega N, Xirodimas D, Lane D, Saville M. The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J. 2007;26:976-86 pubmed
Pääjärvi G, Roudier E, Crisby M, Hogberg J, Stenius U. HMG-CoA reductase inhibitors, statins, induce phosphorylation of Mdm2 and attenuate the p53 response to DNA damage. FASEB J. 2005;19:476-8 pubmed
Minsky N, Oren M. The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression. Mol Cell. 2004;16:631-9 pubmed
Menendez S, Higgins M, Berkson R, Edling C, Lane D, Lain S. Nuclear export inhibitor leptomycin B induces the appearance of novel forms of human Mdm2 protein. Br J Cancer. 2003;88:636-43 pubmed
Goldberg Z, Vogt Sionov R, Berger M, Zwang Y, Perets R, Van Etten R, et al. Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation. EMBO J. 2002;21:3715-27 pubmed
Kersemaekers A, Mayer F, Molier M, Van Weeren P, Oosterhuis J, Bokemeyer C, et al. Role of P53 and MDM2 in treatment response of human germ cell tumors. J Clin Oncol. 2002;20:1551-61 pubmed
Hjerrild M, Milne D, Dumaz N, Hay T, Issinger O, Meek D. Phosphorylation of murine double minute clone 2 (MDM2) protein at serine-267 by protein kinase CK2 in vitro and in cultured cells. Biochem J. 2001;355:347-56 pubmed
Rodriguez Lopez A, Xenaki D, Eden T, Hickman J, Chresta C. MDM2 mediated nuclear exclusion of p53 attenuates etoposide-induced apoptosis in neuroblastoma cells. Mol Pharmacol. 2001;59:135-43 pubmed
Berger M, Vogt Sionov R, Levine A, Haupt Y. A role for the polyproline domain of p53 in its regulation by Mdm2. J Biol Chem. 2001;276:3785-90 pubmed
Sionov R, Moallem E, Berger M, Kazaz A, Gerlitz O, Ben Neriah Y, et al. c-Abl neutralizes the inhibitory effect of Mdm2 on p53. J Biol Chem. 1999;274:8371-4 pubmed
product information
master code :
NB110-41568
SKU :
NB110-41568
product name :
LOX propeptide Antibody - BSA Free
unit size :
0.1 ml (also 0.025 ml)
description :
The LOX propeptide Antibody - BSA Free from Novus is a rabbit polyclonal antibody to LOX propeptide. This antibody reacts with human,mouse,porcine,rat. The LOX propeptide Antibody - BSA Free has been validated for the following applications: Western Blot,Immunohistochemistry-Paraffin,Immunohistochemistry,Immunoblotting,Immunocytochemistry/ Immunofluorescence.
target :
LOX propeptide
category :
Primary Antibodies
buffer :
PBS
clonality :
Polyclonal
concentration :
1 mg/ml
conjugate :
Unconjugated
host :
Rabbit
immunogen :
A synthetic peptide made to an internal region of mouse LOX propeptide (residues 78-115). [UniProt# P28301]
isotype :
IgG
purity :
Immunogen affinity purified
species :
Human,Mouse,Porcine,Rat
specificity :
This antibody specifically recognizes both the pro-enzyme and pro-peptide forms of LOX protein in mouse and rat
gene symbol :
LOX
applications :
Western Blot,Immunohistochemistry-Paraffin,Immunohistochemistry,Immunoblotting,Immunocytochemistry/ Immunofluorescence
USD :
409 USD
alt names :
lysyl oxidaseEC 1.4.3.13, MGC105112, protein-lysine 6-oxidase
storage :
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
more info or order :
company information
Novus Biologicals
10771 E Easter Ave
Centennial, CO 80112
novus@novusbio.com
https://www.novusbio.com
3037301950
headquarters: USA
Novus Biologicals licenses, manufactures, and markets antibodies to over 20,000 unique targets to support a wide array of research areas. Novus is built on honesty, collaboration and strong relationships and continues to provide quality tools that accelerate research. Every product is backed by our 100% guarantee.