Recombinant Mouse Protein-Lysine 6-Oxidase (LOX) Protein (His-Myc)

Name: Recombinant Mouse Protein-Lysine 6-Oxidase (LOX) Protein (His-Myc)
Brand: Beta LifeScience
SKU: BLC-04894P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Protein-Lysine 6-Oxidase (LOX) Protein (His-Myc) is produced by our Baculovirus expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P28301
Target Symbol	LOX
Synonyms	Lox; Rrg; Protein-lysine 6-oxidase; EC 1.4.3.13; Lysyl oxidase; Ras excision protein) [Cleaved into: Protein-lysine 6-oxidase; long form; Protein-lysine 6-oxidase; short form]
Species	Mus musculus (Mouse)
Expression System	Baculovirus
Tag	C-6His-Myc
Target Protein Sequence	DDPYNPYKYSDDNPYYNYYDTYERPRPGSRNRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY
Expression Range	163-411aa
Protein Length	Full Length of Mature Protein
Mol. Weight	32.4
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture.
Subcellular Location	Secreted. Secreted, extracellular space.
Protein Families	Lysyl oxidase family
Database References	KEGG: mmu:16948 STRING: 10090.ENSMUSP00000025409 UniGene: PMID: 28624291 LOX up-regulation is associated with enhanced oxidative stress that promotes p38MAPK activation, elastin structural alterations, and vascular stiffness. PMID: 28010122 These results suggest that LOX has the ability to induce RANKL expression on stromal cells; however, it fails to substitute for RANKL in osteoclastogenesis. PMID: 27606829 UXT Is a LOX-PP Interacting Protein That Modulates Estrogen Receptor Alpha Activity in Breast Cancer Cells. PMID: 28106301 Data show that LOX-PP enhances adipogenesis at least partially through inhibition of FGF-2 receptor signaling. PMID: 28452589 LOX targeting reduces peritoneal fibrosis. PMID: 28800626 Absence of lysyl oxidase (Lox) causes thoracic aortic aneurysms. The aortic mechanical behavior of Lox(-/-) mice is consistent with reduced elastin and collagen cross-linking but demonstrates vascular location-specific differences. Lox(-/-) aortas show upregulation of matrix remodeling genes and location-specific differential expression of other matrix and smooth muscle cell gene sets. PMID: 28550176 Findings from this study indicate that preventing LOX overexpression may be protective against high glucose-induced apoptosis in retinal vascular cells associated with diabetic retinopathy. PMID: 28538980 LOX family members contribute significantly to the detrimental effects of cardiac remodelling, highlighting LOX inhibition as a potential therapeutic strategy for post-infarction recovery PMID: 26260798 Findings suggest that the lysyl oxidase (LOX)-mediated organization of collagen fibers in the extracellular matrix is an important regulator of osteoblastogenesis. PMID: 26497171 The data suggest a fibromodulin-modulated collagen cross-linking mechanism where fibromodulin binds to a specific part of the collagen domain and also forms a complex with lysyl oxidase, targeting the enzyme toward specific cross-linking sites. PMID: 26893379 Data suggest of pharmacologic targeting of lysyl oxidase (LOX) pathway to inhibit liver fibrosis and promote its resolution. PMID: 26700732 Cu chaperone function of Atox1 mediated through Cu transporter ATP7A is required for VEGF-induced angiogenesis via activation of Cu enzyme lysyl oxidase. PMID: 26437801 CTR1, ATP7A, and lysyl oxidase were upregulated in the lung tissues and pulmonary arteries of mice with hypoxia-induced pulmonary hypertension and pulmonary arterial smooth muscle cells. PMID: 24614111 Inhibition of tissue transglutaminase resulted in a reduced rate of compaction compared to controls during early remodeling (up to 2 days). In contrast, inhibition of lysyl oxidase did not alter the early compaction. PMID: 25924936 decreased expression of cross-linking enzymes (LOXs) and increased expression of ECM-degrading proteinases (MMP-1, 2, 3) might be of great contribution to poor healing ability of PCL ligament PMID: 25416119 LOX is indispensable for the progression of BLM-induced experimental lung fibrosis by aggravating the inflammatory response and subsequent fibrosis process after lung injury. PMID: 25348956 LOX and LOXL2 may play an important role in the pathogenesis of AMD. Targeting LOXL2 could have a broader efficacy than targeting LOX, by reducing angiogenesis and inflammation, as well as fibrosis. PMID: 26258612 LOX plays a critical role in vascular remodelling PMID: 24990180 LOX is a novel regulator of NFATc1-driven osteoclastogenesis, independent of RANK ligand, which disrupts normal bone homeostasis leading to the formation of focal pre-metastatic lesions PMID: 26017313 DDR2 binding and activation were disrupted by collagen glycation, pointing to a mechanism for the diminished levels of lysyl oxidase and consequently low lysyl oxidase-derived cross-links in diabetic bone. PMID: 24120383 miR-29b down-regulates HSP47 and LOX expression. PMID: 24650661 lysyl oxidase activity participates in primary tumor growth by directly impacting the senescence stability. PMID: 24113189 Stromally derived lysyl oxidase promotes metastasis of transforming growth factor-beta-deficient mouse mammary carcinomas. PMID: 23856251 Silencing of lysyl oxidase in BMP4-treated C3H10T1/2 cells induced a mesenchymal-epithelial transition (MET)-like response associated with the repression of mesenchymal markers, induction of epithelial markers and decreased cell migration. PMID: 23395997 LOX expression is strongly upregulated in Staphylococcus aureus infections in vivo. PMID: 23649089 Suggest a causal relationship between LOX downregulation and aortic stiffening in obesity. PMID: 23413430 Stress urinary incontinence following vaginal trauma involves over-expression of LOX and decreased synthesis of extracellular matrix components or increased proteolysis in the urethra. PMID: 22572217 Data show that lysyl oxidase LOX staining intensity was intermittent in the ligamentum flavum over from stages E15 to 2 years, and stages that stained intensely were E16 and E18, and P7 through P21. PMID: 22685574 the lysyl oxidase (Lox) protein is degraded through lysosome and accumulated in the Vps18 deficient cerebellum but not in cerebral cortices. PMID: 22699122 Lysyl oxidase activity is essential to generate optimal chemotactic sensitivity of cells to chemoattractants by oxidizing specific cell surface proteins, such as platetlet-derived growth factor receptor (PDGFR)-beta. PMID: 21509606 These results indicate that proLOX could be processed by two different mechanisms producing two forms of active LOX. PMID: 21591931 LOX-PP is shown to negatively regulate pro-oncogenic beta-catenin signaling in lung cancer cells. PMID: 21690299 LOX is a potential mediator that couples mechanotransduction to oncogenic signaling by TGF-beta1 and measures capable of inactivating LOX function may prove effective in diminishing breast cancer progression stimulated by TGF-beta1. PMID: 21532881 in vitro and in vivo data support a novel role for LOX in regulating MK expansion by PDGF-BB and suggest LOX as a new potential therapeutic target for myelofibrosis PMID: 21665949 Data show that CA9, GLUT1 and LOX mRNA levels were equally and strongly correlated to hypoxic extent in FaDudd, and the same profile was observed for CA9 and GLUT1, but not LOX, in SCCVII tumors. PMID: 21306648 LKB1 loss of function promotes lung cancer malignancy through remodeling of extracellular matrix microenvironment, and identify LOX as a potential target for disease treatment in lung cancer patients. PMID: 20956321 Suggest that uric acid increases fibronectin synthesis both in vivo and in vitro via urate transporters through upregulation of lysyl oxidase expression. PMID: 20484295 periostin supported BMP-1-mediated proteolytic activation of LOX on the extracellular matrix, which promoted collagen cross-linking. PMID: 20181949 LOX has a novel function in resolving inflammation by reducing MCP-1 in abdominal aortic aneurysm PMID: 19683237 Lysyl oxidase has a role in oxidizing basic fibroblast growth factor and inactivating its mitogenic potential PMID: 12461785 lysyl oxidase appears critical during embryogenesis for structural stability of the aorta and diaphragm and connective tissue development PMID: 12473682 Lox expression is prominent during embryonic cardiovascular development. PMID: 12524683 Anti-oncogenic effects of lysyl oxidase on ras-mediated transformation are due to its ability to inhibit signaling pathways that lead to activation of NF-kappa B PMID: 12640111 FGF-2 autocrine pathway inhibits lysyl oxidase transcription in the tumorigenic-transformed RS485 cell line. PMID: 12788924 The LOX expressed in the choroid plexus, blood vessel walls, brain matrix, and neurons of normal mice. And LOX gene expression was enhanced in the neurons of the spinal cord, brain stem, cortex, caudoputamen and cerebellum in mSOD1 mice. PMID: 14741400 collagen deposition and lysyl oxidase are regulated by tumor necrosis factor-alpha in osteoblasts PMID: 15138266 lysyl oxidase functions to inhibit ras-dependent cell transformation PMID: 15277520 Results compare the immunohistochemical localization of lysyl oxidase and lysyl oxidase-like in various tissues from normal, young adult mice. PMID: 15609098 the FN matrix may provide specific microenvironments to regulate LOX catalytic activity PMID: 15843371

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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