Recombinant Human LOX Protein

Beta LifeScience SKU/CAT #: BL-1083SG

Recombinant Human LOX Protein

Beta LifeScience SKU/CAT #: BL-1083SG
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag GST
Host Species Human
Accession BC074872
Synonym Lysyl oxidase
Background LOX or lysyl oxidase is an extracellular copper enzyme that initiates the cross-linking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin (1). LOX plays an important role in tumor suppression (2). LOX may be required to create a niche permissive for metastatic growth and it is essential for hypoxia-induced metastasis.
Description Recombinant human LOX (169-end) was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence 169a.a.-end
Molecular Weight 57 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human LOX Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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

HGNC: 6664

OMIM: 153455

KEGG: hsa:4015

STRING: 9606.ENSP00000231004

UniGene: PMID: 28416796

  • The Epithelial-mesenchymal transition (EMT) marker Lox has a differential expression pattern in breast cancer, being significantly overexpressed in triple negative breast cancers. PMID: 29661738
  • Studies indicate that the mature enzyme plays a key role in modifying the extracellular matrix and as a result has been implicated in playing a role in the formation of cancer "niches" where tumors will develop and eventually metastasize [Review]. PMID: 29309816
  • Our results indicate the involvement of LOX in the initiation of fibrous capsule formation which ultimately contributes towards the progression of capsular contracture PMID: 29866167
  • this study has revealed that IL-1beta may contribute to the rupture of fetal membranes by attenuating collagen crosslinking through downregulation of LOX expression in amnion fibroblasts PMID: 28878297
  • This study focused on the relationship between lysyl oxidase (LOX), LOX-like protein 1 (LOXL1), and LOXL2 and pulmonary emphysema pathogenesis. PMID: 28965583
  • The aim was to examine if the serum concentrations of elastin-related proteins correlate to signs of cardiovascular diseases in patients with Diabetes mellitus type 2. PMID: 28715234
  • LOX role in cancer stromal cells activation and promotion of gastric cancer progression PMID: 29343955
  • an association of LOX gene polymorphism (G473A) on diabetes and DFU patients PMID: 28522400
  • LOX expression was mildly but significantly upregulated in CD34+-derived primary myelofibrosis megakaryocytes and platelets compared with controls. These megakaryocytes showed a greater tendency to adhere and spread to monomeric collagen, and this was inhibited by the LOX-specific inhibitor BAPN. PMID: 28592432
  • Data suggest that a missense mutation in lysyl oxidase (LOX) is associated with aortic disease. PMID: 27432961
  • Our findings suggest that LOX has a role in cancer cell mitosis PMID: 27296552
  • Our findings provide new evidence that LOX regulates SNAI2 expression and that SNAI2-mediated TIMP4 secretion plays a role in cancer progression. PMID: 27029493
  • UXT Is a LOX-PP Interacting Protein That Modulates Estrogen Receptor Alpha Activity in Breast Cancer Cells. PMID: 28106301
  • LOX is a prognostic factor for poor progression free survival in patients with ER- breast cancer. LOX overexpression was positively correlated with resistance to radiation and drug therapy. PMID: 27147578
  • This preliminary study indicated that LOX gene polymorphisms, such as rs2303656, rs3900446, and rs763497, may play crucial roles in intracranial aneurysm formation in the Korean population. PMID: 28792146
  • Results show that CTGF mediates the GDF8-induced up-regulation of LOX expression and increases in LOX activity in human granulosa cells. PMID: 27392496
  • The LOXL1 SNPs, rs1048661 and rs3825942, are associated with PXF in the South Indian population correlating with lowered LOX activity in the aqueous humor. The increased level of total TGF-beta in the aqueous humor of PXF cases is possibly associated with LOX regulation which needs further investigation. PMID: 27116380
  • These findings suggest that LOX induces an age-dependent disturbance of diastolic function and aggravates Ang II-induced hypertrophy, which provides novel insights into the role of LOX in cardiac performance. PMID: 28522596
  • LOX, a hypoxia-responsive gene that encodes lysyl oxidase, is activated by HIF-2-alpha more than HIF-1. Two new hypoxia response elements identified in the LOX promoter mediate most HIF responsiveness. PMID: 28624448
  • our findings show that LOX supports colorectal cancer cell dissemination in the bone marrow PMID: 27742687
  • LOX G473A polymorphism apparently elevated human sensitivity to cigarette smoking carcinogens for eliciting cancers in the lung and colon only. Thus, LOX G473A polymorphism positively correlates with carcinogenesis and it may be used as an ideal intrinsic biomarker for prediction or diagnosis of carcinogenesis in humans. PMID: 27367711
  • increased cortisol and 11beta-HSD1 abundance and decreased LOX abundance were observed in human amnion tissue after the labor-initiated spontaneous rupture of membranes PMID: 27533889
  • endogenous LOX is overexpressed in clear cell renal cell carcinoma, is involved in a positive-regulative loop with HIF-1alpha, and has a major action on clear cell renal cell carcinoma progression through cellular adhesion, migration, and collagen matrix stiffness increment PMID: 27449199
  • colorectal carcinoma perilesional extracellular matrix has increased content of lysyl oxidase PMID: 26940881
  • LOX affects the epithelial-mesenchymal transition of gastric cancer cells in hypoxic conditions. PMID: 26100130
  • High expression of LOX is associated with nasopharyngeal carcinoma. PMID: 26882568
  • Here we show that orthotopic implantation of rat prostate AT-1 tumour cells increased LOX and LOXLs mRNA expressions in the tumour and in the surrounding non-malignant prostate tissue PMID: 26804196
  • Results show that LOX expression regulation by FoxF1 increases invasiveness of breast cancer cells. PMID: 26908052
  • LOX gene expression was approximately 2.5-fold higher in fetal membranes from preterm prelabor rupture of membranes (pPROM) compared to preterm and term birth. PMID: 26011922
  • 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
  • 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
  • Our study demonstrated that the LOX rs1800449 genotypes (AA and GA + AA) and allele (A) appears to confer risk for susceptibility to keratoconus. PMID: 24502826
  • Individuals with LOX variants had fusiform enlargement of the aortic root and ascending thoracic aorta, leading to ascending aortic dissections. PMID: 26838787
  • two LOX variants, rs2956540 and rs10519694, may affect individual susceptibility to keratoconus PMID: 26713757
  • LOX expression at the mRNA and protein level, and enzymatic activity were remarkably upregulated in the hypoxic A549 cells, compared with normoxic A549 cells. PMID: 26515140
  • Aortic tissue from Marfan syndrome patients and display enhanced expression of the members of the LOX family, LOX and LOX-like 1. PMID: 25988230
  • Evidence for association was found for both of the tested loci.It was strongest for rs3735520:G>A near HGF with A allele being a risk factor and rs2956540:G>C within LOX with C allele having a protective effect PMID: 25735481
  • Using principal component analysis (PCA), the authors identified a LOX/hypoxia signature associated with poor patient survival in resectable pancreatic ductal adenocarcinoma patients. PMID: 26077591
  • Serum sLOX-1 levels were independently correlated with the presence and severity of OSA. PMID: 25825846
  • hypoxic stress of obstructive sleep apnea may increase circulating lysyl oxidase (LOX) levels; LOX may serve as a biomarker of liver fibrosis in patients with severe obesity and nonalcoholic fatty liver disease PMID: 26085300
  • these results corroborate the role of LOX in the migration, invasion and angiogenesis of astrocytomas. Furthermore, LOX expression is influenced by IDH1 mutational status. PMID: 25790191
  • LOX gene expression is a predictive factor in hepatocellular liver cancer prognosis and mortality. PMID: 26048020
  • High lysyl oxidase expression level in amnion is associated with higher birth weight of Tibetan newborns. PMID: 25501874
  • High LOX expression was associated with a poor disease-free and metastasis-free survival in ER negative but not ER positive breast cancer patients. PMID: 25141126
  • Study demonstrated that reactive oxygen species promote the migration and metastatic growth of ovarian cancer cells via upregulation of HIF-1a and LOX and E-cadherin repression. PMID: 25174950
  • LOX activity is required in the control of collagen fibril architecture. PMID: 25979340
  • Attenuation of lysyl oxidase and collagen gene expression in keratoconus patient corneal epithelium corresponds to disease severity. PMID: 25593510
  • LOX may play a role in the metastasis of non-small cell lung cancer by promoting MMP2/MMP9 expression. LOX expression is an independent prognostic factor for survival in NSCLC. PMID: 25337249
  • 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
  • FAQs

    Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

    Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

    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.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

    Recently viewed