Recombinant Rat Protein-Lysine 6-Oxidase (LOX) Protein (His)

Name: Recombinant Rat Protein-Lysine 6-Oxidase (LOX) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04403P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Protein-Lysine 6-Oxidase (LOX) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P16636
Target Symbol	LOX
Synonyms	LoxProtein-lysine 6-oxidase; EC 1.4.3.13; Lysyl oxidase) [Cleaved into: Protein-lysine 6-oxidase; long form; Protein-lysine 6-oxidase; short form]
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DDPYNPYKYSDDNPYYNYYDTYERPRSGSRHRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYSNNVVRCEIRYTGHHAYASGCTISPY
Expression Range	163-411aa
Protein Length	Full Length of Mature Protein
Mol. Weight	33.0kDa
Research Area	Others
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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: rno:24914 STRING: 10116.ENSRNOP00000065314 UniGene: Rn.11372
Tissue Specificity	Aorta and lung.

Gene Functions References

data suggest a detrimental role for the chronic increase of cardiac LOX expression and activity in the transition from compensated remodeling to decompensated failure. PMID: 28668305
Together, these findings suggest that bone fragility in DM2 is initiated in the matrix phase and that the LOX family may play a critical part in the pathogenesis of DM2 mediated bone fragility. PMID: 29146187
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
The reduction of leptin levels by BAPN in vivo and the ability of this compound to inhibit leptin-induced profibrotic mediators and ROS production in cardiac and vascular cells suggest that interactions between leptin and LOX regulate downstream events responsible for myocardial and vascular fibrosis in obesity. PMID: 26780438
LOX can promote the progress of epithelial-to-mesenchymal transition in a rat model of pulmonary fibrosis. PMID: 26670953
In transgenic mice expressing rat LOX in wild-type megakaryocytes and platelets, higher affinity of Pf4-Lox(tg/tg) platelets to the collagen sequence GFOGER implies that the collagen receptor integrin alpha2beta1 is affected by LOX. PMID: 26755713
Silenced lysyl oxidase expression results the growth of C3H10T1/2 cells by 50%, and blocked osteoblast differentiation. PMID: 24971753
Decreased lox expression in diaphragmatic development and lung branching morphogenesis may contribute to the diaphragmatic defect and impaired airway formation in the nitrofen-induced congenital diaphragmatic hernia model. PMID: 25111273
Results indicate that polyphenols bind to monomeric tropoelastin and enhance coacervation, aid in crosslinking of elastin by increasing lysyl oxidase (LOX) synthesis, and by blocking MMP-2 activity. PMID: 24440697
Study supports a novel mechanism of n-acetylcysteine alleviating idiopathic pulmonary fibrosis by inhibition of LOX activity in a rat model. Time course of LOX activity during bleomycin-induced pulmonary fibrosis was also examined. PMID: 23006535
These results suggest that in an indirect co-culture system, pelvic ligament fibroblasts with mechanical stretch stimulation can promote bone mesenchymal stem cell differentiation, reflecting in the increased expression of elastin, LOX, and Fibulin-5. PMID: 22205540
These findings indicate that TNF-alpha stimulated LOX expression may play an important role in progressive cardiac fibrosis. PMID: 21893029
In cardiac fibroblasts, Rac1 GTPase mediates upregulation of fibronectin via LOX and CTGF. PMID: 21215756
The data presented herein regarding chromatin remodeling indirectly support the hypothesis that LOX binds to histone H1 in vivo. PMID: 20888776
LOX were overexpressed in late stages of intimal hyperplasia in the allografts PMID: 20606470
Suggest that uric acid increases fibronectin synthesis both in vivo and in vitro via urate transporters through upregulation of lysyl oxidase expression. PMID: 20484295
lysyl oxidase propeptide contains both N- and O-linked carbohydrates; its structure is a mostly disordered protein PMID: 20192271
Data indicate that lysyl oxidase propeptide (LOX-PP) inhibits terminal mineralization in primary calvaria osteoblast cultures when added at early stages of differentiation, with no effects seen when present at later stages. PMID: 20048148
a PKC-MEK-MAPK-dependent pathway is critical to the enhanced expression of the LO gene PMID: 11968017
findings indicate control of lysyl oxidase at endocrine, paracrine, and autocrine levels within the ovary and suggest coordinated regulation of ovarian extracellular matrix during follicular development PMID: 12488341
comparison and aa sequence alignment of human and rat lysyl oxidase and lysyl oxidase-like gene (LOXL1); role in formation and repair of ECM elastin and collagen PMID: 12577300
Beta-catenin transformation pathway is activated by lysyl oxidase down-regulation. PMID: 12686140
The results showed that LOX was expressed in the choroid plexus, blood vessel walls, brain matrix, and neurons of normal rat. PMID: 14741400
Upregulation by cigarette smoke condensate(CSC) of cellular thiols may play an important role in the downregulation of lysyl oxidase and subsequently destabilization of the lung ECM in CS-induced emphysema. PMID: 15509664
Downregulation of LO is linked with upregulation of other Cu-binding proteins and with alteration in Cu homeostasis in the cadmium resistant lung fibroblasts. PMID: 17584760
These novel data suggest that LOX-PP may provide a feedback control mechanism that serves to inhibit properties associated with the development of vascular pathology. PMID: 18060869
spatial and temporal expression of LOX and LOXL1 during growth and aging in the aorta and specific roles for LOX and LOXL1 in the synthesis and remodeling of elastic and collagen fibers PMID: 18803461

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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.

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