- Pack type:Vial
- Conjugation:Unconjugated
- Protein/Peptide Type:Recombinant
- Source:E. coli
- Species:Mouse
- Size:50 µg
- Tag sequence:MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDGSTSGSGHHHHHHSAGLVPRGSTAIGMKETAAAKFERQHMDSPDLGTGGGSGIEGRGSMGYRGSEF
- Storage Conditions:–20 °C
- Endotoxin Content:<1.0 EU per 1 μg (determined by the LAL method)
- Gene ID:16948
- Reconstitution Instructions:Reconstitute in 10 mM PBS (pH 7.4) to a concentration of 0.1 - 1.0 mg/ml. Do not vortex.
- Endotoxin-free:N
- Carrier-Free:Y
- Protease-free:N
- Animal-Free:Y
- Protein Synonyms:Lysyl Oxidase
- UniProtKB:P28301
- Protein/Peptide Name:LOX
- Purity:90 - 100%
- Molecular Weight:54 kDa
- Sequence:Pro207~Tyr411
- Endotoxin Level:Low
- Concentration:0.2 mg/ml
- Formulation:Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose.
- Nuclease-free:N
- Shipping Temperature:4 °C
- Tested Applications:Positive control, Immunogen, SDS-PAGE, Western blot.
- Cat. No.:MSPP-RPC580MU1
This is a LOX recombinant protein (prokaryotic), Mouse is sequencing from Pro207~Tyr411 with 90 - 100% purity. Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose with 0.2 mg/ml.
- High quality, purity, reproducibility and effectiveness
- Offers customized buffers and tag options
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Lysyl oxidase is a protein. Its inhibition can cause lathyrism, but at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.Lysyl oxidase is an extracellular copper enzyme that catalyzes formation of aldehydes from lysine residues in collagen and elastin precursors.These aldehydes are highly reactive, and undergo spontaneous chemical reactions with other lysyl oxidase-derived aldehyde residues, or with unmodified lysine residues. This results in cross-linking collagen and elastin, which is essential for stabilization of collagen fibrils and for the integrity and elasticity of mature elastin.Complex cross-links are formed in collagen and in elastin that differ in structure.