Alternative Name(s):

Lysyl oxidase

Species: (Organism)

Homo sapiens (Human)

Gene Names:

LOX

Tag info:

N-terminal 6xHis-tagged

Target Protein AA Sequence:

PYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY

Expression Region:

174-417aa

Subcellular Location:

Secreted, Secreted, extracellular space

Tissue Specificity:

Heart, placenta, skeletal muscle, kidney, lung and pancreas.

Protein Length:

Partial

Pathway:

Mol. Weight:

32.4 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Signal Transduction

Function:

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin

Involvement in disease:

Aortic aneurysm, familial thoracic 10 (AAT10)

Relevance:

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of Extracellular domain matrix proteins, may have a direct role in tumor suppression.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Lysyl oxidase family

Reference:

Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2.Haemaelaeinen E.-R., Jones T.A., Sheer D., Taskinen K., Pihlajaniemi T., Kivirikko K.I.Genomics 11:508-516(1991)