Recombinant Rat Protein-lysine 6-oxidase(Lox) CSB-EP013038RA
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Lysyl oxidase
Species: (Organism)
Rattus norvegicus (Rat)
Gene Names:
Lox
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
DDPYNPYKYSDDNPYYNYYDTYERPRSGSRHRPGYGTGYFQYGLPDLVPDPYYIQASTYVQKMSMYNLRCAAEENCLASSAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDASTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYAADIDCQWIDITDVQPGNYILKVSVNPSYLVPESDYSNNVVRCEIRYTGHHAYASGCTISPY
Expression Region:
163-411aa
Subcellular Location:
Secreted, Secreted, extracellular space
Tissue Specificity:
Aorta and lung.
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
33 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:
Others
Function:
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin
Involvement in disease:
Relevance:
Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin.
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:
Metalloproteinase activity secreted by fibrogenic cells in the processing of prolysyl oxidase. Potential role of procollagen C-proteinase.Panchenko M.V., Stetler-Stevenson W.G., Trubetskoy O.V., Gacheru S.N., Kagan H.M.J. Biol. Chem. 271:7113-7119(1996)
