Recombinant Xenopus laevis Matrix metalloproteinase-21(mmp21) CSB-EP014668XBE
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(MMP-21)(xMMP)
Species: (Organism)
Xenopus laevis (African clawed frog)
Gene Names:
mmp21
Tag info:
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Target Protein AA Sequence:
FLDMLMYSNKYREEQEALQKSTGKVFTKKLLKWRMIGEGYSNQLSINEQRYVFRLAFRMWSEVMPLDFEEDNTSPLSQIDIKLGFGRGRHLGCSRAFDGSGQEFAHAWFLGDIHFDDDEHFTAPSSEHGISLLKVAAHEIGHVLGLSHIHRVGSIMQPNYIPQDSGFELDLSDRRAIQNLYGSCEGPFDTAFDWIYKEKNQYGELVVRYNTYFFRNSWYWMYENRSNRTRYGDPLAIANGWHGIPVQNIDAFVHVWTWTRDASYFFKGTQYWRYDSENDKAYAEDAQGKSYPRLISEGFPGIPSPINAAYFDRRRQYIYFFRDSQVFAFDINRNRVAPDFPKRILDFFPAVAANNHPKGNIDVAYYSYTYSSLFLFKGKEFWKVVSDKDRRQNPSLPYNGLFPRRAISQQWFDICNVHPSLLKI
Expression Region:
181-604aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
57.2 kDa
Purity:
Greater than 85% 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:
Cancer
Function:
Involvement in disease:
Relevance:
Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway.
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:
Reference:
"A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development." Yang M., Murray M.T., Kurkinen M. J. Biol. Chem. 272:13527-13533(1997)
