Recombinant Mouse Properdin(Cfp) CSB-YP005291MOf3
Specifications
| 20ug / 100ug / 500ug price = 100ug |
Alternative Name(s):
Complement factor P
Species: (Organism)
Mus musculus (Mouse)
Gene Names:
Cfp
Tag info:
C-terminal 6xHis-Myc-tagged
Target Protein AA Sequence:
SDPVLCFTQYEESSGRCKGLLGRDIRVEDCCLNAAYAFQEHDGGLCQACRSPQWSAWSLWGPCSVTCSEGSQLRHRRCVGRGGQCSENVAPGTLEWQLQACEDQPCCPEMGGWSEWGPWGPCSVTCSKGTQIRQRVCDNPAPKCGGHCPGEAQQSQACDTQKTCPTHGAWASWGPWSPCSGSCLGGAQEPKETRSRSCSAPAPSHQPPGKPCSGPAYEHKACSGLPPCPVAGGWGPWSPLSPCSVTCGLGQTLEQRTCDHPAPRHGGPFCAGDATRNQMCNKAVPCPVNGEWEAWGKWSDCSRLRMSINCEGTPGQQSRSRSCGGRKFNGKPCAGKLQDIRHCYNIHNCIMKGSWSQWSTWSLCTPPCSPNATRVRQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGTPRPLCEALQGQKLVVEEKRSCLHVPVCKDPEEKKP
Expression Region:
23-464aa
Subcellular Location:
Secreted
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
50.9 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:
Immunology
Function:
A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
Involvement in disease:
Relevance:
A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
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:
"The transcriptional landscape of the mammalian genome."Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005)
