Recombinant Escherichia phage lambda Capsid decoration protein(D) CSB-EP361132FSFe3
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
Capsid decoration protein(Auxiliary protein D)(Gene product D)(gpD)(Major capsid protein D)
Species: (Organism)
Escherichia phage lambda (Bacteriophage lambda)
Gene Names:
D
Tag info:
N-terminal 6xHis-KSI-tagged
Target Protein AA Sequence:
MTSKETFTHYQPQGNSDPAHTATAPGGLSAKAPAMTPLMLDTSSRKLVAWDGTTDGAAVGILAVAADQTSTTLTFYKSGTFRYEDVLWPEAASDETKKRTAFAGTAISIV
Expression Region:
1-110aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length
Pathway:
Mol. Weight:
26.9 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:
Cardiovascular
Function:
Involvement in disease:
Relevance:
Stabilizes the expansion of the capsid head shell after genome packaging. The packaging of viral genome in the procapsid triggers a dramatic reconfiguration of the capsid shell, expanding from roughly 50nm to 60nm while the capsid thickness decreases. 415 capsid decoration protein molecules cooperatively bind the expanded capsid, thereby stabilizing the mature capsid shell.
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:
"Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM." Lander G.C., Evilevitch A., Jeembaeva M., Potter C.S., Carragher B., Johnson J.E. Structure 16:1399-1406(2008)
