Recombinant Staphylococcus aureus Gamma-hemolysin component C(hlgC) CSB-EP739984SKX
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
hlgC; SAR2510; Gamma-hemolysin component C
Species: (Organism)
Staphylococcus aureus (strain MRSA252)
Gene Names:
hlgC
Tag info:
N-terminal 6xHis-SUMO-tagged
Target Protein AA Sequence:
ANDTEDIGKGNDVEIIKRTEDKTSNKWGVTQNIQFDFVKDKKYNKDALILKMQGFISSRTTYYNYKNTNHIKSMRWPFQYNIGLKTNDKYVSLINYLPKNKIESTNVSQTLGYNIGGNFQSAPSLGGNGSFNYSKSISYTQQNYVSEVEQQNSKSVLWGVKANSFATESGQKSAFDSDLFVGYKPHSKDPRDYFVPDSELPPLVQSGFNPSFIATVSHEKGSSDTSEFEITYGRNMDVTHAIKRSTHYGNSYLDGHRVHNAFKNRNYTVKYEVNWKTHEIKVKGQN
Expression Region:
30-315aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
48.6 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:
Microbiology
Function:
Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity (By similarity).
Involvement in disease:
Relevance:
Toxin that seems to act by forming pores in the membrane of the cell. Has a hemolytic and a leucotoxic activity
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:
Aerolysin family
Reference:
"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance."Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004)
