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Home > Products > Recombinant Proteins > Recombinant Human CCS Protein, with Cu (I)

Recombinant Human CCS Protein, with Cu (I)

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GST(1)
His(5)
Cat.No.:
CCS-483H
Product Overview:
Recombinant full length Human Cu (I)-CCS (aa 1-274)(Copper chaperone for superoxide dismutase) with a GSFT sequence at N-terminal was expressed in E. coli. Binding of 2 Cu (I) to the protein was confirmed by ICP.
Description:
Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
Source:
E. coli
Species:
Human
Form:
In 20 mM Phosphate buffer pH 7.0.
Molecular Mass:
29.4 kDa
Protein length:
aa 1-274
AA Sequence:
GMSF-MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTMM CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL
Purity:
>95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight > 25 kDa and < 35 kDa.
Notes:
To avoid oxidation and leaking of the Cu(I) bound to the protein, keep and use the sample under inert atomosphere.
Storage:
Store at - 20 centigrade. The protein is stable at 4 centigrade for at least 2 weeks and at 25 centigrade for at least several hours. After initial deforst, aliquot product into individual tubes under inert atomosphere and refreeze at - 20 centigrade. Avoid repeated freeze/defrost cycles. Avoid exposition to air.
Concentration:
1 mg/ml


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Optional requirements on this protein +Expand
C-fusion   N-fusion  Non-tagged
His   GST  Fc  Others
<1.0 eu/μg   <0.1 eu/μg  <0.01 eu/μg  Not required
Monomer Isolation   Dimer Isolation   Not required
>80% by SDS-PAGE   >90% by SDS-PAGE  >95% by SDS-PAGE  Others
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45-1 Ramsey Road, Shirley, NY 11967, USA
USA: 1-631-559-9269  1-631-448-7888
Europe: 44-207-048-3343
FAX: 1-631-938-8127
EMAIL: info@creative-biomart.com

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