CCS CLIA Kit for Human(Homo sapiens) | EIAab.comCCS CLIA Kit for Human(Homo sapiens)

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Index > Protein center > CCS(Gene name) > Human

CCS (Gene name),

Copper chaperone for superoxide dismutase (Protein name ), CCS_HUMAN from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

Related Databases

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Gene name:

CCS;

Protein name:

Copper chaperone for superoxide dismutase;

Alternative:

Superoxide dismutase copper chaperone;

Organism:

Human (Homo sapiens).

General Annotation

Sub Unit:

Homodimer, and heterodimer with SOD1. Interacts with COMMD1.

Function:

Delivers copper to copper zinc superoxide dismutase (SOD1).

Subcellular Location:

Cytoplasm

Protein Attributes:

Sequence length:

274

Sequence:

50:

100:

150:

200:

250:

274:

IWEERGRPIA | GKGRKESAQP | PAHL

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

String:

O14618

KEGG:

hsa:9973

UniGene:

Hs.502917

Pfam:

PF00403

MIM:

603864

SMR:

O14618

STRING:

9606.ENSP00000307870

Uniprot:

O14618

FOR

ELISA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

E8880r

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96T

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ELISA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

E8880p

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Packing:

96T

ELISA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

E8880h

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Packing:

96T

ELISA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

E8880m

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Packing:

96T

CLIA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

U8880h

Price:

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MSDS:

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Packing:

96T

CLIA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

U8880r

Price:

Please sign in first.

MSDS:

Please sign in first.

Packing:

96T

CLIA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

U8880m

Price:

Please sign in first.

MSDS:

Please sign in first.

Packing:

96T

CLIA Kit for Human Copper chaperone for superoxide dismutase

Cat.:

U8880p

Price:

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MSDS:

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Packing:

96T

Polyclonal Antibody for Human Copper chaperone for superoxide dismutase

Cat.:

P8880Rb-m

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Packing:

40ug/0.2ml

Polyclonal Antibody for Human Copper chaperone for superoxide dismutase

Cat.:

P8880Rb-h

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Packing:

40ug/0.2ml

Polyclonal Antibody for Human Copper chaperone for superoxide dismutase

Cat.:

P8880Rb-r

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Packing:

40ug/0.2ml

Monoclonal Antibody for Human Copper chaperone for superoxide dismutase

Protein for Human Copper chaperone for superoxide dismutase

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

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Linearity

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References

1.

"The copper chaperone for superoxide dismutase."
Culotta V.C. , Klomp L.W. , Strain J. , Casareno R.L.B. , Krems B. , Gitlin J.D.
J. Biol. Chem.272:23469-23472(1997) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
2.

"Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants."
Banci L. , Cantini F. , Kozyreva T. , Rubino J.T.
ChemBioChem14:1839-1844(2013) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 1-85;COPPER-BINDING SITES;SUBUNIT
3.

"Human macrophage copper chaperone for superoxide dismutase (CCS), full length mRNA sequence."
Bhat K.S.
Submitted (2002-05) to the EMBL/GenBank/DDBJ databases

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
4.

"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A. , Ebert L. , Mkoundinya M. , Schick M. , Eisenstein S. , Neubert P. , Kstrang K. , Schatten R. , Shen B. , Henze S. , Mar W. , Korn B. , Zuo D. , Hu Y. , LaBaer J.
Submitted (2004-06) to the EMBL/GenBank/DDBJ databases

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
5.

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
tissue: Brain.
6.

"The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase."
Casareno R.L.B. , Waggoner D. , Gitlin J.D.
J. Biol. Chem.273:23625-23628(1998) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBUNIT;SUBCELLULAR LOCATION
7.

"Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface."
Stasser J.P. , Eisses J.F. , Barry A.N. , Kaplan J.H. , Blackburn N.J.
Biochemistry44:3143-3152(2005) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: MUTAGENESIS OF CYS-22; CYS-25; CYS-244 AND CYS-246;METAL-BINDING
8.

"Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1."
Vonk W.I. , Wijmenga C. , Berger R. , van de Sluis B. , Klomp L.W.
J. Biol. Chem.285:28991-29000(2010) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH COMMD1
9.

"Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination."
Brady G.F. , Galban S. , Liu X. , Basrur V. , Gitlin J.D. , Elenitoba-Johnson K.S. , Wilson T.E. , Duckett C.S.
Mol. Cell. Biol.30:1923-1936(2010) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: UBIQUITINATION AT LYS-76; LYS-189; LYS-216 AND LYS-241 BY XIAP/BIRC4;INTERACTION WITH XIAP/BIRC4
10.

"Initial characterization of the human central proteome."
Burkard T.R. , Planyavsky M. , Kaupe I. , Breitwieser F.P. , Buerckstuemmer T. , Bennett K.L. , Superti-Furga G. , Colinge J.
BMC Syst. Biol.5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
11.

"Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase."
Huppke P. , Brendel C. , Korenke G.C. , Marquardt I. , Donsante A. , Yi L. , Hicks J.D. , Steinbach P.J. , Wilson C. , Elpeleg O. , Moller L.B. , Christodoulou J. , Kaler S.G. , Gartner J.
Hum. Mutat.33:1207-1215(2012) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SOD1;VARIANT TRP-163;CHARACTERIZATION OF VARIANT TRP-163
12.

"Crystal structure of the second domain of the human copper chaperone for superoxide dismutase."
Lamb A.L. , Wernimont A.K. , Pufahl R.A. , O'Halloran T.V. , Rosenzweig A.C.
Biochemistry39:1589-1595(2000) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 84-237 IN COMPLEX WITH ZINC;SUBUNIT;DISULFIDE BOND
13.

"The apo form of HMA domain of copper chaperone for superoxide dismutase."
RIKEN structural genomics initiative (RSGI)
Submitted (2005-11) to the PDB data bank

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 1-87

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