Protein name:
Complement component C8 gamma chain ;
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
C8 is composed of three chains: alpha, beta and gamma. The alpha and gamma chains are disulfide bonded.
Function:
C8 is a constituent of the membrane attack complex. C8 binds to the C5B-7 complex, forming the C5B-8 complex. C5-B8 binds C9 and acts as a catalyst in the polymerization of C9. The gamma subunit seems to be able to bind retinol.
Subcellular Location:
Secreted
Protein Attributes:
50:
MLPPGTATLL | TLLLAAGSLG | QKPQRPRRPA | SPISTIQPKA | NFDAQQFAGT |
100:
WLLVAVGSAC | RFLQEQGHRA | EATTLHVAPQ | GTAMAVSTFR | KLDGICWQVR |
150:
QLYGDTGVLG | RFLLQARDAR | GAVHVVVAET | DYQSFAVLYL | ERAGQLSVKL |
200:
YARSLPVSDS | VLSGFEQRVQ | EAHLTEDQIF | YFPKYGFCEA | ADQFHVLDEV |
Vaild Sequence:
Related Databases
Uniprot:
ELISA Kit
CLIA Kit
Polyclonal Antibody
Monoclonal Antibody
Protein
FOR
Human
Mouse
Rabbit
ELISA Kit for Human Complement component C8 gamma chain
ELISA Kit for Human Complement component C8 gamma chain
ELISA Kit for Human Complement component C8 gamma chain
CLIA Kit for Human Complement component C8 gamma chain
CLIA Kit for Human Complement component C8 gamma chain
CLIA Kit for Human Complement component C8 gamma chain
Polyclonal Antibody for Human Complement component C8 gamma chain
Polyclonal Antibody for Human Complement component C8 gamma chain
Polyclonal Antibody for Human Complement component C8 gamma chain
Monoclonal Antibody for Human Complement component C8 gamma chain
Monoclonal Antibody for Human Complement component C8 gamma chain
Monoclonal Antibody for Human Complement component C8 gamma chain
Protein for Human Complement component C8 gamma chain
Protein for Human Complement component C8 gamma chain
Protein for Human Complement component C8 gamma chain
R&D Technical Data
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Precision
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Recovery
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Linearity
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References
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Cited for : NUCLEOTIDE SEQUENCE [MRNA];PARTIAL PROTEIN SEQUENCE;PYROGLUTAMATE FORMATION AT GLN-21;VARIANT GLY-118
2.
[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];VARIANT GLY-118
tissue :
Liver .
3.
[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 [GENOMIC DNA];VARIANT GLY-118
tissue :
Blood .
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[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 GENOMIC DNA]
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Submitted (2005-07) 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 GENOMIC DNA];VARIANT GLY-118
6.
[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];VARIANTS GLY-118 AND ASN-124
tissue :
Colon .
7.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : SIMILARITY TO LIPOCALINS
8.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : DISULFIDE BONDS;RETINOL-BINDING;3D-STRUCTURE MODELING
9.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for : REVIEW
10.
[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 (1.2 ANGSTROMS) OF 21-202;DISULFIDE BOND
11.
[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 (1.5 ANGSTROMS) OF 21-202;DISULFIDE BOND
12.
[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 (1.81 ANGSTROMS) OF 30-202;DISULFIDE BOND