Metalloproteinase inhibitor 1 (Protein name
), TIMP1_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Related Databases
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Citations (1)
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Gene name:
TIMP1(CLGI;TIMP);
Protein name:
Metalloproteinase inhibitor 1;
Alternative:
Fibroblast collagenase inhibitor(Collagenase inhibitor);Erythroid-potentiating activity(EPA);Tissue inhibitor of metalloproteinases 1(TIMP-1);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
N/A
Function:
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16. Does not act on MMP-14.
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12% SDS-PAGE Analysis
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Precision
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Intra-assay Precision (Precision within an assay):Three samples of known concentration were tested twenty times on one plate to assess intra-assay precision.
Intra-Assay CV: ≤ 5.8%
Inter-assay Precision (Precision between assays):Three samples of known concentration were tested in five separate assays to assess inter-assay precision.
Inter-Assay CV: ≤ 8.9%
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Recovery
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Recovery was determined by spiking various levels of ACE into serum and plasma .
Sample Type
Average(%)
Recovery Range(%)
Serum
99
92-105
Plasma
98
91-106
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Linearity
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The linearity of the kit was assayed by testing samples spiked with appropriate concentration of ACE and their serial dilutions. The results were demonstrated by the percentage of calculated concentration to the expected.
Sample
1:2
1:4
1:8
1:16
serum(n=5)
90-103%
91-104%
94-102%
92-105%
EDTA plasma(n=5)
91-97%
93-102%
89-105%
91-106%
heparin plasma(n=5)
92-104%
94-108%
95-109%
91-107%
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 24-51;FUNCTION;SUBCELLULAR LOCATION;GLYCOSYLATION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 24-49;SUBCELLULAR LOCATION;GLYCOSYLATION;FUNCTION
[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];PROTEIN SEQUENCE OF 24-207;DISULFIDE BOND;SUBCELLULAR LOCATION;GLYCOSYLATION
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 24-38;SUBCELLULAR LOCATION;TISSUE SPECIFICITY;FUNCTION
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: FUNCTION AS A GROWTH FACTOR AND PROTEASE INHIBITOR;INTERACTION WITH MMP3;SUBCELLULAR LOCATION;MUTAGENESIS OF HIS-30 AND GLN-32
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-101
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION IN A COMPLEX WITH CD63 AND ITGB1
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Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP3;INTERACTION WITH MMP3
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Cited for: STRUCTURE BY NMR OF 24-149 IN COMPLEX WITH MMP3;INTERACTION WITH MMP3
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Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 24-149 IN COMPLEX WITH MMP1;FUNCTION;INTERACTION WITH MMP1 AND MMP3;DISULFIDE BOND;MUTAGENESIS OF THR-25
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Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-148 OF MUTANT LEU-121 IN COMPLEX WITH MMP14;FUNCTION;INTERACTION WITH MMP14;DISULFIDE BOND;MUTAGENESIS OF THR-121
[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 (1.90 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP10;FUNCTION;INTERACTION WITH MMP10;DISULFIDE BOND