Matrix metalloproteinase-9 (Protein name
), MMP9_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 (3)
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Gene name:
MMP9(CLG4B);
Protein name:
Matrix metalloproteinase-9(MMP-9);
Alternative:
92 kDa type IV collagenase;92 kDa gelatinase;Gelatinase B(GELB);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.
Function:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
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Precision
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: ≤3.5
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: ≤7.0
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Recovery
Recovery was determined by spiking various levels of Human MMP9 into Human serum, plasma and cell culture media.
Sample Type
Average(%)
Recovery Range (%)
Serum
95
81-104
Plasma
96
89-102
Cell culture media
90
84-99
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Linearity
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 20-37;VARIANTS ARG-279 AND PRO-574
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA];VARIANT PRO-574
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS VAL-20; LYS-127; ARG-279; PRO-574 AND GLN-668
5.
NIEHS SNPs program
Submitted (2005-09) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS VAL-20; HIS-239; VAL-571; PRO-574 AND GLN-668
[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 ARG-279 AND PRO-574
[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 20-34; 60-71 AND 107-118;INDUCTION;PROTEOLYTIC PROCESSING BY MMP3
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Cited for: PROTEIN SEQUENCE OF 20-32 AND 94-111;PROTEOLYTIC PROCESSING;INDUCTION
[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 20-27; 60-67; 94-101 AND 107-113
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Cited for: PROTEIN SEQUENCE OF 93-115;FUNCTION;CATALYTIC ACTIVITY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-444 IN COMPLEX WITH ZINC AND MAGNESIUM IONS
[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 (2.1 ANGSTROMS) OF 107-215 IN COMPLEX WITH INHIBITOR; ZINC AND CALCIUM IONS;MUTAGENESIS OF GLU-402
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Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 513-707;SUBUNIT
28.
"Theoretical model of human type IV collagenase precursor." Mallena S.C.
,
Sagajkar R.D.
Submitted (2002-04) to the PDB data bank
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Cited for: 3D-STRUCTURE MODELING