Human MMP-9 ELISA Kit | MMP-9 elisa kit

Human MMP-9 ELISA KIT

Cat. Num. AAA9424837

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Reactivity: Human
• Synonyms: MMP-9; Human MMP-9 ELISA KIT; Human MMP-9; MMP-9 elisa kit

• Reactivity: Human
• Specificity: Natural and recombinant Human MMP-9 Ligand

• Assay Type: Solid Phase Sandwich ELISA
• Samples: Cell culture supernatant, serum, plasma (EDTA, citrate, heparin)
• Detection Range: 62.5-4000pg/mL
• Sensitivity: 31pg/mL
• Assay Time: 3 hours
• Sample Volume: 20 uL
• Detection Method: Colorimetric
• Preparation and Storage: Store at 4 degree C

Typical Testing Data/Standard Curve (for reference only)

(Representative standard curve for MMP-9 ELISA. MMP-9 was diluted in serial two-fold steps in Sample Diluent.)

Related Product Information for MMP-9 elisa kit

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade extracellular matrix proteins (1 - 3). They are secreted as zymogens (Pro-MMPs) that are activated by a variety of proteinases or by reaction with organic mercurials. They are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs) and by 2-macroglobulin (3 - 6). The regulation of MMP activity is important in tissue remodeling, inflammation, tumor growth and metastasis (3, 7 - 9).Human MMP-9 (also known as gelatinase B) is secreted as a 92 kDa zymogen (2, 3). Cleavage of Pro-MMP-9 at or near residue 87 results in the active enzyme with a mass of approximately 82 kDa (1). MMP-9 has three fibronectin type II domains, a hemopexin-like domain and a proline-rich type V collagen-homologous domain (1 - 3). Pro-MMP-9 can be activated by MMP-3 (5) or by certain bacterial proteinases (10). MMP-9 is inhibited bya2-macroglobulin or by TIMP-1 (3 - 6), which binds to Pro-MMP-9 as well as to active MMP-9 (3). In vitro treatment of Pro-MMP-9 with 4-aminophenylmercuric acid (APMA) produces not only the 82 kDa active enzyme but also a C-terminal truncated form of approximately 65 kDa with the activity comparable to that of the 82 kDa form (11).Pro-MMP-9 is secreted by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts, chondrocytes, skeletal muscle satellite cells, endothelial cells, and various tumor cells (1, 7- 21). Pro-MMP-9 expression is upregulated by TGF-b1, IL-1b, TGF-a, PDGF-AB, TNF-a, and IL-1a (7, 15, 17). Substrates for MMP-9 include denatured collagen type I (gelatin), native collagens type IV, V, VII, X and XI, fibrinogen, vitronectin, IL-1b, and entactin, a molecule that bridges laminin and type IV collagen (3, 4, 6, 13, 21 - 23).

NCBI and Uniprot Product Information

• NCBI GI #: 74272287
• NCBI GeneID: 4318
• NCBI Accession #: NP_004985.2
• NCBI GenBank Nucleotide #: NM_004994.2
• UniProt Accession #: P14780; Q3LR70; Q8N725; Q9H4Z1; Q9UCJ9; Q9UCL1; Q9UDK2; B2R7V9
• Molecular Weight: 78,458 Da
• NCBI Official Full Name: matrix metalloproteinase-9 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 9
• NCBI Official Symbol: MMP9
• NCBI Official Synonym Symbols: GELB; CLG4B; MMP-9; MANDP2
• NCBI Protein Information: matrix metalloproteinase-9
• UniProt Protein Name: Matrix metalloproteinase-9
• UniProt Gene Name: MMP9
• UniProt Synonym Gene Names: CLG4B; MMP-9; GELB

NCBI Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]

Uniprot Description

MMP9: 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. 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. Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Produced by normal alveolar macrophages and granulocytes. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Belongs to the peptidase M10A family.

Protein type: EC 3.4.24.35; Motility/polarity/chemotaxis; Protease; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 20q13.12

Cellular Component: extracellular region; extracellular space

Molecular Function: collagen binding; endopeptidase activity; identical protein binding; metalloendopeptidase activity; metallopeptidase activity; protein binding; serine-type endopeptidase activity; zinc ion binding

Biological Process: collagen catabolic process; ephrin receptor signaling pathway; extracellular matrix disassembly; macrophage differentiation; negative regulation of apoptosis; neutrophil degranulation; positive regulation of cell migration; positive regulation of DNA binding; positive regulation of epidermal growth factor receptor signaling pathway; positive regulation of keratinocyte migration; positive regulation of protein amino acid phosphorylation; proteolysis

Disease: Metaphyseal Anadysplasia 2