Mouse anti-Human Matrix Metalloproteinase 9 (MMP9) Monoclonal Antibody | anti-MMP9 antibody

Matrix Metalloproteinase 9 (MMP9)

Cat. Num. AAA395259

• Gene Names: MMP9; GELB; CLG4B; MMP-9; MANDP2
• Reactivity: Human
• Applications: Western Blot, Immunohistochemistry
• Purity: Protein A/G Chromatography
• Synonyms: Matrix Metalloproteinase 9 (MMP9); Monoclonal Antibody; CLG4B; GELB; 92 kDa gelatinase; matrix metallopeptidase 9; anti-MMP9 antibody

• Host: Mouse
• Reactivity: Human
• Clonality: Monoclonal
• Isotype: IgG1
• Clone Number: 2C3
• Purity/Purification: Protein A/G Chromatography
• Form/Format: Provided as solution in phosphate buffered saline with 0.08% sodium azide
• Sequence Length: 707

• Applicable Applications for anti-MMP9 antibody: Western Blot (WB), Immunohistochemistry (IHC) Paraffin
• Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP9 protein and mouse myeloma Ag8563 cells.
• Positive Control: Colon, oesophageal and gastric tissues. Stronger expression in tumor versus normal tissue.
• Preparation and Storage: Product should be stored at -20 degree C. Aliquot to avoid freeze/thaw cycles

Immunohistochemistry (IHC)

(Left: Immunohistochemical staining of paraffin embedded colon carcinoma using MMP9 antibody . Antigen retreival using 10mM citrate buffer and microwave method was used.)

Related Product Information for anti-MMP9 antibody

The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92-kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Product Categories/Family for anti-MMP9 antibody

Monoclonal Antibody; Extracellular Matrix

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: 92 kDa
• NCBI Official Full Name: matrix metalloproteinase-9 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
• NCBI Official Symbol: MMP9
• NCBI Official Synonym Symbols: GELB; CLG4B; MMP-9; MANDP2
• NCBI Protein Information: matrix metalloproteinase-9; 92 kDa gelatinase; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
• UniProt Protein Name: Matrix metalloproteinase-9
• Protein Family: Matrix metalloproteinase
• UniProt Gene Name: MMP9
• UniProt Synonym Gene Names: CLG4B; MMP-9; GELB
• UniProt Entry Name: MMP9_HUMAN

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

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. Ref.16

Catalytic activity: Cleavage of gelatin types I and V and collagen types IV and V. Ref.16

Cofactor: Binds 2 zinc ions per subunit.Binds 3 calcium ions per subunit.

Enzyme regulation: Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Ref.19 Ref.21

Subunit structure: 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. Ref.18 Ref.21 Ref.27

Subcellular location: Secreted › extracellular space › extracellular matrix

Probable.

Tissue specificity: Produced by normal alveolar macrophages and granulocytes.

Induction: Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Ref.11 Ref.12 Ref.19 Ref.21 Ref.24

Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification: Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.N- and O-glycosylated. Ref.9

Involvement in disease: Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.22Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous: In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.

Sequence similarities: Belongs to the peptidase M10A family.Contains 3 fibronectin type-II domains.Contains 4 hemopexin repeats.