CLG4B; GELB; 92 kDa gelatinase; matrix metallopeptidase 9

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 20; NC_000020.10 (44637547..44645200). Location: 20q11.2-q13.1

Monoclonal

IgG1

4A3

Mouse

Protein A/G Chromatography

Provided as solution in phosphate buffered saline with 0.08% sodium azide

Product should be stored at -20 degree C. Aliquot to avoid freeze/thaw cycles

Small volumes of anti-MMP9 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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.

Monoclonal Antibody; Extracellular Matrix

Western Blot (WB), Immunohistochemistry (IHC) Paraffin

Left: Immunohistochemical staining of paraffin embedded esophageal tumors using Act-MMP9 antibody .

63 kDa

matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)

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)

Matrix metalloproteinase-9

CLG4B; MMP-9; GELB??[Similar Products]

MMP9_HUMAN

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]

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.

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