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Key Specifications Table
| Species Reactivity | Key Applications | Host | Format | Antibody Type |
|---|---|---|---|---|
| H, R, Mk, Pm, Eq, Ca, Po | WB | Rb | Affinity Purified | Polyclonal Antibody |
| Description | |
|---|---|
| Catalogue Number | AB6001 |
| Replaces | AB805 |
| Description | Anti-MMP-9 Antibody, NT |
| Alternate Names |
|
| Background Information | All cells within tissues are surrounded by an extracellular matrix (ECM) giving the tissues shape and structure. The ECM is constantly being remodeled and constant communication is maintained between cells through this matrix. Secreted proteins, termed matrix metalloproteinases (MMPs), are involved in the modulation of cell matrix interactions. MMPs are Zn2+ binding endopeptidases that degrade various components of the ECM. MMPs are enzymes implicated in normal and pathologic tissue remodeling processes, wound healing, angiogenesis, and tumor invasion. These enzymes are very potent when active, and are associated with extracellular space inhibitors called TIMPs (tissue inhibitors of matrix metalloproteinases). MMP9, also known as gelatinase B, is a secreted enzyme which degrades the interstitial collagens, types I, II, and III and is produced by normal alveolar macrophages and granulocytes. |
| Product Information | |
|---|---|
| Format | Affinity Purified |
| Control |
|
| Presentation | Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide. |
| Quality Level | MQ100 |
| Applications | |
|---|---|
| Application | Anti-MMP-9 Antibody, N-terminus is an antibody against MMP-9 for use in WB. |
| Key Applications |
|
| Biological Information | |
|---|---|
| Immunogen | KLH-conjugated synthetic peptide corresponding to the N-terminus of MMP-9. |
| Epitope | N-terminus |
| Concentration | Please refer to the Certificate of Analysis for the lot-specific concentration. |
| Host | Rabbit |
| Specificity | The antibody recognizes human MMP-9. It does not cross react with MMP-1 or MMP-2. |
| Species Reactivity |
|
| Species Reactivity Note | Human. Predicted to react with rat, monkey, primate, horse, dog, and pig based on 100% sequence homology. |
| Antibody Type | Polyclonal Antibody |
| Entrez Gene Number |
|
| Entrez Gene Summary | 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 MMPs 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] |
| Gene Symbol |
|
| Purification Method | Antigen Affinity Purified |
| UniProt Number |
|
| UniProt Summary | 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. CATALYTIC ACTIVITY: Cleavage of gelatin types I and V and collagen types IV and V. Cofactor Binds 2 zinc ions per subunit. Binds 3 calcium ions per subunit. ENZYME REGULATION: Inhibited by histatin-3 1/24 (histatin-5). SUBUNIT STRUCTURE: Exists as monomer, disulfide-linked homodimer, and as a heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. SUBCELLUAR LOCATION: Secreted › extracellular space › extracellular matrix Probable. TISSUE SPECIFICTY: Produced by normal alveolar macrophages and granulocytes. INDUCTION: Activated by 4-aminophenylmercuric acetate and phorbol ester. 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. PTM: 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. INVOLVEMENT IN DISEASE: Defects in MMP9 may be a cause of susceptibility to lumbar disk herniation (LDH) [MIM:603932]. LDH is the predominant cause of low-back pain and unilateral leg pain. 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-like domains. |
| Molecular Weight | 92kDa (pro-form) and 88kDa (active form) |
| Product Usage Statements | |
|---|---|
| Quality Assurance | Evaluated on a representative lot by Western blot using an HL-60 cell lysate supplemented with a PMA conditioned media. Western Blot Analysis: 0.5 µg/ml of this antibody detected MMP-9 on 10 µg of HL-60 plus PMA conditioned media. |
| Usage Statement |
|
| Storage and Shipping Information | |
|---|---|
| Storage Conditions | Stable for 1 year at 2-8°C from date of receipt. |
| Packaging Information | |
|---|---|
| Material Size | 100 µg |