antibody

Rabbit anti MMP-9 Polyclonal antibody

MBS462084

0.1 mg

340 USD

polyclonal

rabbit

nonconjugated

human, mouse, rat, dog, chicken

western blot, ELISA, immunohistochemistry

Antibody

Rabbit anti MMP-9 Polyclonal antibody

MMP-9

Rabbit anti-MMP-9; Matrix Metalloproteinase 9 (MMP-9); Gelatinase B; 92 kDa type IV collagenase

matrix metalloproteinase-9 preproprotein; Matrix metalloproteinase-9; matrix metalloproteinase-9; 92 kDa gelatinase; OTTHUMP00000031674; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B

MMP-9

MMP9; MMP9; GELB; CLG4B; MMP-9; MANDP2; CLG4B

MMP9_HUMAN

Polyclonal

Rabbit

Human, Rat, Mouse, Chicken, Canine

This antibody recognizes ~92 kDa of human MMP-9 protein. The other species are not tested.

The Rabbit IgG is purified by Epitope Affinity Purification.

This affinity purified antibody is supplied in sterile Phosphate buffered saline (pH7.2) containing antibody stabilizer

Size: 100 ug/200 ul

The antibodies are stable for 12 months from date of receipt when stored at -20 degree C to -70 degree C. The antibodies can be stored at 2 degree C -8 degree C for three month without detectable loss of activity. Avoid repeated freezing-thawing cycles.

ELISA, Western Blot, Immunohistochemistry

Western Blot: 0.1-1 ug/ml. ELISA: 0.01-0.1 ug/ml. Immunoprecipitation: 2-5 ug/ml. Immunohistochemistry: 2-5 ug/ml

Antigen Preparation: A synthetic peptide corresponding to the hinge of human MMP-9. This sequence is identical among human, rat, mouse, chicken, dog and bovine.

Positive Control: A431. Cellular Location: Cytoplasmic and extracellular matrix

Matrix metalloproteinases (MMPs) belong to a family of proteinases that target many extracellular matrix proteins including additional proteinases, growth factors, cell surface receptors and adhesion molecules. MMPs contain common domain structures that include a signal sequence, a propeptide, a catalytic domain, and a hemopexin-like (Hpx) domain. The MMP activity requires proteolytic cleavage of MMPs in order to generate activie MMPs by release of the inhibitory propeptide domain from the whole molecules. MMP-2, MMP-3, MMP-7, MMP-9 and MMP-13 have been characterized as important factors for normal tissue remodeling during embryo development and wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis. MMP activities are correlated with cancer metastatic process.MMP-2 and MMP-9, gelatinases, degrade basement membrane collagen.

Brigitte Lelongt, et al. Matrix Metalloproteinases MMP2 and MMP9 Are Produced in Early Stages of Kidney Morphogenesis but Only MMP9 Is Required for Renal Organogenesis In Vitro. J. Cell Biol. 1997. 136 (6), 1363-1373.

74272287

NP_004985.2

NM_004994.2

P14780

92 kDa

Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); CXCR4-mediated Signaling Events Pathway (137910); Endochondral Ossification Pathway (198812); FGF Signaling Pathway (137989); IL-3 Signaling Pathway (198881); LPA Receptor Mediated Events Pathway (137928); Leukocyte Transendothelial Migration Pathway (83083); Leukocyte Transendothelial Migration Pathway (494); Matrix Metalloproteinases Pathway (198900)

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]

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: Defects in MMP9 may be a cause of susceptibility to intervertebral disc disease (IDD) [. MIM:603932]; also known as lumbar disk herniation (LDH). IDD is one of the most common musculo-skeletal disorders and the predominant cause of low-back pain and unilateral leg pain. Ref.22Defects in MMP9 are the cause of metaphyseal anadysplasia type 2 (MANDP2) [. MIM:613073]. Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, 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. 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.

0.1 mg

340 USD