ELISA/assay

MMP-9 Human ELISA Kit

MBS355257

96 Tests

465 USD

ELISA Kit

MMP-9 Human ELISA Kit

[MMP-9]

[Human MMP-9]

[matrix metalloproteinase-9 preproprotein; Matrix metalloproteinase-9; 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 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; MMP-9; GELB]

MMP9_HUMAN

Human

Store at 2-8 degree C for 4 months, or at -20 degree C for 8 months.

Quantitative sELISA (EIA)

For quantitative detection of MMP-9 in Human serum, plasma, body fluids, tissue lysates or cell culture supernatants.

Typical Testing Data/Standard Curve (for reference only)

Samples: Tissue Lysates Or Cell Culture Supernates, Human Serum And Plasma Should Be Validated By End Users. Assay Type: Sandwich. Detection Range: 62.5 pg/ml-4000 pg/ml. Sensitivity: < 10pg/ml

Principle of the Assay: This kit was based on sandwich enzyme-linked immune-sorbent assay technology. Anti-M-CSF polyclonal antibody was pre-coated onto 96-well plates. And the biotin conjugated anti-M-CSF polyclonal antibody was used as detection antibodies. The standards, test samples and biotin conjugated detection antibody were added to the wells subsequently, and wash with wash buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with wash buffer. TMB substrates were used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the M-CSF amount of sample captured in plate. Read the O.D. absorbance at 450nm in a microplate reader, and then the concentration of M-CSF can be calculated!!Background/Introduction: Macrophage colony-stimulating factor, or M-CSF, is a secreted cytokine which influences hematopoietic stem cells to differentiate into macrophages or other related cell types. Ladner et al. (1987) showed that there are 2 forms of M-CSF, with 224 and 522 amino acids, resulting from alternative splicing. It is a hematopoietic growth factor that is involved in the proliferation, differentiation, and survival of monocytes, macrophages, and bone marrow progenitor cells. It released by osteoblasts (as a result of endocrine stimulation by parathyroid hormone) exerts paracrine effects on osteoclasts. M-CSF binds to receptors on osteoclasts inducing differentiation, and ultimately leading to increased plasma calcium levels—through the resorption (breakdown) of bone. More recently, it was discovered that CSF-1 and its receptor CSF1R are implicated in the mammary gland during normal development and neoplastic growth.

74272287

NP_004985.2

NM_004994.2

P14780

78,458 Da

AGE/RAGE Pathway (698754); Activation Of Matrix Metalloproteinases Pathway (576264); Angiogenesis Pathway (198772); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (730306); Bladder Cancer Pathway (83115); Bladder Cancer Pathway (527); CXCR4-mediated Signaling Events Pathway (137910); Collagen Formation Pathway (645288); Degradation Of Collagen Pathway (730309); Degradation Of Collagen Pathway (827690)

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.

96 Tests

465 USD