ELISA/assay

Guinea Pig matrix metalloproteinase 9, MMP-9 ELISA Kit

MBS703033

96 Strip Wells

725 USD

ELISA Kit

Guinea Pig matrix metalloproteinase 9, MMP-9 ELISA Kit

pig matrix metalloproteinase 9, MMP-9

guinea pig matrix metalloproteinase 9; MMP-9 ELISA Kit; pig matrix metalloproteinase 9; 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; GELB

MMP-9

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

MMP9_HUMAN

Guinea Pig

707

Unopened test kits should be stored at 2 to 8 degree C upon receipt. Please refer to pdf manual for further storage instructions.

Detection Wavelength: 450 nm

Sample Volume: 50-100ul

Introduction: 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. Thrombospondins, intervertebral disc proteins, regulate the effective levels of matrix metalloproteinases (MMPs) 2 and 9, which are key effectors of ECM remodeling. Principle of the Assay: The microtiter plate provided in this kit has been pre-coated with an antibody specific to MMP-9. Standards or samples are then 3 added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific for MMP-9 and Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. Then a TMB (3,3',5,5' tetramethyl-benzidine) substrate solution is added to each well. Only those wells that contain MMP-9, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of a sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450 nm +/- 2 nm. The concentration of MMP-9 in the samples is then determined by comparing the O.D. of the samples to the standard curve.

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!!Axon Guidance Pathway 105688!!Bladder Cancer Pathway 83115!!Bladder Cancer Pathway 527!!CXCR4-mediated Signaling Events Pathway 137910!!Collagen Degradation Pathway 730309!!Collagen Formation Pathway 645288

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.1 PublicationManual assertion based on experiment in:Ref.16. Catalytic activity: Cleavage of gelatin types I and V and collagen types IV and V.1 PublicationManual assertion based on experiment in:Ref.16. Cofactor: Binds 2 zinc ions per subunit. Enzyme regulation: Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1.2 PublicationsManual assertion based on experiment in:Ref.19

96 Strip Wells

725 USD