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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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48-602MAG
Buffer Detection Kit for Magnetic Beads
1 Kit
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AB6001
Sigma-AldrichAnti-MMP-9 Antibody, NT
Anti-MMP-9 Antibody, N-terminus is an antibody against MMP-9 for use in WB.
More>>Anti-MMP-9 Antibody, N-terminus is an antibody against MMP-9 for use in WB. Less<<
Anti-MMP-9 Antibody, NT: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
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.
References
Product Information
Format
Affinity Purified
HS Code
3002 15 90
Control
HL-60 plus PMA conditioned media
Presentation
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4, 150 mM NaCl) with 0.05% sodium azide.
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.
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)
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
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
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Relapse to cocaine use necessitates remodeling excitatory synapses in the nucleus accumbens and synaptic reorganization requires matrix metalloproteinase (MMP) degradation of the extracellular matrix proteins. We found enduring increases in MMP-2 activity in rats after withdrawal from self-administered cocaine and transient increases in MMP-9 during cue-induced cocaine relapse. Cue-induced heroin and nicotine relapse increased MMP activity, and increased MMP activity was required for both cocaine relapse and relapse-associated synaptic plasticity.
