Rabbit Polyclonal MMP10 Antibody

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     Red: Control Antigen (100ng); Purple: Antigen (10ng); Green: Antigen (50ng); Blue: Antigen (100ng);    

  
  

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     Immunofluorescence analysis of HepG2 cells using ApoB mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor-555 phalloidin.    

  
  

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     Flow cytometric analysis of serun using ApoB mouse mAb (green) and negative control (purple).    

  
  

Matrix metalloproteinase 10 (MMP10), also known as stromelysin-2. is a member of the MMP family of zinc-dependent endopeptidases that regulate extracellular matrix (ECM) remodeling. It is secreted as an inactive zymogen and activated via proteolytic cleavage, enabling its enzymatic function. MMP10 primarily targets substrates such as collagen, proteoglycans, and glycoproteins, playing roles in tissue repair, inflammation, and cellular signaling. Unlike broader-spectrum MMPs, MMP10 exhibits substrate specificity linked to processes like wound healing and epithelial regeneration.

In pathological contexts, MMP10 is implicated in chronic inflammatory diseases (e.g., arthritis, atherosclerosis), fibrosis, and cancer progression. Overexpression in tumors correlates with enhanced invasion, angiogenesis, and metastasis by degrading ECM barriers and modulating cytokine activity.

MMP10 antibodies are essential tools for detecting and quantifying MMP10 expression in research and diagnostics. These antibodies enable techniques like Western blotting, immunohistochemistry, and ELISA to study MMP10 localization, regulation, and activity in tissues or biofluids. Specific monoclonal or polyclonal antibodies help identify MMP10's role in disease mechanisms, aiding therapeutic target validation. Recent studies also explore MMP10 as a biomarker for conditions like chronic obstructive pulmonary disease (COPD) and certain cancers. However, cross-reactivity with other MMPs requires careful antibody validation to ensure specificity in experimental models.