Laminin P1 Fragment Rat Monoclonal Antibody [Clone ID: MEC5]

CAT#: AM32792SU-N

Laminin P1 Fragment rat monoclonal antibody, clone MEC5, Supernatant

Specifications

Product Data

• Clone Name: MEC5
• Applications: IHC
• Recommended Dilution: MEC5 monoclonal antibodies are suitable for Immunohistochemical detection of Laminin in extracellular matrix or basement membranes in freshly frozen tissue sections of Rat, Mouse, or Humans. It is recommended to pretreat the sections with pepsin.
• Reactivities: Human, Mouse, Rat
• Host: Rat
• Isotype: IgG1
• Clonality: Monoclonal
• Specificity: This Rat monoclonal antibody is directed against the P1 fragment of Laminin. They are species-independent as it has been shown that they bind to Laminin of Rat, Mouse and Human (Aten et al. 1995).
  MEC5 is an auto-antibody derived from DZB rats that had developed membranous glomerulopathy upon exposure to Mercuric Chloride (Aten et al. 1995).
• Formulation: State: Supernatant
  State: Liquid Hybridoma Culture Supernatant
  Preservative: 0.05% Sodium Azide
• Conjugation: Unconjugated
• Storage: Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.
  Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.
• Background: Laminin, the most abundant structural and biologically active component in basement membranes, is a complex extracellular glycoprotein with an approximate molecular weight of 900 kDa. It plays an important role in many aspects of the cell biology. Laminin is composed of one A chain (400 kDa) one B1 chain (215 kDa) and one B2 chain (205 kDa) all held together by disulfide bonds. The molecule has a cross like form with globular units near the ends of each chain, the sites where it is bound to Collagen IV, heparan sulfate, proteoglycan as well as to the surface of epithelial cells. Laminins from various species have common antigenic determinants. Laminin is only found in significant quantities in basement membranes, the thin extracellular matrices that surround epithelial tissue, nerve, fat cells and smooth, striated and cardiac muscle. It has been found to modulate cell differentiation, cell shaping and also cell movement because it appears to be an important cell substrate adhesion protein. Variations in the expression of this protein have been observed in embryogenesis, organogenesis, post traumatic healing and cancer. The greatest interest in laminin has been provoked by the discovery of its ability to promote neurite regeneration.