Aoc3 Rat Monoclonal Antibody [Clone ID: 7-88]

CAT#: AM26314PU-N

Aoc3 rat monoclonal antibody, clone 7-88, Purified

Product Images

Frozen Sections: VAP-1 expression in mouse muscle tissue.

Specifications

Product Data

• Clone Name: 7-88
• Applications: FN, IF, IHC, IP
• Recommended Dilution: Immunohistochemistry on Frozen Sections (Ref.2,3): Tissue sections were fixed in acetone and incubated with antibody 7-88 for 20 minutes at room temperature. As negative control an irrelevant isotype-matched antibody was used (Ref.2).
  Flow Cytometry: Stains the extracellular domain of mouse VAP-1 in CHO cells transfected with mouse VAP-1 cDNA. As positive control anti-VAP-1 clone 7-106 was used and as negative control an isotype-matched control antibody (Ref. 2).
  Functional Assays (Ref.2,4): Antibody 7-88 (200µg) was intravenously injected which resulted in the inhibition of leukocyte trafficking in inflamed peritoneum (Ref.2).
  Immunofluorescence (Ref.5).
  Immunoprecipitation (Ref.1).
  Positive Control: Mouse VAP-1-transfected CHO cells (Ref.2).
  Negative Control: Mock-transfected CHO cells (Ref.2).
• Reactivities: Mouse
• Host: Rat
• Isotype: IgG2b
• Clonality: Monoclonal
• Immunogen: Vessels from mouse lymph nodes
• Specificity: The monoclonal antibody 7-88 recognizes mouse Vascular Adhesion Protein-1 (VAP-1) which is a glycosylated homodimeric membrane protein consisting of two 90 kDa subunits connected by disulfide bonds. It inhibits migration of granulocytes and monocytes in acute models of inflammation.
• Formulation: PBS
  State: Purified
  State: Liquid 0.2 µm filtered Ig fraction
  Stabilizer: 0.1% BSA
• Concentration: 0.1 mg/ml
• Purification: Protein G Chromatography
• Database Link:
  Entrez Gene 11754 Mouse
• Background:

  VAP-1 is a glycosylated homodimeric membrane protein consisting of two 90 kDa subunits connected by disulfide bonds. It contains a short N-terminal cytoplasmic tail, a single membrane-spanning domain and a large extracellular part. A soluble form of VAP-1 (sVAP-1) has been described, which presumably results from the proteolytic cleavage of membrane-bound VAP-1. Structurally VAP-1 belongs to enzymes called semicarbamizide-sensitive amine oxidases, which contain copper as a cofactor. These enzymes deaminate primary amines in a reaction producing hydrogen peroxide, aldehyde, and ammonia.
  VAP-1 is expressed in endothelial cells, smooth muscle cells, adipocytes, and in follicular dendritic cells. In endothelial cells the majority of VAP-1 is stored within intracellular granules and translocated to the surface upon inflammation where it regulates leukocyte tissue infiltration. Furthermore, the end-products formed by VAP-1 can also regulate leukocyte migration by signaling effects, have insulin-like effects in energy metabolism, and can cause vascular damage by direct cytotoxicity.
  In white adipose tissue of obese and diabetic db-/- mice increased expression of VAP-1 has been observed suggesting that it contributes to the arthrosclerosis and vascular dysfunction observed in these diseases. Moreover, inhibition of VAP-1reduced the accumulation of myeloid cells into tumors and attenuates tumor growth.

• Synonyms: HPAO