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

CAT#: AM26314PU-N

Aoc3 rat monoclonal antibody, clone 7-88, Purified



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CNY 7940.00


货期*
5周

规格
    • 100 ug

Product images

Specifications

Product Data
Clone Name 7-88
Applications FN, IF, IHC, IP
Recommend 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).
Reactivity Mouse
Host Rat
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.
Isotype IgG2b
Formulation PBS
State: Purified
State: Liquid 0.2 µm filtered Ig fraction
Stabilizer: 0.1% BSA
Concentration lot specific
Purification Protein G Chromatography
Conjugation Unconjugated
Storage Condition

Store undiluted at 2-8°C.

Gene Name amine oxidase, copper containing 3
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
Reference Data
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