F11 Receptor (F11R) (AA 126-237) antibody

Details for Product No. ABIN968747
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Synonyms CD321, JAM, JAM1, JAMA, JCAM, KAT, PAM-1, 9130004G24, AA638916, ESTM33, JAM-1, JAM-A, Jcam, Jcam1, Ly106, Jam1
AA 126-237
(12), (10), (10), (9), (8), (5), (2), (1), (1), (1), (1)
(93), (52), (20), (2), (2), (1), (1), (1)
(40), (39), (32), (12), (2)
Clonality (Clone)
Monoclonal ()
(10), (8), (4), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB)
(68), (64), (31), (15), (14), (13), (13), (10), (8), (5), (4), (4), (3), (3), (1), (1), (1)
Pubmed 4 references available
Quantity 50 μg
Shipping to United States (Change)
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Catalog No. ABIN968747
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Immunogen Human JAM
Clone BE10
Isotype IgG1
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name JAM-1
Background Tight junctions (zonulae occludens) are critical to the maintenance of cell polarity and intercellular barriers. Protein components of the tight junctions include actin filaments, symplekin, occludin, ZO-1, ZO-2, and ZO-3. Junctional adhesion molecules, JAM-1, -2, and -3, are a new subfamily in the immunoglobulin (Ig) superfamily that colocalize with these components of tight junctions. JAM-1 was identified through a screen of antibodies that recognizes antigens located at cell-cell contacts. The structure of JAM-1 includes two V-type Ig domains in the extracellular region, two N-glycosylation sites, and a small C-terminal cytoplasmic region. JAM-1 protein is expressed at cell-cell junctions in endothelial and epithelial cells, and antibodies to JAM-1 inhibit spontaneous and chemokine-induced monocyte transmigration through an endothelial cell monolayer. In addition, TNFalpha and IFN-gamma cause redistribution of JAM-1 from intercellular junctions to the cytoplasm. JAM-1 also is the receptor for the platelet membrane protein, F11 antigen, and activation of platelets leads to PKC phosphorylation of JAM-1. Thus, JAM-1 is a junctional adhesion molecule that functions in endothelial, epithelial, and platelet adhesion.
Molecular Weight 38 kDa

Related Products: ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-F11 Receptor (F11R) (AA 126-237) antibody Western blot analysis of JAM-1 on human endothelial lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of JAM-1.
Product cited in: Gupta, Pillarisetti, Ohlstein: "Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages." in: IUBMB life, Vol. 50, Issue 1, pp. 51-6, 2001 (PubMed).

Ozaki, Ishii, Arai et al.: "Junctional adhesion molecule (JAM) is phosphorylated by protein kinase C upon platelet activation." in: Biochemical and biophysical research communications, Vol. 276, Issue 3, pp. 873-8, 2000 (PubMed).

Ozaki, Ishii, Horiuchi et al.: "Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 163, Issue 2, pp. 553-7, 1999 (PubMed).

Martìn-Padura, Lostaglio, Schneemann et al.: "Junctional adhesion molecule, a novel member of the immunoglobulin superfamily that distributes at intercellular junctions and modulates monocyte transmigration." in: The Journal of cell biology, Vol. 142, Issue 1, pp. 117-27, 1998 (PubMed).

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