AN2/NG2 Proteoglycan (0) (extracellular domain) Antikörper

Antigen: AN2/NG2 Proteoglycan (0)

Synonyme: AN2, NG2, 4732461B14Rik

Epitope: extracellular domain

Klonalität: Polyklonal

Wirt: Kaninchen

Reaktivität: Maus

Applikation: Immunhistochemie (IHC), Western Blot (WB)

Produktnummer: ABIN350515

Produktbeschreibung

Weitere Bezeichnung: NG2 (Chondroitin sulfate proteoglycan 4, AN2 proteoglycan) (extracellular domain)

Swiss-Prot: Q8VHY0

Immunogen: A synthetic peptide from the extracellular domain of mouse NG2 (Chondroitin sulfate proteoglycan 4, AN2 proteoglycan) conjugated to an immunogenic carrier protein was used as the immunogen.

Format: Lyophilized

Beschreibung: Valuable marker for several incompletely differentiated precursor cells. Function: Proteoglycan playing a role in cell proliferation and migration which stimulates endothelial cells motility during microvascular morphogenesis. May also inhibit neurite outgrowth and growth cone collapse during axon regeneration. Cell surface receptor for collagen alpha 2(VI) which may confer cells ability to migrate on that substrate. Binds through its extracellular N-terminus growth factors, extracellular matrix proteases modulating their activity. May regulate MPP16-dependent degradation and invasion of type I collagen participating in melanoma cells invasion properties. May modulate the plasminogen system by enhancing plasminogen activation and inhibiting angiostatin. Functions also as a signal transducing protein by binding through its cytoplasmic C-terminus scaffolding and signaling proteins. May promote retraction fiber formation and cell polarization through Rho GTPase activation. May stimulate alpha-4, beta-1 integrin-mediated adhesion and spreading by recruiting and activating a signaling cascade through CDC42, ACK1 and BCAR1. May activate FAK and ERK1/ERK2 signaling cascades. Subcellular location: Apical cell membrane; Single-pass type I membrane protein; Extracellular side. Cell projection › lamellipodium membrane; Single-pass type I membrane protein; Extracellular side. Tissue specificity: Expressed in microcascular pericytes and not endothelial cells. Also known as: MEL CSPG, MELCSPG, Chondroitin sulfate proteoglycan 4, Chondroitin sulfate proteoglycan NG2, CSPG4, MCSP, MCSPG, Melanoma associated chondroitin sulfate proteoglycan, Melanoma chondroitin sulfate proteoglycan, MSK16.

Spezifität: Appears to be specific for NG2.

Anwendungen

Applikationshinweise: IHC, WB. A dilution of 1 : 300 to 1 : 2000 is recommended. The optimal dilution should be determined by the end user. Not yet tested in other applications.

Reinheit: whole serum

Lagerung: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Publikationen

Publikationen: Petersen, Nielsen, Nykjaer et al.: "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography." in: The Journal of biological chemistry, Vol. 272, Issue 6, pp. 3599-605, 1997 (PubMed).

Mazella, Zsuerger, Navarro et al.: "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor." in: The Journal of biological chemistry, Vol. 273, Issue 41, pp. 26273-6, 1998 (PubMed).

Nielsen, Jacobsen, Olivecrona et al.: "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase." in: The Journal of biological chemistry, Vol. 274, Issue 13, pp. 8832-6, 1999 (PubMed).

Nielsen, Madsen, Christensen et al.: "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein." in: The EMBO journal, Vol. 20, Issue 9, pp. 2180-90, 2001 (PubMed).

Shiba, Takatsu, Nogi et al.: "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1." in: Nature, Vol. 415, Issue 6874, pp. 937-41, 2002 (PubMed).

Maeda, Nobukuni, Shimo-Onoda et al.: "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization." in: Journal of cellular physiology, Vol. 193, Issue 1, pp. 73-9, 2002 (PubMed).

Martin, Vincent, Mazella: "Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 23, Issue 4, pp. 1198-205, 2003 (PubMed).

Teng, Teng, Lee et al.: "ProBDNF induces neuronal apoptosis via activation of a receptor complex of p75NTR and sortilin." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 25, Issue 22, pp. 5455-63, 2005 (PubMed).

Gregory, Barlow, McLay et al.: "The DNA sequence and biological annotation of human chromosome 1." in: Nature, Vol. 441, Issue 7091, pp. 315-21, 2006 (PubMed).

Zahedi, Lewandrowski, Wiesner et al.: "Phosphoproteome of resting human platelets." in: Journal of proteome research, Vol. 7, Issue 2, pp. 526-34, 2008 (PubMed).