产品详情
  • 产品名称:Neuroligin4,X-Linked(NLGN4X)(AA42-676)(Active)protein(Histag)

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  • 产品厂商:ACROBiosystems
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简单介绍:
Neuroligin4,X-Linked(NLGN4X)(AA42-676)(Active)protein(Histag)
详情介绍:
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 72.2 kDa. The protein migrates as 80-110 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Neuroligin-4, X-linked (NLGN4X) is also known as HNLX, KIAA1260, NLGN4, ASPGX2, AUTSX2, HLNX, HNL4X, NLGN, NLGN4, which belongs to the type-B carboxylesterase/lipase family, a neuronal cell surface proteins. NLGN4X is a homodimer, which can interacts with NRXN1 in a calcium-dependent manner and also interacts through its C-terminus with DLG4/PSD-95 third PDZ domain. Neuroligins may act as splice site-specific ligands for beta-neurexins and may be involved in the formation and remodeling of central nervous system synapses. NLGN4X is putative neuronal cell surface protein involved in cell-cell-interactions.
Molecular Weight 72.2 kDa
UniProt Q8N0W4
Pathways Cell-Cell Junction Organization, Synaptic Membrane
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for Neuroligin 4, X-Linked (NLGN4X) (AA 42-676) (Active) protein (His tag) (ABIN2181539) Human Neuroligin-4, X-linked, His Tag on SDS-PAGE under reducing (R) condition. The g...
Background publications Fabrichny, Leone, Sulzenbacher, Comoletti, Miller, Taylor, Bourne, Marchot: "Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion." in: Neuron, Vol. 56, Issue 6, pp. 979-91, 2007 (PubMed).

Irie, Hata, Takeuchi, Ichtchenko, Toyoda, Hirao, Takai, Rosahl, Südhof: "Binding of neuroligins to PSD-95." in: Science (New York, N.Y.), Vol. 277, Issue 5331, pp. 1511-5, 1997 (PubMed).