Thermo Fisher Scientific SAP102/DLG3 Polyclonal Antibody

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

Immunohistochemistry (Paraffin) (IHC (P))

1:200

-

Immunohistochemistry (Frozen) (IHC (F))

1:100-1:500

-

Immunocytochemistry (ICC/IF)

1:500

-

ELISA (ELISA)

1:500-1:1,000

-

Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

KLH conjugated synthetic peptide derived from human SAP102, amino acids 501-600. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:SAP102,uniProtId:Q92796-1,ncbiNodeId:9606,antigenRange:501-600,antigenLength:817,antigenImageFileName:BS-11315R_SAP102_Q92796-1_Rabbit.svg,antigenImageFileNamePDP:BS-11315R_SAP102_Q92796-1_Rabbit_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

1 mg/mL

Purification

Protein A

Storage buffer

0.01M TBS, pH 7.4, with 1% BSA, 50% glycerol

Contains

0.02% ProClin 300

Storage conditions

-20°C

Shipping conditions

Ambient (domestic); Wet ice (international)

Target Information

Synapse-Associated Protein 102 (SAP102) is one of a family of plasma membrane-associated proteins found in synaptic junctions. Like other members of the family, SAP102 has three approximately 90 amino acid repeats called PDZ domains followed by an SH3 domain and a yeast guanylate kinase homology (GuK) domain. It is hypothesized that PDZ-domain interactions play a role in receptor and channel clustering which contributes to neuronal plasticity. SAP102 is believed to participate in the clustering of certain proteins, including NMDA receptors, shaker-type potassium channels at the synaptic membrane in CNS neurons. NMDA receptors and Shaker-type potassium channels both share C-terminal sequence homology consisting of a threonine/serine-X-valine-COOH (T/SXV) motif. Other neuronal proteins that share this motif (beta 1 adrenergic receptor, some serotonin receptors, some sodium channel subunits, and additional potassium channel subunits) may interact with SAP102 by binding to its PDZ domains. Neuronal nitric oxide synthase (nNOS), which lacks the T/SXV motif but which has its own PDZ domain, has been shown to associate with SAP102 in vitro through a pseudo-homotypic PDZ-PDZ interaction.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.