Anti-Phospho-SYN1-Ser9 antibody (STJA0003783)

SPECIFICATIONS
ClonalityPolyclonal
HostRabbit
ConjugationUnconjugated
IsotypeIgG
ImmunogenSynthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 conjugated to KLH.
STJA0003783-100
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General Information

Short DescriptionRabbit polyclonal anti-Phospho-Synapsin I-Ser9 for use in WB and ICC in Mouse, Rat, Zebrafish, Bovine, Human and Xenopus samples. Datasheet included with dilution recommendations, and related reagents.
ApplicationsWB/ICC
HostRabbit
ReactivityMouse/Rat/Zebrafish/Bovine/Human/Xenopus
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

ClonalityPolyclonal
IsotypeIgG
ConjugationUnconjugated
PurificationThis antibody was antigen affinity purified from pooled serum.
Dilution RangeWB 1:1000
ICC 1:500
Formulation100 ยตl in 10 mM HEPES (pH 7.5) , 150 mM NaCl, 100 ยตg per ml BSA and 50% Glycerol.
Storage InstructionStore at-20ยฐC for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.

Target Information

ImmunogenSynthetic phospho-peptide corresponding to amino acid residues surrounding Ser9 conjugated to KLH.

Additional Info

Background Synapsin I plays a key role in synaptic plasticity in brain (Feng et al., 2002; Nayak et al., 1996). This effect is due in large part to the ability of the synapsins to regulate the availability of synaptic vesicles for release. In addition to its role in plasticity, the expression of synapsin I is a precise indicator of synapse formation (Moore and Bernstein, 1989; Stone et al., 1994). Thus, synapsin I immunocytochemistry provides a valuable tool for the study of synaptogenesis. The role of synapsin in synaptic plasticity and in synaptogensis is regulated by phosphorylation (Jovanovic et al., 2001; Kao et al., 2002). Serine 9 is the site on synapsin I that is phosphorylated by cAMP-dependent protein kinase and by calcium calmodulin kinase I (Czernik et al., 1987). Phosphorylation of this site is thought to Western blot of rat cortical lysate showing specific regulate synaptic vesicle function and neurite outgrowth (Kao et al., immunolabeling of the ~78 kDa synapsin I phosphorylated at 9 2002). Ser in the first lane (-). Phosphospecificity is shown in the second lane (+) where the immunolabeling is completely eliminated by blot treatment with lambda phosphatase ( Lambda-

Information sourced from Uniprot.org

Citations

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