Detection of Phospho-Synaptotagmin-1 (T202) by Western Blot. Western Blot of rat cortex lysate showing specific immunolabeling of the ~60 - 62 kDa Synaptotagmin phosphorylated at T202 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase; lambda PPase). The blot is identical to the control except that it was incubated in lambda PPase (1200 units for 30 minutes) before being exposed to anti-Synaptotagmin (T202). The immunolabeling is completely eliminated by treatment with lambda PPase.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
For long-term storage, ≤ -20° C is recommended. Product is stable at ≤ -20° C for at least 1 year.
Synaptotagmins are integral membrane proteins
of synaptic vesicles. Synaptotagmin-1 is a glycoprotein containing two
C2 domains related to protein kinase C and sites for calcium-dependent
binding of acidic phospholipids. Synaptotagmin-1 participates in the
process of vesicular trafficking and exocytosis by inducing local
calcium-dependent buckling of the plasma membrane. Synaptotagmin-2 is a
single-pass, type Ia/III (no signal sequence) transmembrane (TM)
glycoprotein. Synaptotagmin-2 is an integral component of
neurotransmitter-containing synaptic vesicles that detects action
potential-induced increases in presynaptic cytosolic calcium. Increased
ionic calcium binds to synaptotagmin II at two sites (C2a and C2b) on
its cytoplasmic tail. The first site also binds phospholipid, while the
second site binds syntaxin. This promotes vesicle membrane fusion with
the presynaptic plasma membrane, resulting in neurotransmitter release.
undergo three types of posttranslational modification that may affect
function. N-linked glycosylation and/or O-linked glycosylation are
likely necessary for recycling (internalization) of vesicle membrane
after neurotransmitter release. Fatty acylation/palmitoylation of
synaptotagmin may be necessary for proper cycling. Finally, synaptoagmin
phosphorylation within the C2a site regulates calcium-binding, while
phosphorylation in the C2b site may regulate calcium and syntaxin
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