CoraLite® Plus 488-conjugated SNAP25 Recombinant antibody

SNAP25 Recombinant Antibody for IF/ICC

Host / Isotype

Rabbit / IgG

Reactivity

human, mouse, rat

Applications

IF/ICC

Conjugate

CoraLite® Plus 488 Fluorescent Dye

CloneNo.

240069F12

Cat no : CL488-83259-5

Synonyms

SNAP 25, SNAP, RIC-4, RIC4, RIC 4

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Validation Data Gallery

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  IF Staining of PC-12 using CL488-83259-5

  Immunofluorescent analysis of (-20°C Ethanol) fixed PC-12 cells using CoraLite® Plus 488 SNAP25 antibody (CL488-83259-5, Clone: 240069F12 ) at dilution of 1:200.

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Tested Applications

• Positive IF/ICC detected in: PC-12 cells

Recommended dilution

• Immunofluorescence (IF)/ICC: IF/ICC : 1:50-1:500

It is recommended that this reagent should be titrated in each testing system to obtain optimal results.

Sample-dependent, Check data in validation data gallery.

Product Information

The immunogen of CL488-83259-5 is SNAP25 Fusion Protein expressed in E. coli.

• Tested Reactivity: human, mouse, rat
• Host / Isotype: Rabbit / IgG
• Class: Recombinant
• Type: Antibody
• Immunogen: SNAP25 fusion protein Ag6695
• Full Name: synaptosomal-associated protein, 25kDa
• Calculated Molecular Weight: 23 kDa
• Observed Molecular Weight: 25 kDa
• GenBank Accession Number: BC010647
• Gene Symbol: SNAP25
• Gene ID (NCBI): 6616
• Conjugate: CoraLite® Plus 488 Fluorescent Dye
• Excitation/Emission Maxima Wavelengths: 493 nm / 522 nm
• Form: Liquid
• Purification Method: Protein A purification
• Storage Buffer: PBS with 50% Glycerol, 0.05% Proclin300, 0.5% BSA, pH 7.3.
• Storage Conditions: Store at -20°C. Avoid exposure to light. Stable for one year after shipment. Aliquoting is unnecessary for -20^oC storage.

Background Information

The synaptosomal associated protein of 25 kD (SNAP-25) was first identified as a major synaptic protein by Wilson and colleagues. The protein interacts with syntaxin and synaptobrevin through its N-terminal and C-terminal -helical domains. Its palmitoylation domain is located in the middle of the molecule that contains four cysteine residues. Mutation of the cysteines abolishes palmitoylation and membrane binding. Several elegant studies using synaptosome preparations and permeabilized PC12 cells have suggested that SNAP-25 may act in the late post-docking steps of exocytosis. By limited proteolysis and in vitro binding assay, it is proposed that the two helix domains act independently and contribute equally to form the SNARE complex with syntaxin and synaptobrevin. It seems that a major regulatory element is located in the C-terminus of SNAP-25. Removing a 9 amino acid sequence of SNAP-25 inhibited neurosecretion in chromaffin cells.