Cat. No.: 123 004
Amount: 100 µl
Price:
$365.00
Cat. No. 123 004 |
100 µl antiserum, lyophilized. For reconstitution add 100 µl H2O, then aliquot and store at -20°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
Applications |
Immunoprecipitation (IP); Immunoisolation or pulldown of a target molecule using an antibody. For details and product specific hints, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IP: not tested yet Immunocytochemistry (ICC) on 4% PFA fixed cells. Immunoreactivity is usually revealed by fluorescence. Some antibodies require special fixation methods. For details, please refer to the “Remarks” section.', $event)" style="cursor: help;">ICC: 1 : 500 up to 1 : 1000 gallery Immunohistochemistry (IHC) on 4% PFA perfusion fixed tissue with 24h PFA post fixation. Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate. Some antibodies require special fixation methods or antigen retrieval steps. For details, please refer to the ”Remarks” section.', $event)" style="cursor: help;">IHC: 1 : 500 gallery Immunohistochemistry (IHC-P) of formalin fixed, paraffin embedded (FFPE) tissue (some antibodies require special antigen retrieval steps, please refer to the ”Remarks” section). Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate.', $event)" style="cursor: help;">IHC-P: 1 : 500 gallery |
Immunogen | Synthetic peptide corresponding to AA 733 to 744 from rat NSF (UniProt Id: Q9QUL6) |
Reactivity |
Reacts with: rat (Q9QUL6), mouse (P46460). Other species not tested yet. |
Matching control protein/peptide | 123-0P |
Data sheet | 123_004.pdf |
N-ethylamide sensitive fusion protein NSF functions together with SNAPs (soluble NSF attachment proteins) and SNAREs (SNAP receptors) in vesicular transport.
NSF is a homotrimer whose polypeptide subunits are made up of three distinct domains: an amino - terminal domain (N) and two homologous ATP-binding domains (D1 and D2). NSF is an ATPase that dissociates SNARE complexes, such as the core complex composed of synaptobrevin/VAMP, syntaxin 1 and SNAP 25 under ATP hydrolysis. The ability of the D1 domain to hydrolyze ATP is required for NSF activity. The D2 domain is required for trimerization, but its ability to hydrolyze ATP is not absolutely required for NSF function.