Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Sodium azide is a reversible inhibitor of oxidative metabolism; therefore, antibody preparations containing this preservative agent must not be used in cell cultures nor injected into animals. Sodium azide may be removed by washing stained cells or plate-bound antibody or dialyzing soluble antibody in sodium azide-free buffer. Since endotoxin may also affect the results of functional studies, we recommend the NA/LE (No Azide/Low Endotoxin) antibody format, if available, for in vitro and in vivo use.
- This antibody has been developed and certified for the bioimaging application. However, a routine bioimaging test is not performed on every lot. Researchers are encouraged to titrate the reagent for optimal performance.
- Alexa Fluor® is a registered trademark of Molecular Probes, Inc., Eugene, OR.
- Triton is a trademark of the Dow Chemical Company.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Companion Products
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Munc18-1-interacting proteins, Mint1, Mint2, and Mint3, are members of the X11 family of proteins, which contain a phosphotyrosine-binding (PTB) domain and two PSD-95-DLG-ZO-1 (PDZ) domains. The PTB domain binds Asn-Pro-X-pTyr, a β-turn motif found on activated growth factor receptors and other signaling molecules. PDZ domains bind the C-terminus of proteins involved in receptor and channel clustering and protein localization in polarized cells. Both Mint1 and Mint2 are expressed primarily in the nervous system and may interact with Munc18-1 and syntaxin to form a multimeric complex that mediates appropriate docking/fusion of synaptic vesicles. In addition, both Mint1 and Mint2 may be involved in Alzheimer's disease, since Mint2 colocalizes with amyloid precursor protein (APP) and is found in neuritic plaques, while Mint1 can bind APP, and inhibits the processing of APP to the amyloid β peptide. Mint3 can also bind APP, but differs from Mint1 and Mint2 in its N-terminal region. It is also more widely expressed. Thus, Mint3 may function in signaling pathways, vesicle exocytosis, and/or protein targeting in a wide range of tissues. Mint3 has a calculated molecular weight of 61 kD, but reportedly is observed migrating at 86-89 kD.
Development References (3)
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Borg JP, Straight SW, Kaech SM. Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting. J Biol Chem. 1998; 273(48):31633-31636. (Biology). View Reference
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Borg JP, Yang Y, De Taddeo-Borg M, Margolis B, Turner RS. The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. J Biol Chem. 1998; 273(24):14761-14766. (Biology). View Reference
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McLoughlin DM, Irving NG, Brownlees J, Brion JP, Leroy K, Miller CC. Mint2/X11-like colocalizes with the Alzheimer's disease amyloid precursor protein and is associated with neuritic plaques in Alzheimer's disease. Eur J Neurosci. 1999; 11(6):1988-1994. (Biology). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.
