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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.
- For fluorochrome spectra and suitable instrument settings, please refer to our Multicolor Flow Cytometry web page at www.bdbiosciences.com/colors.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Annexin II (p36), originally discovered as a substrate for the src oncogene, is one of the most studied members of the annexin family of calcium-dependent phospholipid-binding proteins. It exists in cells as either a monomer or a heterotetramer complexed with p11, an S100-related protein. In vitro, it has been found that unphosphorylated annexin II is capable of causing aggregation of chromaffin granules, and, upon phosphorylation, induces fusion of the granules' membranes. A similiar phenomenon may occur in the final steps of exocytosis after cytoplasmic annexin translocates to the subplasmalemmal region and is phosphorylated by protein kinase C. However, other studies refute annexin II's involvement in exocytosis, and a conclusive role for annexin II in membrane trafficking remains debated.
This antibody is routinely tested by immunofluorescence microscopy. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (3)
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Chasserot-Golaz S, Vitale N, Sagot I, et al. Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells. J Cell Biol. 1996; 133(6):1217-1236. (Biology). View Reference
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Graham ME, Gerke V, Burgoyne RD. Modification of annexin II expression in PC12 cell lines does not affect Ca(2+)-dependent exocytosis. Mol Biol Cell. 1997; 8(3):431-442. (Biology). View Reference
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Regnouf F, Sagot I, Delouche B, et al. "In vitro" phosphorylation of annexin 2 heterotetramer by protein kinase C. Comparative properties of the unphosphorylated and phosphorylated annexin 2 on the aggregation and fusion of chromaffin granule membranes. J Biol Chem. 1995; 270(45):27143-27150. (Biology). View Reference
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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described
Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
