Human ST6 GalNAc alpha-2,6-sialyltransferase V/ST6GALNAC5 Antibody Summary
Accession # Q9BVH7
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
GalNAc alpha ‑2,6‑sialyltransferase V/ST6GALNAC5 in MDA‑MB‑231 Human Cell Line. GalNAc a-2,6-sialyltransferase V/ST6GALNAC5 was detected in immersion fixed MDA-MB-231 human breast cancer cell line using Mouse Anti-Human GalNAc a-2,6-sialyltransferase V/ST6GALNAC5 Monoclonal Antibody (Catalog # MAB67151) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red, upper panel; Catalog # NL007) and counterstained with DAPI (blue, lower panel). Specific staining was localized to cell membranes and cytoplasm. View our protocol for Fluorescent ICC Staining of Cells on Coverslips.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: ST6 GalNAc alpha-2,6-sialyltransferaseV/ST6GALNAC5
Gangliosides are acidic glycosphingolipids that contain one or more sialic acid residues (1). They are abundant in the nervous system, where they play crucial modulatory roles in cellular recognition, interaction, adhesion, and signal transduction, particularly during early developmental stages. The expression of gangliosides in the nervous system is developmentally regulated through various sialyltransferases (2). ST6GALNAC5 is a sialyltransferase involved in the biosynthesis of ganglioside GD1a (NeuAc alpha 2,3Gal beta 1,3GalNAc beta 1,4(NeuAc alpha 2,3)Gal beta 1,4Glc beta 1-Cer) from GM1b (NeuAc alpha 2,3Gal beta 1,3GalNAc beta 1,4Gal beta 1,4Glc beta 1-Cer), and its expression is restricted to the brain (3, 4). ST6GALNAC5 has been identified as a key player in the metastasis of breast cancer cells to the brain by potentially enabling the cancer cells to cross the blood-brain barrier (5, 6). The recombinant ST6GALNAC5 was active on fetuin from fetal calf serum when assayed using a phosphatase-coupled method (7) suggesting the substrate specificity of ST6GALNAC5 may require further characterization.
- Kolter, T. et al. (2002) J. Biol. Chem. 277:25859.
- Yu, R.K. et al. (2008) Glycoscience DOI: 10.1007/978-3-540-30429-6_41.
- Okajima, T. et al. (1999) J. Biol. Chem.274:30557.
- Harduin-Lepers, A. et al. (2005) Glycobiology 15:805.
- Bos, P.D. et al. (2009) Nature 459:1005.
- Arshad, F. et al. (2011). Patholog. Res. Int. DOI: 10.4061/2011/920509.
- Wu, Z.L. et al. (2010) Glycobiology DOI: 10.1093/glycob/cwq187.
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