Human ST6 GalNAc alpha-2,6-sialyltransferase V/ST6GALNAC5 Alexa Fluor™ Plus 488‑conjugated Antibody

R&D Systems | Catalog # FAB67151AFP488

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Key Product Details

Species Reactivity

Human

Applications

Immunocytochemistry

Label

Alexa Fluor Plus 488 (Excitation = 493 nm, Emission = 518 nm)

Antibody Source

Monoclonal Mouse IgG2A Clone # 719508
View all ST6 GalNAc alpha-2,6-sialyltransferaseV/ST6GALNAC5 Primary Antibodies »

Product Specifications

Specificity

Detects human GalNAc alpha -2,6-sialyltransferase V/ST6GALNAC5 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human (rh) ST6GALNAC4 or rhST6GALNAC6 is observed.

Clonality

Monoclonal

Host

Mouse

Isotype

IgG2A

Applications

Application
Recommended Usage

Immunocytochemistry

Optimal dilution of this antibody should be experimentally determined.

Formulation, Preparation, and Storage

Formulation

Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

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.

References

  1. Kolter, T. et al. (2002) J. Biol. Chem. 277:25859.
  2. Yu, R.K. et al. (2008) Glycoscience DOI: 10.1007/978-3-540-30429-6_41.
  3. Okajima, T. et al. (1999) J. Biol. Chem.274:30557.
  4. Harduin-Lepers, A. et al. (2005) Glycobiology 15:805.
  5. Bos, P.D. et al. (2009) Nature 459:1005.
  6. Arshad, F. et al. (2011). Patholog. Res. Int. DOI: 10.4061/2011/920509.
  7. Wu, Z.L. et al. (2010) Glycobiology DOI: 10.1093/glycob/cwq187.

Long Name

ST6 alpha-N-acetylGalactosaminide alpha-2,6-sialyltransferase 5

Alternate Names

GD1 alpha synthase, SIAT7E, ST6GalNAcV

Entrez Gene IDs

81849 (Human); 26938 (Mouse)

Gene Symbol

ST6GALNAC5

UniProt

Q9BVH7

Additional ST6 GalNAc alpha-2,6-sialyltransferaseV/ST6GALNAC5 Products

Product Documents

Certificate of Analysis

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Note: Certificate of Analysis not available for kit components.

Product Specific Notices


This product is provided under an intellectual property license from Life Technologies Corporation. The transfer of this product is conditioned on the buyer using the purchased product solely in research conducted by the buyer, excluding contract research or any fee for service research, and the buyer must not (1) use this product or its components for (a) diagnostic, therapeutic or prophylactic purposes; (b) testing, analysis or screening services, or information in return for compensation on a per-test basis; or (c) manufacturing or quality assurance or quality control, and/or (2) sell or transfer this product or its components for resale, whether or not resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5781 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@thermofisher.com.

For research use only

Related Research Areas

Glycobiology-related Enzymes

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