Anti-Human MUC1 (CD227) - Dylight® 594

Leinco Technologies
Product Code: LEI-M472
Product Group: Primary Antibodies
CodeSizePrice
LEI-M472-250ug25 ug£183.00
Quantity:
LEI-M472-100ug100 ug£271.00
Quantity:
LEI-M472-500ug500 ug£681.00
Quantity:
Prices exclude any Taxes / VAT

Overview

Host Type: Mouse
Antibody Isotype: Mouse IgG1 L
Antibody Clonality: Monoclonal
Antibody Clone: HMFG2
Regulatory Status: RUO
Target Species: Human
Applications:
  • Enzyme-Linked Immunosorbent Assay (ELISA)
  • Flow Cytometry
  • Immunohistochemistry (IHC)
  • Immunoprecipitation (IP)
  • Western Blot (WB)
Shipping:
2 - 8°C Wet Ice
Storage:
This DyLight® 594 conjugate is stable when stored at 2-8°C. Do not freeze.

Further Information

Antigen Distribution:
MUC1 is a cell surface antigen expressed on mucosal epithelial tissues, T cells, B cells, bone marrow mononuclear cells, human blood dendritic cells, and monocyte-derived dendritic cells following in vitro activation. MUC1 is also found in the cytoplasm and cytoplasmic membrane of ductal cells, primarily in the striated ducts of the parotid and submandibular human glands and in the secretory compartment.
Concentration:
0.5 mg/ml
Conjugate/Tag/Label:
DyLight® 594
Format:
This DyLight® 594 conjugate is formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.4, 1% BSA and 0.09% sodium azide as a preservative.
Formulation:
This DyLight® 594 conjugate is formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.4, 1% BSA and 0.09% sodium azide as a preservative.
Immunogen:
MUC1 (CD227)
Long Description:
MUC1 is a large, highly glycosylated transmembrane mucin which contains a very large extracellular domain of 1000-2200 amino acids consisting primarily of 20 amino acid tandem repeats 1. MUC1 is a member of a family of related cell surface epithelial mucins 1,2 and is structurally related to hemopoietic and endothelial sialomucins such as GlyCAM1 and MadCAM-1 2. MUC1 forms part of the mucous gel that covers the external surface of epithelial tissues and acts as a barrier to infection 1. Additionally, MUC1 is involved in signal transduction via its highly conserved cytoplasmic tail, which is tyrosine phosphorylated in activated dendritic cells and T cells 2, and binds all members of the ErbB family of receptor tyrosine kinases as well as β-catenin 1. Additionally, there is interest in using MUC1 as a target antigen for cancer immunotherapy for carcinomas and multiple myeloma 2, due to variations in glycosylation that can be present in cancer 1. HMFG2 was generated by immunizing BALB/c mice with delipidated human milk fat globule (HMFG) containing the intact mucin, and subsequently immunizing with mammary epithelial cells 3. Spleen cells were fused with myeloma line P3/NSl/l-Ag4-1 to create hybridomas, which were screened for specificity against epithelial cells. HMFG2 reacts with an underglycosylated MUC1 mucin 4 and recognizes oligosaccharide sequences containing galactose, N-acetyl glucosamine and N-acetyl galactosamine, specifically the DTR sequence of the core protein 5. Binding to the core-protein epitopes is influenced by the length of the carbohydrate side chains 6.
NCBI Gene:
17829
Target:
CD227 (MUC1)

References

1. Ponce-Bravo S, Ledesma-Montes C, Morales-S?nchez I. APMIS. 116(2):93-98. 2008. 2. Wykes M, MacDonald KP, Tran M, et al. J Leukoc Biol. 72(4):692-701. 2002. 3. Taylor-Papadimitriou J, Peterson JA, Arklie J, et al. Int J Cancer. 28(1):17-21. 1981. 4. Burchell J, Gendler S, Taylor-Papadimitriou J, et al. Cancer Res. 47(20):5476-5482. 1987. 5. Burchell J, Durbin H, Taylor-Papadimitriou J. J Immunol. 131(1):508-513. 1983. 6. Burchell J, Taylor-Papadimitriou J. Epithelial Cell Biol. 2(4):155-162. 1993. 7. Price MR, Edwards S, Owainati A, et al. Int J Cancer. 36(5):567-574. 1985. 8. Schettini J, Kidiyoor A, Besmer DM, et al. Cancer Immunol Immunother. 61(11):2055-2065. 2012. 9. Arklie J, Taylor-Papadimitrious J, Bodmer W, et al. Int J Cancer. 28(1):23-29. 1981. 10. Berry N, Jones DB, Smallwood J, et al. Br J Cancer. 51(2):179-186. 1985. 11. Heyderman E, Strudley I, Powell G, et al. 52(3):355-361. 1985. 12. Demichelis SO, Alberdi CG, Servi WJ, et al. Appl Immunohistochem Mol Morphol. 18(1):41-50. 2010. 13. Beckford U, Barbatis C, Beesley JE, et al. J Clin Pathol. 38(5):512-520. 1985. 14. Ormerod MG, Steele K, Edwards PA, et al. J Exp Pathol. 1(4):263-271. 1984. 15. Dhokia B, Canney PA, Pectasides D, et al. Br J Cancer. 54(6):891-895. 1986. 16. Epenetos AA, Shepherd J, Britton KE, et al. Cancer. 55(5):984-987. 1985. 17. Singer S, Boddington MM, Hudson EA. J Clin Pathol. 38(2):180-184. 1985. 18. Epenetos AA, Hooker G, Krausz T, et al. Obstet Gynecol. 68(3 Suppl):71S-74S. 1986. 19. Swallow DM, Griffiths B, Bramwell M, et al. Dis Markers. 4(4):247-254. 1986.

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