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Syndecan 1 (E7F7T) Rabbit mAb #96489

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  • F
Immunohistochemical analysis of paraffin-embedded human urothelial carcinoma using Syndecan 1 (E7F7T) Rabbit mAb.

To Purchase # 96489

Supporting Data

REACTIVITY H
SENSITIVITY Endogenous
MW (kDa)
Source/Isotype Rabbit IgG
Application Key:
  • IHC-Immunohistochemistry 
  • F-Flow Cytometry 
Species Cross-Reactivity Key:
  • H-Human 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Immunohistochemistry (Paraffin) 1:100 - 1:400
Flow Cytometry (Fixed/Permeabilized) 1:50 - 1:200
Flow Cytometry (Live) 1:50 - 1:200

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

For a carrier free (BSA and azide free) version of this product see product #25851.

Protocol

Specificity / Sensitivity

Syndecan 1 (E7F7T) Rabbit mAb recognizes endogenous levels of total syndecan 1 protein for approved applications. Non-specific staining was observed in skeletal muscle by immunohistochemistry.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus in the extracellular region of human syndecan 1 protein.

Background

Syndecans are a family of type 1 transmembrane heparan sulfate proteoglycans comprising four members in mammals (SDC1-4) (1) encoded by four syndecan genes. Syndecans are involved in embryonic development, tumorigenesis, and angiogenesis (2). The extracellular domain harbors attachment sites for heparan sulfate and chondroitin sulfate chains, facilitating interaction with an array of proteins, including a plethora of growth factors. In addition, the hydrophobic C-terminal intracellular domain can interact with proteins containing a PDZ domain (2). These interactions place syndecans as important integrators of membrane signaling (3). Syndecans undergo proteolytic cleavage causing the release of their extracellular domain (shedding), converting the membrane-bound proteins into soluble molecular effectors (4).

Syndecan 1 (SDC1) is a specific marker for plasmacytic differentiation in hematologic disorders (5-7). This cell surface proteoglycan is also expressed in normal epithelial cells and tissues as well as various types of cancer tissues (8-11). The extracellular shed form of syndecan 1 remains soluble or accumulates in the extracellular matrix where it binds growth factors, cytokines and other extracellular matrix proteins (12,13). This binding activates signaling of bound growth factors or cytokines, which results in enhanced tumor growth, dissemination, angiogenesis, and osteolysis (14-17). As a result, the level of syndecan 1 protein and its shed form may serve as prognostic factors for a list of malignancies (6,18,19). Syndecan 1 has recently been found to be a critical mediator of macropinocytosis in pancreatic cancer (20).
  1. Couchman, J.R. (2003) Nat Rev Mol Cell Biol 4, 926-37.
  2. Multhaupt, H.A. et al. (2009) J Physiol Pharmacol 60 Suppl 4, 31-8.
  3. Zimmermann, P. and David, G. (1999) FASEB J 13 Suppl, S91-S100.
  4. Manon-Jensen, T. et al. (2010) FEBS J 277, 3876-89.
  5. Chilosi, M. et al. (1999) Mod Pathol 12, 1101-6.
  6. Seidel, C. et al. (2000) Blood 95, 388-92.
  7. O'Connell, F.P. et al. (2004) Am J Clin Pathol 121, 254-63.
  8. Inki, P. and Jalkanen, M. (1996) Ann Med 28, 63-7.
  9. Matsumoto, A. et al. (1997) Int J Cancer 74, 482-91.
  10. Conejo, J.R. et al. (2000) Int J Cancer 88, 12-20.
  11. Zellweger, T. et al. (2003) Prostate 55, 20-9.
  12. Bayer-Garner, I.B. et al. (2001) Mod Pathol 14, 1052-8.
  13. Ramani, V.C. et al. (2013) FEBS J 280, 2294-306.
  14. Derksen, P.W. et al. (2002) Blood 99, 1405-10.
  15. You, W.K. and McDonald, D.M. (2008) BMB Rep 41, 833-9.
  16. Ramani, V.C. et al. (2011) J Biol Chem 286, 6490-9.
  17. Aragão, A.Z. et al. (2012) PLoS One 7, e43521.
  18. Joensuu, H. et al. (2002) Cancer Res 62, 5210-7.
  19. Lee, S.H. et al. (2014) Int J Clin Oncol 19, 247-53.
  20. Yao, W. et al. (2019) Nature 568, 410-414.
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