Recombinant Human epsilon-Sarcoglycan Fc Chimera Protein, CF

Recombinant Human epsilon‑Sarcoglycan Fc Chimera (Catalog #10170-SG) supports the adhesion of RT4‑D6P2T rat schwannoma cells. The ED50for this effect is 0.8-4.8 μg/mL.

2 μg/lane of Recombinant Human epsilon-Sarcoglycan Fc Chimera (Catalog # 10170-SG) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 57-71 kDa and 110-140 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human epsilon-Sarcoglycan Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of RT4‑D6P2T rat schwannoma cells. The ED₅₀ for this effect is 0.8-4.8 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human epsilon-Sarcoglycan protein
  

  Human epsilon-Sarcoglycan (Asp47-Phe317) Accession # O43556-1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: O43556-1
• N-terminal Sequence: Asp47
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 58 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 57-71 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human epsilon-Sarcoglycan Fc Chimera Protein, CF

• dystonia 11, myoclonic
• DYT11
• epsilon-Sarcoglycan
• Epsilon-SG
• ESG
• Sarcoglycan epsilon
• sarcoglycan, epsilon
• SGCE

Background

SGCE, or Epsilon-Sarcoglycan, is a type 1 transmembrane glycoprotein which was found as a homologue of alpha -sarcoglycan (1, 2). Sarcoglycans are part of the dystrophin-associated glycoprotein complex (DGC). This multiprotein complex connects the actin cytoskeleton to the extracellular matrix in cardiac and skeletal muscles (3, 4). The sarcogylcan complex is a subcomplex within the DGC and is composed of several muscle-specific forms. alpha , beta , gamma and δ-sarcoglycans are expressed predominantly in striated and smooth muscles while epsilon -Sarcoglycan (SGCE) is expressed in a wide range of tissues, with the highest levels in heart and lung (1-2, 5). Mutations in the human SGCE gene have been shown to be associated with myoclonus-dystonia (6). Human SGCE is synthesized as a 437 amino acid (aa) protein that includes a 317 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 99 aa cytoplasmic domain. Within the ECD, human SGCE shares 95% and 66% aa sequence identity the mouse and rat SGCE, respectively. There are multiple isoforms of SGCE protein present in humans. SGCE exon 11b isoform is differentially expressed in the brain (1). Knockout mutations in this isoform result in psychiatric diseases (7).

1. Ettinger, A.J. et al. (1997) J. Biol. Chem. 272:32534.
2. McNally, E.M. et al. (1998) FEBS Lett. 422:27.
3. Blake, D.J. et al. (2002) Physiol. Rev. 82:291.
4. Xiao, J. et al. (2017) Neurobiol. Dis. 98:52.
5. Nishiyama, A. et al. (2004) Brain Res. Mol. Brain Res. 125:1.
6. Zimprich, A. et al. (2001) Nat. Genet. 29:66.
7. Peall. K.J. et al. (2013) Brain. 136:294.

Bioinformatics

• Uniprot:
  • O43556-1()