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Recombinant Human CD30/TNFRSF8 Fc Alexa Fluor® 647 Protein

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Transfected cells were stained with the indicated concentrations of Recombinant Human CD30 Fc Chimera Alexa Fluor® 647 (Catalog # AFR11155).
2 μg/lane of Recombinant Human CD30/TNFRSF8 Fc Chimera Alexa Fluor® 647 Protein (Catalog # AFR11155) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

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Recombinant Human CD30/TNFRSF8 Fc Alexa Fluor® 647 Protein Summary

Additional Information
Fc Chimera
Details of Functionality
Measured by flow cytometry for its ability to bind HEK293 human embryonic kidney cells transfected with human CD30 Ligand. The concentration of Recombinant Human CD30/TNFRSF8 Fc Chimera Alexa Fluor® 647 (Catalog # AFR11155) that produces 50% of the binding response is 0.500-5.00 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human CD30/TNFRSF8 protein
Human CD30
(Phe19-Lys379)
Accession # P28908.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Phe19
Structure / Form
Disulfide-linked homodimer
Labeled with Alexa Fluor® 647
Excitation Wavelength: 650 nm
Emission Wavelength: 668 nm
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
65 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
80 - 110 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

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

Alternate Names for Recombinant Human CD30/TNFRSF8 Fc Alexa Fluor® 647 Protein

  • CD30 antigen
  • CD30
  • CD30KI-1
  • CD30L receptor
  • cytokine receptor CD30
  • D1S166EKi-1
  • Ki-1 antigen
  • Lymphocyte activation antigen CD30
  • TNFRSF8
  • tumor necrosis factor receptor superfamily member 8
  • tumor necrosis factor receptor superfamily, member 8

Background

CD30, also known as Ki-1 antigen and TNFRSF8, is a 120 kDa type I transmembrane glycoprotein belonging to the TNF receptor superfamily (1, 2). Mature human CD30 consists of a 361 amino acid (aa) extracellular domain (ECD) with six cysteine-rich repeats, a 28 aa transmembrane segment, and a 188 aa cytoplasmic domain (3). In contrast, mouse and rat CD30 lack 90 aa of the ECD and contain only three cysteine-rich repeats. Within common regions of the ECD, human CD30 shares 53% and 49% aa sequence identity with mouse and rat CD30, respectively. Alternate splicing of human CD30 generates an isoform that includes only the C‑terminal 132 aa of the cytoplasmic domain. CD30 is normally expressed on antigen-stimulated Th cells and B cells (4 ‑ 6). However, it is up‑regulated in Hodgkin’s disease (on Reed-Sternberg cells), other lymphomas, chronic inflammation, and autoimmunity (7). CD30 binds to CD30 Ligand/TNFSF8 which is expressed on activated Th cells, monocytes, granulocytes and medullary thymic epithelial cells (1, 5). CD30 signaling co‑stimulates antigen-induced Th0 and Th2 proliferation and cytokine secretion but favors a Th2-biased immune response (8). In the absence of antigenic stimulation, it can still induce T cell expression of IL‑13 (9). CD30 contributes to thymic negative selection by inducing the apoptotic cell death of CD4+CD8+ T cells (10, 11). In B cells, CD30 ligation promotes cellular proliferation and antibody production in addition to the expression of CXCR4, CCL3, and CCL5 (5, 12). An 85 ‑ 90 kDa soluble form of CD30 is shed from the cell surface by TACE-mediated cleavage (13, 14). Soluble CD30 retains the ability to bind CD30 Ligand and functions as an inhibitor of normal CD30 signaling (15).
  1. Kennedy, M.K. et al. (2006) Immunology 118:143.
  2. Tarkowski, M. (2003) Curr. Opin. Hematol. 10:267.
  3. Durkop, H. et al. (1992) Cell 68:421.
  4. Hamann, D. et al. (1996) J. Immunol. 156:1387.
  5. Shanebeck, S.D. et al. (1995) Eur. J. Immunol. 25:2147.
  6. Gruss, H.-J. et al. (1994) Blood 83:2045.
  7. Oflzoglu E. et al. (2009) Adv. Exp. Med. Biol. 647:174.
  8. Del Prete, G. et al. (1995) J. Exp. Med. 182:1655.
  9. Harlin, H. et al. (2002) J. Immunol. 169:2451.
  10. Amakawa, R. et al. (1996) Cell 84:551.
  11. Chiarle, R. et al. (1999) J. Immunol. 163:194.
  12. Vinante, F. et al. (2002) Blood 99:52.
  13. Hansen, H.P. et al. (1995) Int. J. Cancer 63:750.
  14. Hansen, H.P. et al. (2000) J. Immunol. 165:6703.
  15. Hargreaves, P.G. and A. Al-Shamkhani (2002) Eur. J. Immunol. 32:163.

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