Recombinant Human CD30-Fc Chimera (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
TNFRSF8, CD30L Receptor, Ki-1 Antigen, Cytokine Receptor CD30, TNF Receptor Superfamily Member 8.
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Product Citations
publications
Human_CD30_CF_RECOM_1_120721
Recombinant human CD30-Fc chimera binds to immobilized recombinant human CD30L (Cat. No. 767102) in a dose-dependent manner. The ED50 for this effect is 2 – 8 ng/mL.
  • Human_CD30_CF_RECOM_1_120721
    Recombinant human CD30-Fc chimera binds to immobilized recombinant human CD30L (Cat. No. 767102) in a dose-dependent manner. The ED50 for this effect is 2 – 8 ng/mL.
  • Human_CD30_CF_RECOM_2_120721
    Stability Testing for Recombinant Human CD30-Fc Chimera. Recombinant human CD30-Fc chimera was aliquoted in PBS, pH 7.2. One aliquot was frozen and thawed four times (4x Freeze/Thaw) and compared to the control that was kept at 4°C (Control). The samples were tested for their ability to bind to immobilized recombinant human CD30L (Cat. No. 767102) in a dose-dependent manner. The ED50 for this effect is 2 – 8 ng/mL.
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796704 25 µg 111€
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796706 100 µg 273€
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Description

Human CD30, a mature protein of 577 amino acids and a member of the TNF receptor family, is characterized by repeated cysteine-rich motifs in the extracellular domain. CD30 is a type I transmembrane glycoprotein, and it is expressed on some B cells and on mitogen-stimulated T cells. CD30 was originally identified as a cell surface antigen, Ki-1, on Hodgkin and Reed-Sternberg cells. CD30 binds to CD30L, a type II transmembrane protein, and the CD30-CD30L interaction induces NF-κB activation which is mediated by TNFR-associated factor 2 (TRAF2). CD30L/CD30 signaling seems to be involved in Th1 and Th2 cell responses and plays a key role in Th17 differentiation in mice. TNFRs such as CD30, OX40, and 4-1BB participate in survival of activated T cells. Mice lacking both OX40 and CD30 signals have severe loss of CD4+ memory T cells in the spleen and lamina propria. In addition, CD30-deficient mice show a decreased capacity to sustain follicular germinal center responses, and double KO mice (OX40 and CD30) lack memory antibody responses because of deficient CD4 T cell memory. Mast cells are the predominant CD30L-positive cell in chronic inflammatory skin diseases psoriasis and atopic dermatitis, and CD30 and CD30L expression is upregulated in lesional skin in these conditions. An agonistic anti-CD30 drug conjugate, Brentuximab vedotin, has been approved for the treatment of CD30-positive lymphomas.

Product Details
Technical Data Sheet (pdf)

Product Details

Source
Human CD30, amino acids (Phe19-Lys379) (Accession No. P28908) with a linker and a C-terminal human IgG1 (Pro100-Lys330) was expressed in CHO cells.
Molecular Mass
The 600 amino acid recombinant protein has a predicted molecular mass of approximately 63.3 KD. The DTT-reduced and non-reduced glycosylated protein migrate at approximately 90 kD and 180 kD respectively by SDS-PAGE. The predicted N-terminal amino acid is Phe.
Purity
> 95%, as determined by Coomassie stained SDS-PAGE
Formulation
0.22 µm filtered protein solution in PBS, pH 7.2
Endotoxin Level
Less than 0.1 EU per µg cytokine as determined by the LAL method
Concentration
25 µg size is bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration, please enter the lot number in our Concentration and Expiration Lookup or Certificate of Analysis online tools.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
Recombinant human CD30-Fc chimera binds to immobilized recombinant human CD30L (Cat. No. 767102) in a dose-dependent manner.The ED50 for this effect is 2 – 8 ng/mL.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

Structure
Trimer
Distribution

Activated T, B cells, Th1, Th2, Th0, CD8 T cells, NK cells

Function
CD30 could induce survival, proliferation, differentiation, or apoptosis. Regulation of B cell growth and differentiation. CD30 expression in activated T cells depends on CD28 signal transduction or IL-4. CD30 signals augment T cell proliferation, thymocyte survival.
Interaction
CD4 T cells, Th1, Th2, mast cells, macrophages, dendritic cells, B cells, neutrophils
Ligand/Receptor
CD30L (CD153)
Bioactivity
Recombinant human CD30-Fc chimera binds to immobilized recombinant human CD30L in a dose-dependent manner.
Cell Type
B cells, Dendritic cells, Granulocytes, Lymphocytes, Macrophages, Mast cells, Neutrophils, T cells, Th1, Th17, Th2
Biology Area
Cancer Biomarkers, Cell Biology, Immuno-Oncology, Immunology
Molecular Family
CD Molecules, Soluble Receptors
Antigen References
  1. Bowen NA, et al., 1996 J Immunol 156:442-9.
  2. Gilfillan MC, et al., 1998 J Immunol 160:2180-7.
  3. Schneider C and Hübinger G. 2002 Leuk Lymphoma 43:1355-66.
  4. Fabrina MC, et al., 2005 J Immunol 174:3891-6.
  5. Withers DR, et al., 2009 J Immunol 183:5079-84.
  6. Sun X, et al., 2010 J Immunol 185:2222-30.
  7. Muta H and Podack ER, 2013 Immunol Res 57:151-8.
  8. Kumar A, et al., 2013 Mediators Inflamm Article 2013:484378.
  9. Thakar NY, et al., 2015 Mol Biol Cell 26:993-1006.
  10. Van der Weyden CA, et al., 2017 Blood Cancer J. 7(9):e603. 
Gene ID
943 View all products for this Gene ID
UniProt
View information about CD30 on UniProt.org

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
Go To Top Version: 1    Revision Date: 12/07/2021

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

BioLegend Inc., 8999 BioLegend Way, San Diego, CA 92121 www.biolegend.com
Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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