Recombinant Human CD30 (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
TNFRSF8, CD30L Receptor, Ki-1 Antigen, Cytokine Receptor CD30, TNF Receptor Superfamily Member 8
Ave. Rating
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Product Citations
publications
a.
Human_CD30_CF_RECOM_1_011224
When recombinant human CD30 is immobilized at 1 µg/mL, recombinant human CD30L (Cat. No. 767104) binds in a dose-dependent manner with ED50 of 5 – 30 ng/mL.
  • a.
Human_CD30_CF_RECOM_1_011224
    When recombinant human CD30 is immobilized at 1 µg/mL, recombinant human CD30L (Cat. No. 767104) binds in a dose-dependent manner with ED50 of 5 – 30 ng/mL.
  • b.
Human_CD30_CF_RECOM_2_011224
    Stability Testing for Recombinant human CD30. Human CD30 was aliquoted in PBS. One aliquot was frozen and thawed four times (4x Freeze/Thaw) and compared to a control kept at 4°C (Control). The samples were tested in a binding assay with recombinant human CD30L. The ED50 for this effect is 5 – 30 ng/mL.
Cat # Size Price Save
564204 25 µg ¥67,660
564206 100 µg ¥124,380
Description

CD30, also known as TNFRSF8, is a member of the tumor necrosis factor (TNF) receptor superfamily and was originally identified as a cell surface antigen Ki-1, on Hodgkin and Reed-Sternberg cells. Human CD30 is a 120 kD type I transmembrane glycoprotein, bearing the 361 amino acid extracellular domain with six cysteine-rich repeats, a short transmembrane domain, and a 188 amino acid cytoplasmic domain. CD30 can be cleaved by cell membrane-anchored metalloproteinases and then released from the cell as a soluble form protein. CD30 is expressed on activated T, B, and NK cells, but not on resting T, and B cells. CD30 is also highly expressed in, among others, classical Hodgkin lymphoma (HL) and anaplastic large cell lymphoma (ALCL). CD30 interacts with a number of proteins including TRAF1, TRAF2, TRAF3, TRAF5, NPM-ALK, TRAF-interacting protein, and CD30 ligand (CD153). Signaling through CD30 is thought to limit the proliferative potential of autoreactive CD8 effector T cells and protect against autoimmunity. CD30 mediates the signal transduction that leads to the activation of the nuclear factor kappaB (NF-kB) transcription factor. Coexpression of CD30 with TRAF1 augments NF-kB activation. In addition, CD30 also has been identified as a critical therapeutic target for lymphoma immunotherapy. CD30L/CD30 signaling has been implicated in the pathogenesis of several autoimmune and inflammatory conditions, such as rheumatoid arthritis (RA). Furthermore, CD30L/CD30 signaling appears to be involved in Th1 and Th2 cell responses and plays a key role in Th17 differentiation in mice.

Product Details
Technical data sheet

Product Details

Source
Human CD30, amino acid (Phe19-Gly385) (Accession: #P28908.1), with N-terminal 9His and a linker (SGGGSGGGIEGR), was expressed in CHO cells
Molecular Mass
The 388 amino acid recombinant protein has a predicted molecular mass of approximately 41.18 kD. The DTT-reduced and non-reduced protein migrates at approximately 60-80 kD 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 is in PBS.
Endotoxin Level
Less than 0.1 EU per µg of 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 and expiration, please enter the lot number in our Certificate of Analysis online tool.
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
When recombinant human CD30 is immobilized at 1 µg/mL, human CD30L (Cat. No. 767104) binds in a dose-dependent manner with ED50 of 5 – 30 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
Monomer
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 CD30L binds to immobilized recombinant human CD30 in a dose-dependent manner.
Cell Type
B cells, Embryonic Stem Cells, Tregs
Biology Area
Immunology, Stem Cells
Molecular Family
CD Molecules
Antigen References
  1. Hymowitz, S, et al. 2005. J Biol Chem. 280:7218-27.
  2. Ingold K, et al. 2005. J Exp Med. 201:1375-83.
  3. Good K, et al. 2009. J Immunol. 182:890-901.
  4. Bossen C, et al. 2008. Blood. 111:1004-12.
  5. Bossen C, et al. 2006. J Biol Chem. 281:13964-71.
  6. Pradet-Balade B, et al. 2002. EMBO J. 21:5711-20.
  7. Hahne M, et al. 1998. J Exp Med. 188:1185-90.
  8. Medema JP, et al. 2003. Cell Death Differ. 10:1121-5.
  9. Planelles L, et al. 2007. Haematologica. 92:1284-5.
  10. Dillon SR, et al. 2010. Arthritis Res. Ther 12:R48.
  11. Wallweber H, et al. 2004. J Mol Biol. 343:283-90.
  12. Chen Y, et al. 2011. PLoS ONE 6:e22202.
  13. Roschke V, et al. 2002. J. Immunol. 169:4314-21.
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) = 10^6/ ED50 (ng/mL)

Go To Top Version: 1    Revision Date: 12/06/2023

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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