CD27/TNFRSF7 Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human CD27. Source: E. coli
Amino Acid Sequence: HQRRKYRSNKGESPVEPAEPCRYSCPREEEGSTIPIQEDYR Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
CD27 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10 - 100 molar excess
|
Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-38434. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml. For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
Theoretical MW |
22 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. |
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
PBS and 1M Urea, pH 7.4. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for CD27/TNFRSF7 Recombinant Protein Antigen
Background
CD27, also referred to as tumor necrosis factor receptor superfamily, member 7 (TNFRSF7), is a type I transmembrane glycoprotein that functions as a co-stimulatory T cell receptor and is expressed on the surface of T cells, natural killer (NK) cells, and B cells (1,2). The human CD27 protein is 260 amino acids (aa) in length and consists of a 19 aa signal sequence, 172 aa extracellular domain (ECD) containing three characteristic cysteine-rich domains (CRDs), a 21 aa helical transmembrane region, and a 48 aa cytoplasmic tail domain (3,4). The CD27 protein has a theoretical molecular weight (MW) of 29 kDa, but is typically is closer to 50-55 kDa due to N-linked and O-linked glycosylation (3). Mouse CD27 cDNA encodes a 250 aa protein with a theoretical molecular weight of 28 kDa (5). Human CD27 shares ~64% aa sequence identity with mouse CD27 protein.
Membrane-bound CD27 is expressed as a disulfide-linked homodimer (3). CD27 binds to the ligand CD70, a transmembrane glycoprotein that is transiently expressed on activated immune cells such as antigen presenting cells (APCs), dendritic cells (DCs), NK cells, B cells, and T cells (1,2,6,7). The receptor-ligand binding interaction leads to NFkappaB and c-Jun pathway activation which promotes immune stimulation and activation and survival of CD4+ T cells, CD8+ T cells, memory T cells, and NK cells (2,6,7). Both CD27 and CD70 are often abnormally expressed or dysregulated on malignant and cancer cells leading to immune evasion and tumor progression (7). CD27 has become a target of interest of immunotherapies for viral infections, autoimmune disease, and cancer (2). Varlilumab, an agonistic CD27 monoclonal antibody (mAB), has entered clinical trials for the treatment of hematological and solid tumor cancers (1,6). Additional clinical trials are in process that combine varlilumab with other immune checkpoint inhibitors like the programmed cell death protein-1 (PD-1) blocking mAb nivolumab (1,2). Initial results are promising, suggesting that targeting CD27, especially in combination with other therapeutics, may be a promising and effective immunotherapy for a variety of pathologies (1,2,6).
References
1. Starzer AM, Berghoff AS. New emerging targets in cancer immunotherapy: CD27 (TNFRSF7). ESMO Open. 2020;4(Suppl 3):e000629. https://doi.org/10.1136/esmoopen-2019-000629
2. Grant EJ, Nussing S, Sant S, Clemens EB, Kedzierska K. The role of CD27 in anti-viral T-cell immunity. Curr Opin Virol. 2017;22:77-88. https://doi.org/10.1016/j.coviro.2016.12.001
3. Buchan SL, Rogel A, Al-Shamkhani A. The immunobiology of CD27 and OX40 and their potential as targets for cancer immunotherapy. Blood. 2018;131(1):39-48. https://10.1182/blood-2017-07-741025
4. Uniprot (P26842)
5. Uniprot (P41272)
6. van de Ven K, Borst J. Targeting the T-cell co-stimulatory CD27/CD70 pathway in cancer immunotherapy: rationale and potential. Immunotherapy. 2015;7(6):655-667. https://doi.org/10.2217/imt.15.32
7. Flieswasser T, Van den Eynde A, Van Audenaerde J, et al. The CD70-CD27 axis in oncology: the new kids on the block. J Exp Clin Cancer Res. 2022;41(1):12. https://doi.org/10.1186/s13046-021-02215-y
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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