ELISA with Human CD27/TNFRSF7 Protein 4896

Human CD27/TNFRSF7 Protein 4896

$165.00 – $550.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Thr21-Ile192

SKU: 4896parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P26842
express system	HEK293
product tag	C-hFc
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	CD27, also known as TNFRSF7, is an approximately 55 kDa transmembrane protein in the TNF receptor superfamily. It functions as a co‑stimulatory molecule that supports lymphocyte activation and survival. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis.
molecular weight	The protein has a predicted MW of 46.2 kDa. Due to glycosylation, the protein migrates to 60-75 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human CD27/TNFRSF7 Protein 4896

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
CD27, also known as TNFRSF7, is an approximately 55 kDa transmembrane protein in the TNF receptor superfamily. It functions as a co-stimulatory molecule that supports lymphocyte activation and survival. It binds to ligand CD70, and plays a key role in regulating B-cell activation and immunoglobulin synthesis.
Protein names CD27 antigen (CD27L receptor) (T-cell activation antigen CD27) (T14) (Tumor necrosis factor receptor superfamily member 7) (CD antigen CD27)
Gene names CD27,CD27 TNFRSF7
Mass 29137Da
Function FUNCTION: Costimulatory immune-checkpoint receptor expressed at the surface of T-cells, NK-cells and B-cells which binds to and is activated by its ligand CD70/CD27L expressed by B-cells (PubMed:28011863). The CD70-CD27 signaling pathway mediates antigen-specific T-cell activation and expansion which in turn provides immune surveillance of B-cells (PubMed:28011863). Mechanistically, CD70 ligation activates the TRAF2-PTPN6 axis that subsequently inhibits LCK phosphorylation to promote phenotypic and transcriptional adaptations of T-cell memory (PubMed:38354704). In addition, activation by CD70 on early progenitor cells provides a negative feedback signal to leukocyte differentiation during immune activation and thus modulates hematopoiesis (By similarity). Negatively regulates the function of Th2 lymphocytes in the adipose tissue (By similarity). {ECO:0000250\|UniProtKB:P41272, ECO:0000269\|PubMed:28011863, ECO:0000269\|PubMed:38354704}.
Subellular location SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:28011863}; Single-pass type I membrane protein {ECO:0000255}.
Tissues TISSUE SPECIFICITY: Found in most T-lymphocytes. {ECO:0000269\|PubMed:1655907}.
Structure SUBUNIT: Homodimer (PubMed:1655907, PubMed:34419446). Interacts with SIVA1; may play a role in apoptosis through association with SIVA1 (PubMed:9177220). Interacts with TRAF2 (PubMed:38354704, PubMed:9692890). Interacts ith PTPN6 (PubMed:38354704). {ECO:0000269\|PubMed:1655907, ECO:0000269\|PubMed:34419446, ECO:0000269\|PubMed:38354704, ECO:0000269\|PubMed:9177220, ECO:0000269\|PubMed:9692890}.
Post-translational modification PTM: Phosphorylated. {ECO:0000303\|PubMed:1655907}.; PTM: N-glycosylated. {ECO:0000269\|PubMed:34419446}.; PTM: O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269\|PubMed:22171320}.
Target Relevance information above includes information from UniProt accession: P26842
The UniProt Consortium

Data

No results found

Publications

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We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.