Recombinant Human Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), partial

SKU:BHP10500992
Overview
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Recombinant TNFRSF21 Human protein produced in E. coli, N-terminal 6xHis-SUMO-tagged spanning 371-655aa. Suitable for binding assays, functional studies, and assay development.
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Species Homo sapiens (Human)
Molecular Weight 48 kDa
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 1 mg, 100 ug, 20 ug
  • Lead time: Made to Order — production begins after purchase. Lead time is typically 13-23 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Options selector
Catalog no. Size
CSB-EP023979HU-1MG 1 mg
CSB-EP023979HU-100UG 100 ug
CSB-EP023979HU-20UG 20 ug
Field Specification
Activity
  • Not Test
Alternative Names Death receptor 6; CD358
Endotoxin Level Not test
Expression System
  • E. coli
Form Liquid or Lyophilized powder
Function
  • Promotes apoptosis
  • possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis
  • including apoptosis in response to amyloid peptides derived from APP
  • and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21; this triggers caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Negatively regulates oligodendrocyte survival
  • maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors
  • in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4
  • IL5
  • IL10
  • IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG
  • IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation.
Molecular Weight 48 kDa
Product Type
  • Recombinant Protein
Purity Greater than 90% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # O75509

Scientific Background

Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning.

Product Description

E. coli Expression

Recombinant Human Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), partial is a recombinant protein expressed in E. coli and purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Liquid or Lyophilized powder, n-terminal 6xhis-sumo-tagged. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 48 kDa
Expression Region 371-655aa
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Form Liquid or Lyophilized powder
Storage Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Endotoxin Level Not test
UniProt Accession O75509
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as N-terminal 6xHis-SUMO-tagged and has been purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Biological activity data are available in the product datasheet. Please contact our support team for activity specifications relevant to your specific application.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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