Recombinant hCD268(BAFFR)-muIg

SKU:BHP14700016
Research Validated
Overview
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Recombinant human Murine IgG Fc Fusion (muIg) expressed in CHO Cells cells. Validated for ELISA. Human origin. Available unconjugated and conjugated (Biotin, FITC, PE).
Expression System CHO Cells
Fusion Format Murine IgG Fc Fusion
Molecular Weight 33.5 kDa
Species Reactivity Human
Storage 2–5°C
Validated Applications ELISA
Options selector
Catalog no. Form Size
524-020 Purified (with Antibiotic)
524-820 Purified (Preservative-free)
524-030 Biotin conjugate
Available Options

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

  • Options: Form (3) – Purified (with Antibiotic), Purified (Preservative-free), Biotin conjugate | Size: 25 µg
  • Lead time: options listed in "Availability Content"; other statuses may take longer.
  • Storage: Store at 2 - 5°C. Freeze/Thawing is not recommended.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: refrigerate upon receipt.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No 524
Conjugate
  • Biotin
  • Unconjugated
Formulation 50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150mM NaCl, 0.5% Gentamicin sulfate
Host CHO cells
Product Type
  • Recombinant Protein
Shipping Shipped on blue ice
Storage Store at 2 - 5°C. Freeze/Thawing is not recommended.

Scientific Background

The human B cell activating factor (BAFF) and APRIL(a proliferation inducing ligand) are both type II molecules belonging to the TNF superfamily. They are expressed by non-B cells, and are down regulated by mitogenic stimulation(2). BAFF and APRIL bind to at least two receptors: TACI (transmembrane activator and CAML-interactor) and BCMA (B cell maturation antigen), both of which are restricted to B cells(3,4). Ligation of these receptors with recombinant BAFF dramatically increases IgM production by peripheral blood B cells(1). A third receptor for BAFF (BAFF-R) has been described(5). BAFF and BAFFR knockout mice have a reduced numbers of mature B cells in the periphery, however TACI and BCMA knockouts do not share this phenotype, suggesting that BAFF-R may the primary receptor for BAFF in mice(8,9,10). Cell surface BAFF can be proteolytically cleaved to form a soluble trimeric molecule(2). Levels of soluble BAFF correspond with levels of autoantibodies in Sjogren’s Syndrome(11). Recombinant human BAFFR-muIg binds to recombinant BAFF-muCD8 and can inhibit binding of this molecule to receptors on Raji cells.

Product Description

CHO Cells

Recombinant hCD268(BAFFR)-muIg is a recombinant human fusion protein produced in CHO Cells cells. Molecular Structure: A soluble molecule consisting of the extracellular (60aa) domain of human BAFFR fused to the murine IgG2a Fc (232 aa). Predicted non glycosylated monomeric weight: 33.5 kd.

Protein Specifications

Fusion Format Murine IgG Fc Fusion (muIg)
Expression System CHO Cells
Molecular Weight 33.5 kDa
Formulation 50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150mM NaCl, 0.5% Gentamicin sulfate
Storage Store at 2 - 5°C. Freeze/Thawing is not recommended.
Species Reactivity Human
Validated Applications ELISA
Available Conjugates Biotin, Unconjugated

✔ Research Use Only (RUO)

Functional Activity

BAFFR-muIg binds to recombinant BAFF-muCD8 and can inhibit this molecule’s abiltiy to bind to receptors on Raji cells.

Safety & Handling

Research Use Only. Not intended for diagnostic, therapeutic, or clinical use. Handle according to good laboratory practice (GLP). Consult the Safety Data Sheet (SDS) prior to use.

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What expression system was used to produce Recombinant hCD268(BAFFR)-muIg?

This protein was expressed in CHO Cells cells. Mammalian expression is critical for this Fc fusion protein because it ensures proper glycosylation and tertiary folding of the extracellular immunoglobulin-like domains, preserving native receptor-binding activity.

Which applications has this product been validated for?

Recombinant hCD268(BAFFR)-muIg has been validated for: ELISA. It is produced as a Murine IgG Fc Fusion (muIg), making it suitable as a blocking reagent, binding standard, or functional stimulant/inhibitor in immunology assays.

How should I store this product?

Recommended storage: Store at 2 - 5°C. Freeze/Thawing is not recommended.. Formulation: 50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150mM NaCl, 0.5% Gentamicin sulfate. Avoid repeated freeze-thaw cycles. If long-term storage is needed, aliquot upon first use.

What species does this fusion protein cross-react with?

Species reactivity includes: human. Cross-reactivity was confirmed by functional binding assays (e.g., ELISA and/or FACS) against cells or recombinant proteins from the indicated species.

What conjugate formats are available for this product?

Available formats include: Biotin, Unconjugated. Conjugated forms are ready-to-use without secondary detection reagents for flow cytometry. Unconjugated (purified) forms can be used with anti-Fc secondary antibodies in ELISA.

Can't Find What You're Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

  1. Schneider P., J. Tschopp, et al. J. Exp. Med. 1999, 189(11):1747-1756.
  2. Shu, H.B., H. Johnson, W.H. Hui. J Leukoc Biol 1999, 65:680-683.
  3. Marsters, S.A., A. Ashkenazi, et al. 2000, Curr Biol 10:785-788.
  4. Xia, X., H. Hsu, et al. 2000, J Exp Med, 192(1): 137-143.
  5. Thompson J.S., C. Ambrose, et al. Science 2001, 293: 2108-2111.
  6. Roschke,V, T.S. Migone, et al. J Immunol . 2002, 169: 4314-4321.
  7. MacLennan, C.M., C.G. Vinuesa, 2002, Immunity 17:235-238.
  8. B. Schiemann, et al, (2001) Science 293: 2111-2114.
  9. S.M. Harless,et al, (2001) Curr Biol 11: 1988-1989.
  10. Mol Cell Biol (2001) 21: 4067-4074.
  11. X. Mariette, et al, (2003) Ann Rhem Dis 62: 168-171.
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