Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 13C Protein (TNFRSF13C), Active

Name: Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 13C Protein (TNFRSF13C), Active
Brand: Beta LifeScience
SKU: BLC-06047P
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins, Tumor necrosis factors and receptors (tnfs)

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Product Overview

Description	Recombinant Human Tumor Necrosis Factor Receptor Superfamily Member 13C Protein (TNFRSF13C), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by its ability to block BAFF induced mouse splenocyte survival is 1.0-5.0 ug/ml in the presence of 1.0 μg/ml of rHuBAFF.
Uniprotkb	Q96RJ3
Target Symbol	TNFRSF13C
Synonyms	B cell activating factor receptor; B-cell-activating factor receptor; BAFF R; BAFF receptor; BAFF-R; BAFFR; BLyS receptor 3; BlySR3; BR 3; BR3; BROMIX; CD 268; CD268; CD268 antigen; CVID4; MGC138235; OTTHUMP00000028746; Prolixin; TNFRSF 13C; Tnfrsf13c; TR13C_HUMAN; Tumor necrosis factor receptor subunit member 13C; Tumor necrosis factor receptor superfamily member 13C
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	MRRGPRSLRG RDAPAPTPCV PAECFDLLVR HCVACGLLRT PRPKPAGASS PAPRTALQPQ ESVGAGAGEA ALPLPG
Expression Range	1-76aa
Protein Length	Partial
Mol. Weight	7.8 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered 20 mM PB, pH 8.0, 500 mM NaCl
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response.
Subcellular Location	Membrane; Single-pass type III membrane protein.
Database References	HGNC: 17755 OMIM: 606269 KEGG: hsa:115650 STRING: 9606.ENSP00000291232 UniGene: Hs.344088
Associated Diseases	Immunodeficiency, common variable, 4 (CVID4)
Tissue Specificity	Highly expressed in spleen and lymph node, and in resting B-cells. Detected at lower levels in activated B-cells, resting CD4+ T-cells, in thymus and peripheral blood leukocytes.

Gene Functions References

the B-cell receptor BR3 modulates cellular branching via Rac1 during neuronal migration PMID: 27436754
Expression patterns of BAFF and its receptor BAFF-R differ according to lupus nephritis class. PMID: 29087261
up-regulated expression in intractable temporal lobe epilepsy PMID: 28441631
Inhibition of ADAM10 augments BAFF-dependent survival of primary human B cells, whereas inhibition of ADAM17 increases BAFFR expression levels. PMID: 28249164
Relationships between serum BAFF and BBR expression [(BAFFR, calcium signal modulating cyclophilic ligand interactor (TACI) and B cell maturation antigen (BCMA)] were determined on B cell subsets, defined using immunoglobulin (Ig)D/CD38. Twenty pre-RTX and 18 rheumatoid arthritis patients relapsing after B cell depletion were included. PMID: 28800164
Among the BAFF receptors in a cohort of rheumatoid arthritis (RA) patients, the AA have shown, by fluorescence activated cell sorter (FACS) analysis of median fluorescence intensity (MFI), that transmembrane activator and calcium-modulating cyclophilin ligand interactor (TACI) and B cell maturation antigen (BCMA) do not change PMID: 28834574
The expression levels of serum BAFF and the three receptors (TACI, BCMA and BAFF-R) in non-Hodgkin lymphoma patients were significantly higher than in healthy controls. PMID: 28028945
Variants in BAFF-R gene is associated with chronic lymphocytic leukemia. PMID: 27468724
BAFF-R, as the principal receptor of BAFF, not only decreased the apoptosis of B cells and CD8+ T cells by upregulating the expression of Bcl-2 and BclxL, but also promoted B-cell proliferation in immune thrombocytopenia. PMID: 26749059
genetic polymorphism contributes to the pathogenesis of primary antibody deficiency PMID: 26613719
BAFF and BAFF-R are expressed in the thyrocytes derived from patients with either autoimmune thyroid disorders or multinodular goiter, as well in the infiltrating immune cells of Graves' disease and Hashimoto's thyroiditis PMID: 26214745
There is an increased prevalence of the BAFF-R His159Tyr mutation in patients with Sjogren's syndrome (SS), particularly in those with SS complicated by MALT lymphoma whose disease onset occurred at a younger age. PMID: 26097183
Expression of mutant caspase-9 correlated with a downregulation of BAFFR (B-cell-activating factor belonging to the TNF family (BAFF) receptor) in B cells and ICOS (inducible T-cell costimulator) in T cells. PMID: 25569260
Variants of TNFRSF13C were associated with common variable immunodeficiency. PMID: 26122175
Negative expression of BAFF-R, but not of BAFF, could be an independent risk factor for progression-free survival and Overall survival in patients with diffuse large B-cell lymphoma treated with standard R-CHOP. PMID: 26327569
the common TLR4-D299G, TLR4-T399I and BAFFR-P21R polymorphisms provide the carriers with a protective advantage against ICU-acquired sepsis; this finding was more profound for medical patients compared to trauma or surgical ones PMID: 25454804
Data show significant differences in expression of tumour necrosis factor family (BAFF) receptors BAFF-R, BCMA and TACI in patients with and without anti-Jo-1 or anti-Ro52/anti-Ro60 autoantibodies. PMID: 25301447
In view of the restricted expression of the BAFF-R on normal cells and the multiple anti-pre-B ALL activities stimulated by this antibody, a further examination of its use for treatment of pre-B ALL is warranted. PMID: 24825858
Availability of BAFF determines BAFF-R and TACI expression on B cells in common variable immunodeficiency. PMID: 24809296
Our study demonstrates that BR3 is involved in the survival of cultured epithelial cells due to an autocrine effect of BAFF. PMID: 24602383
BAFF-R, but not BAFF, may have a role in progression-free survival and overall survival in follicular lymphoma PMID: 23272079
BLyS and its receptors are expressed by B lymphocytes in the peripheral blood and the bone marrow of patients with multiple myeloma. PMID: 23276925
P21R/H159Y TNFRSF13C compound heterozygous mutation and P21R heterozygous mutations were detected in Turkish patients with common variable immunodeficiency. PMID: 22699762
BAFF-R expression is tightly regulated during B-cell development in mouse and human and this exprssion is correlated with posirive selection. PMID: 22028296
It was also found that NF-kappaB was an important transcription factor involved in regulating BAFF-R expression through one NF-kappaB binding site in the BAFF-R promoter PMID: 21607696
Soluble BAFF levels inversely correlate with peripheral B cell numbers and the expression of BAFF receptors. PMID: 22124120
The activation profile of diffuse large B-cell lymphomas/posttransplantation lymphoproliferative disorders was not associated with BAFF/BAFF-R expression, whereas nuclear p52 activation might be linked to Epstein-Barr virus. PMID: 21871426
The human BAFF-R gene might be regulated via a transcriptional event through one putative NF-kappaB site on the BAFF-R gene promoter. PMID: 21744373
reduced expression via inhibition of the NF-KappaB pathway in B cells of rheumatoid arthritis patients PMID: 21515993
primary leukemia B-cell precursors aberrantly express receptors of the BAFF-system, BAFF-R, BCMA, and TACI PMID: 21687682
This is the first study, presenting together the TNFSF members APRIL, BAFF, TWEAK and their receptors in different areas of normal renal tissue and renal cell carcinoma. PMID: 21483105
BLyS and its receptors might have a potential role in the growth and survival of malignant plasma cells. PMID: 19731825
Results describe the mechanisms underlying aberrant BAFF-R expression in precursor B acute lymphoblastic leukemia (precursor B-ALL) and mature B chronic lymphocytic leukemia (CLL). PMID: 21099364
BAFF-R was rather specifically related to low growth activity of germinal center B-cell-like -type diffuse large B-cell lymphoma of nodal origin. PMID: 21123970
inverse correlation between BAFF and APRIL in Kawasaki disease is reversed by IVIG treatment PMID: 20945608
Elevated plasma BAFF and reduced BAFF receptor 3 (BR3) protein expression on peripheral B cells could act as biomarkers for active disease in systemic lupus erythematosus patients PMID: 20974656
a novel lymphoma-associated mutation in human BAFF-R that results in NF-kappaB activation and reveals TRAF6 as a necessary component of normal BAFF-R signaling. PMID: 21041452
Data from BAFF-R-expressing cells suggested potential regulatory sites in TNFRSF13C promoter region. PMID: 20554963
This report is the first showing universal expression of BAFF-R by pre-B ALL cells. PMID: 20460528
IFN-gamma and the NF-kappaB pathway could be involved in regulating the transcription and mRNA expression of BAFF-R gene. PMID: 20230666
the mechanism of transcriptional regulation of BAFF-R PMID: 20025535
BAFF-R is a receptor for the TNF family member ligand, BAFF [review] PMID: 12456020
BAFFR-mediated NF-kappa B activation and IL-10 production in B cells is downregulated by TNFR-associated factor-3. PMID: 12471121
crystal structure and interaction with BAFF protein PMID: 12715002
BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site. PMID: 12755599
Expression of BCMA, TACI, and BAFF-R by multiple myeloma cells support cell growth and survival. PMID: 14512299
This study reports the crystal structure of a 24-residue fragment of the cytoplasmic portion of BAFF-R bound in complex with TRAF3. PMID: 15585864
the PVPAT sequence of BAFFR not only functions as a key signaling motif of BAFFR but also determines its signaling specificity in the induction of the noncanonical NF-kappaB pathway PMID: 15644327
amino acid sequence of genomic DNA from blood of common variable immunodeficiency patients;mutations may result in humoral immunodeficiency PMID: 16160919
BAFF-R is expressed on most mature B cells and B-cell lymphoproliferative disorders. PMID: 16226112

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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