Name :
Human NGFR Protein, ECD (Extracellular Domain), Fc-fusion, Biotinylated, Recombinant
Description :
NGFR (nerve growth factor receptor), also known as Low affinity neurotrophin receptor p75NTR and CD271, is a single-pass type I transmembrane glycoprotein in the TNF receptor superfamily (TNFRSF16). The extracellular region contains four cysteinerich domains and binds NGF, BDNF, NT3 and NT4 approximately equally with low affinity. The cytoplasmic region contains a death domain (DD). NGFR is widely expressed during development and in the adult. Expression has been detected in both neuronal and nonneuronal cells. NGFR was originally reported to function as a positive regulator of TrkA, a high- affinity nerve growth factor receptor. NGFR has also been shown to signal by itself. Depending on its cellular environment, NGFR has now been shown to regulate cell migration, gene expression and to mediate apoptosis. Recombinant NGF R/Fc chimera binds NGF with high affinity and is a potent NGF antagonist. Naturally occurring truncated NGF R containing the extracellular domain and lacking the transmembrane or intracellular domain has been detected in vivo in urine, plasma and in amniotic fluid of humans and animals. NGFR is also necessary for the circadian oscillation of the clock genes in the suprachiasmatic nucleus of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver. It may plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin and thereby contributes to the regulation of insulin-dependent glucose uptake.
Gene Symbol :
TNFRSF16; CD271; p75NTR; p75(NTR); Gp80-LNGFR; p75 ICD
NCBI Gene ID :
4804
Uniprot Entry :
P08138
Construct Details :
The recombinant human NGFR-Fc fusion is expressed as a 450 amino acid protein consisting of Lys29 -Asn250 region of NGFR (UniProt accession #P08138) and a C-terminal Fc from human IgG1, which exists as a dimer under non-reducing conditions (see the gel image inserted above).
Source :
Human cells stably expressing human NGFR-Fc and growing in chemical-defined media with no animal components or antibiotics
Amino Acid Sequence: :
10 20 30 40 50 60 KEACPTGLYT HSGECCKACN LGEGVAQPCG ANQTVCEPCL DSVTFSDVVS ATEPCKPCTE 70 80 90 100 110 120 CVGLQSMSAP CVEADDAVCR CAYGYYQDET TGRCEACRVC EAGSGLVFSC QDKQNTVCEE 130 140 150 160 170 180 CPDGTYSDEA NHVDPCLPCT VCEDTERQLR ECTRWADAEC EEIPGRWITR STPPEGSDST 190 200 210 220 230 240 APSTQEPEAP PEQDLIASTV AGVVTTVMGS SQPVVTRGTT DNSTGTHTCP PCPAPELLGG 250 260 270 280 290 300 PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN 310 320 330 340 350 360 STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSREE 370 380 390 400 410 420 MTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW 430 440 450 QQGNVFSCSV MHEALHNHYT QKSLSLSPGK
M.W. :
Calculated molecular mass (kDa): 49.1; Estimated by SDS-PAGE under reducing condition (kDa): 70-80
Calculated PI :
4.80
Calculated Extinction Coefficients :
(M-1 cm-1, at 280nm): 55735
Endotoxin Level :
>95% judged by SDS-PAGE under reducing condition (see the gel image above, labeled as “DTT: +”)
Formulation :
Supplied at 0.5 mg/ml in sterile PBSpH7.4 (carrier & preservative free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure.
Endotoxin Level :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Biological Activity :
Binds to its ligand NGF and inhibits NGF dependent proliferation of human TF-1 erythroleukemic cells.
Molecule Class :
1-Pass Type I Transmembrane
Gene Synonym :
<0.1 EU per 1 μg of purified recombinant protein determined by the LAL method
Gene Family :
TNFRSF16; CD271; p75NTR; p75(NTR); Gp80-LNGFR; p75 ICD
Research Area :
Neuroscience
Pathway/Disease :
Biological Rhythms
Species :
Human
CD Antigen :
CD271
References :
1. Cell 47:545-554 (1986). 2. J. Cell Biol. 140:911 (1998). 3. J Biol Chem. 279 (3): 1703 (2004). 4. Mol Biol Cell. 20 (16): 3620 (2009). 5. J. Neurosci. 33:10221 (2013).
Related category websites: https://www.medchemexpress.com/recombinant-proteins.html
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