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Neurturin Protein, Human, Recombinant

Neurturin Protein, Human, Recombinant

Catalog Number: orb1961048

DispatchUsually dispatched within 5-10 working days
$ 230.00
Catalog Numberorb1961048
CategoryProteins
DescriptionNeurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. Neurturin is expressed in both neuronal and nonneuronal tissues. Similarly to other TGFβ family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain. The carboxy terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Unlike other members of TGF-β family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFRα-1-GFRα-4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations. It may play a role in regulating the development and maintenance of the central and peripheral nervous systems and as well as non neuronal systems.
TagTag Free
Purity98.00%
MW15 KDa (reducing condition)
UniProt IDQ99748
Protein SequenceAla96-Val197
Expression SystemE. coli
Biological OriginHuman
Biological ActivityNeurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. Neurturin is expressed in both neuronal and nonneuronal tissues. Similarly to other TGFβ family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain. The carboxy terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Unlike other members of TGF-β family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFRα-1-GFRα-4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations. It may play a role in regulating the development and maintenance of the central and peripheral nervous systems and as well as non neuronal systems.
Expression RegionAla96-Val197
Storage-20°C
NoteFor research use only
Application notesReconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Expiration Date6 months from date of receipt.
  • Human GFRA2 protein [orb391796]

    ELISA,  MS,  SDS-PAGE,  WB

    Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.

    Human cells

    500 μg, 50 μg, 10 μg
  • Human GFRA2 protein [orb391797]

    ELISA,  MS,  SDS-PAGE,  WB

    Greater than 95% as determined by reducing SDS-PAGE.

    Human cells

    500 μg, 50 μg, 10 μg
  • Human NRTN protein [orb707013]

    ELISA,  MS,  SDS-PAGE,  WB

    Greater than 95% as determined by reducing SDS-PAGE.

    E. coli

    50 μg, 500 μg, 10 μg
  • Persephin Protein, Human, Recombinant [orb1961611]

    98.00%

    12 KDa (reducing condition)

    1 mg, 500 μg, 50 μg, 10 μg
  • GFR Alpha-2/GFRA2 Protein, Human, Recombinant (hFc & His) [orb1961951]

    98.00%

    120 KDa (reducing condition)

    500 μg, 50 μg, 10 μg, 1 mg