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You are here:Home » Molecular Biology » MB-Neurotrophins » Persephin, Recombinant, Mouse (PSP, Pspn)

Persephin, Recombinant, Mouse (PSP, Pspn)

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Specifications

Persephin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, Artemin, and Neurturin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFRa (a1-a4) receptors. The GFRa4 was first identified in chicken and was later shown to be the preferential binding subunit for Persephin. Persephin promotes the survival of ventral midbrain dompaminergic neurons and motor neurons after sciatic nerve oxotomy, and like GNDF, promotes ureteric bud branching. However, in contrast to GDNF and Neurturin, Persephin does not support survival of peripheral neurons. Recombinant murine Persephin is a disulfide-linked homodimer, composed of two 10.3kD polypeptide chains (96 total aa residues). Each chain contains seven conserved cysteine residues, one of which (Cys 63) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.
Catalog #143468
Biological ActivityThe ED50 was determined by its ability to stimulate proliferation of human thyroid carcinoma cells (TT cells) is ~0.1ng/ml, corresponding to a specific activity of ~1x10e7 units/mg.
AA SequenceALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
CrossreactivityHuman
Quality ControlVerified by N-terminal and Mass Spectrometry analyses (when applicable).
Endotoxin<0.1ng/ug of protein (<1EU/ug).
Protein ContentVerified by UV Spectroscopy and/or SDS-PAGE gel.
Storage and StabilityStore lyophilized products at -20°C. For reconstituted solutions of most products, we recommend short-term storage at 4°C. For longer term storage the protein solution should be stored with a carrier protein (eg. 0.1% BSA) in working aliquots and stored frozen at -20°C. Additional freeze/thaw cycles may cause some denaturation of the protein.
SourceE. coli
Purity98% by SDS-PAGE gel and HPLC analyses.
FormSupplied as a lyophilized powder.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.


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