|Calculated MW||10.3 kDa|
|Other Names||PSP, PSPN|
|Sequence||ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.|
|Storage||-20°C; Sterile filtered through a 0.2 micron filter. Lyophilized from 10 mM Sodium Citrate, pH 4.0|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
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 GFRα (α1-α4) receptors. The GFRα4 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 10.3 kDa polypeptide chains (96 total amino acid 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.
Milbrandt J.,et al.Neuron 20:245-253(1998).
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