PSPN Human

Persephin Human Recombinant
Cat. No.
BT11396
Source
Escherichia Coli.
Synonyms

Persephin, PSP, PSPN.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa.                   
The PSPN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
As a member of the GDNF ligand subfamily within the TGF-beta superfamily, Persephin plays a crucial role in the survival and growth of essential dopaminergic and motor neurons. It is also involved in kidney development. However, it's important to note that persephin does not contribute to the survival of peripheral neurons.
Description
Recombinant Human PSPN, produced in E. coli, is a homodimer linked by disulfide bonds. It consists of two chains, each containing 96 amino acids, resulting in a molecular weight of 20.5kDa.
The purification of PSPN is achieved using proprietary chromatographic techniques.
Physical Appearance
White powder, sterile filtered and lyophilized (freeze-dried).
Formulation
Lyophilized from a concentrated solution (0.2µm filtered) in PBS with a pH of 7.4.
Solubility
To reconstitute the lyophilized PSPN, it is recommended to dissolve it in 4mM HCl at a concentration of at least 100µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized PSPN remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. Once reconstituted, PSPN should be stored at 4°C for a period of 2 to 7 days. For extended storage, it is advisable to add a carrier protein (0.1% HSA or BSA) and store it below -18°C. Repeated freeze-thaw cycles should be avoided.
Purity
Exceeds 95.0% purity, as determined by: (a) RP-HPLC analysis and (b) SDS-PAGE analysis.
Biological Activity
Demonstrates full biological activity when compared to the standard. The ED50, determined by a cell proliferation assay using human TT medullary thyroid cancer cells, is less than 10ng/ml. This corresponds to a specific activity greater than 1.0 × 100,000 IU/mg.
Synonyms

Persephin, PSP, PSPN.

Source
Escherichia Coli.
Amino Acid Sequence

ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.

Product Science Overview

Structure and Expression

Persephin is a secreted protein that forms a disulfide-linked homodimer . The recombinant human Persephin protein is typically produced in E. coli and has a predicted molecular mass of approximately 10.3 kDa per monomer . It is expressed at very low levels in most tissues .

Biological Activity

Persephin promotes the survival of mesencephalic, dopaminergic, and motor neurons . Unlike other members of the GDNF family, Persephin does not support the survival of neurons from peripheral ganglia, including sympathetic, parasympathetic, sensory, and enteric neurons . However, it does promote the survival of midbrain dopaminergic neurons after neurotoxic injury and the survival of spinal motor neurons .

Receptor Interaction

The receptor for Persephin is a multi-component complex composed of the RET tyrosine kinase and the glycosyl-phosphatidylinositol (GPI)-anchored co-receptor GFRα1-α4 . This interaction is crucial for its neurotrophic activities.

Potential Therapeutic Applications

Experiments using animal models suggest that Persephin could be useful in the treatment of neurodegenerative diseases, including Parkinson’s disease and Amyotrophic Lateral Sclerosis (ALS) . Its ability to promote neuron survival makes it a promising candidate for therapeutic development.

Research and Usage

Recombinant human Persephin is used in various research applications, including cell proliferation assays and studies on neuroprotection . It is typically lyophilized and reconstituted in sterile solutions for experimental use .

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