human GDNF proDomain

SKU:BHP21300119 Toxins and Venom Peptides
Suppliers
Alomone Labs
Alomone Labs
Details Products
Overview
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human GDNF proDomain is supplied as a reagent reagent. Key specifications include Form: Lyophilized; Purity: ≥98% (HPLC); MW: 6334 Da. Commonly used in neuroscience studies, including measure target modulation in patch-clamp electrophysiology (dose–response) and profile target pharmacology in cell-based assays (concentration–response + time-course).
Purity ≥98% (HPLC)
Molecular Weight 6334 Da
Form Lyophilized
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options:
    Size: 10 mcg
    Quantity (2) - 1, 5
  • Lead time: typically ships in ~1-2 business days; timing may vary by selected option.
  • Storage: Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No SPG-100
Activity
  • Different peptides which are part of the GDNF proDomain sequence can induce synaptic excitability and possess some dopaminergic activities in vitro (thus named dopamine neuron-stimulating peptides)
  • in addition to possessing neurotrophic-like properties1-3.
Form Lyophilized
Formulation Lyophilized Powder.
Molecular Weight 6334 Da
Product Type
  • Proteins & Peptides
  • Proteins
Purity ≥98% (HPLC)
Reconstitution Centrifuge the vial (10,000 × g for 5 minutes) before adding solvent to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Gently tap, tilt, and roll the vial to aid dissolution. Avoid vigorous vortexing; light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. Repeated freeze-thaw cycles may result in loss of activity.
Solubility Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. Repeat freeze-thawing may result in loss of activity.
Source Synthetic protein
Storage Storage before reconstitution: The product is shipped as a lyophilized powder at room temperature. Upon receipt, store the product at -20°C. Protect from moisture. Storage after reconstitution: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles. Storage of solutions: The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods (up to 6 months), small aliquots should be stored at -20°C. We do not recommend storing the product in working solutions for longer than a few days. Avoid multiple freeze-thaw cycles.
Target proGDNF

Overview

human GDNF proDomain is a research-grade protein/peptide reagent used in research settings. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows.

Key elements and design rationale

  • Molecular identity: MW: 6334 Da, Formula: C279H433N79O86S2.
  • Source / origin: Synthetic protein.
  • Quality attributes: Purity: ≥98% (HPLC); Sterile / endotoxin-free: Yes.

When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.

Biological background

Glial-Derived Neurotrophic Factor (GDNF) is a member of the TGF-β superfamily. GDNF signals through a multi-component receptor system, composed of a RET protooncogene and one of the four α1-α4 receptors1.GDNF promotes survival of various neuronal cells, including motoneurons2,3, Purkinje cells and sympathetic neurons4. In embryonic midbrain cultures, GDNF promotes the survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake5. Cells that express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells6, neurons, pinealocytes, and skeletal muscle cells7.In vivo, following transection of facial motor neuron axons, locally applied GDNF has been shown to rescue virtually all damaged neurons from death8. GDNF may be of clinical relevance in the treatment of Parkinson's disease that is characterized by progressive degeneration of midbrain dopaminergic neurons9,10.Recently, it has been hypothesized that functional, carboxy-terminally amidated peptides are processed from the GDNF precursor upon proteolytic cleavage by furin-like endopeptidase11,12,13. Those different peptides (a 5-mer and 11-mer) have not been isolated endogenously to date. However, the rat 11-mer sequence (named brain excitatory peptide, BEP) significantly induced synaptic excitability and possessed some dopaminergic activities in vitro (thus named dopamine neuron stimulating peptides, DNSP)13. Furthermore, the human 11-mer sequence (named DNSP-11) exhibits neurotrophic-like properties13.Thus, the role of the full proDomain of GDNF, which is a product of proteolytic cleavage of proGDNF, is not clearly understood yet.

Research relevance and current trends

  • Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
  • Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
  • Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.

Common research applications

  • Assay development and optimization: used as a reference material or tool reagent in RUO workflows.
  • Reagent validation: supports conceptual controls such as competition/neutralization, when relevant.

Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.

Notes for experimental interpretation

  • Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
  • Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
  • Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Watanabe. T.

et al. (1995) Br. J. Pharmacol.114, 949.

Airaksinen, M.S.

et al. (2002) Nat. Rev. Neurosci.3, 383.

Henderson, C.E.

et al. (1994) Science266, 1062.

Houenou, L.J.

et al. (1996) Cell. Tissue Res.286, 219.

Kobayashi, M.

et al. (2000) Neuroreport 11, 2541.

Tomac, A.

et al. (1995) Nature373, 335.

Zhou, F.Q.

et al. (2003) Cell 113, 814.

Lin, L.F.

et al. (1993) Science260, 1130.

Matheson, C.R.

et al. (1997) Neuroreport8, 1739.

Brundin, P.

(2002) Brain125, 2149.

Grondin, R.

et al. (1998) J. Neurol.245, P35.

Bradley, L.H.

et al. (2010) PLoS ONE5, e9752.

Immonen, T.

et al. (2008) Exp. Neurol.210, 793.

Kelps, K.A.

et al. (2011) Neuropeptides 45, 213.

Bradley, L.H.

et al. (2010) PLoS ONE5, e9752.

Immonen, T.

et al. (2008) Exp. Neurol.210, 793.

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