CDNF (cerebral dopamine neurotrophic factor or conserved dopamine neurotrophic factor) is also known as ARMETL1 (arginine­rich, mutated in early stage tumors­-like 1) in mouse.  Mature CDNF protein consists of 161 amino acid residues (its precursor has 187 amino acids), and shares 62% amino acid (aa) identity with human MANF (mesencephalic­ astrocyte­derived neurotrophic factor), termed ARMET in mouse.  CDNF was first identified by bioinformatics and then biochemically characterized.  Vertebrates appear to have CDNF and MANF genes, whereas invertebrates have a single homologous gene more closely related to MANF than to CDNF.  Mature human CDNF shares 80%, 84%, 90% and 92% aa identity with mouse, rat, equine and bovine CDNF, respectively.  Human CDNF contains one potential N-linked glycosylation site, and both unglycosylated and glycosylated form of human CDNF is secreted from transiently overexpressing cells.  Both CDNF and MANF have a high proportion of charged residues, a pattern of eight cysteines shown to form intramoleculular disulfides, and a C-­terminal endoplasmic reticulum retention signal.  The CDNF gene is widely expressed in neuronal and non-neuronal tissues.  In the brain, highest levels in the optic nerve and corpus callosum. Although CDNF mRNA and protein are expressed in pre­ and post­natal mouse brain, they are most abundant in adult heart, skeletal muscle and testis.  Similar to MANF and GDNF, CDNF promotes survival of dopaminergic neurons in vitro. In a rat Parkinson’s disease model, CDNF also promotes rescue and restoration of dopaminergic neurons in vivo.

CDNF (cerebral dopamine neurotrophic factor or conserved dopamine neurotrophic factor) is also known as ARMETL1 (arginine­rich, mutated in early stage tumors­-like 1) in mouse.  Mature CDNF protein consists of 161 amino acid residues (its precursor has 187 amino acids), and shares 62% amino acid (aa) identity with human MANF (mesencephalic­ astrocyte­derived neurotrophic factor), termed ARMET in mouse.  CDNF was first identified by bioinformatics and then biochemically characterized.  Vertebrates appear to have CDNF and MANF genes, whereas invertebrates have a single homologous gene more closely related to MANF than to CDNF.  Mature human CDNF shares 80%, 84%, 90% and 92% aa identity with mouse, rat, equine and bovine CDNF, respectively.  Human CDNF contains one potential N-linked glycosylation site, and both unglycosylated and glycosylated form of human CDNF is secreted from transiently overexpressing cells.  Both CDNF and MANF have a high proportion of charged residues, a pattern of eight cysteines shown to form intramoleculular disulfides, and a C-­terminal endoplasmic reticulum retention signal.  The CDNF gene is widely expressed in neuronal and non-neuronal tissues.  In the brain, highest levels in the optic nerve and corpus callosum. Although CDNF mRNA and protein are expressed in pre­ and post­natal mouse brain, they are most abundant in adult heart, skeletal muscle and testis.  Similar to MANF and GDNF, CDNF promotes survival of dopaminergic neurons in vitro. In a rat Parkinson’s disease model, CDNF also promotes rescue and restoration of dopaminergic neurons in vivo.

 

Product Details

 

Gene Symbol: CDNF; ARMETL1

 

NCBI Gene ID: 441549

 

Uniprot Entry: Q49AH0

 

Construct Details: The recombinant human CDNF is expressed as a 174 amino acid protein consisting of Gln25 - Leu187 region of CDNF (UniProt entry Q49AH0) and a C-terminal poly-Histidine tag.

 

Source: Human cells stably expressing CDNF and growing in chemical-defined media with no animal components or antibiotics

 

Deduced Amino Acid Sequence: 

QGQEAGGRPGADCEVCKEFLNRFYKSLIDRGVNFSLDTIEKELISFCLDTKGKENRLCYYLGATKDAATKILSEVTRPMSVH

MPAMKICEKLKKLDSQICELKYEKTLDLASVDLRKMRVAELKQILHSWGEECRACAEKTDYVNLIQELAPKYAATHPKTELS

TGHHHHHHHH

M.W.: Calculated molecular mass 19.9 kDa; estimated by SDS-PAGE under reducing condition  ~22 kDa with a higher molecular mass band (~25 kDa) resembling a glycosylated state.

 

Calculated PI: 7.75

 

Calculated Extinction Coefficient: 14940 (M^-1 cm^-1, at 280nm)

 

Purity: >95% judged by SDS-PAGE under reducing condition (see the gel image above, sample is labeled as "S" and "M" stands for markers)

 

Formulation:Supplied at 0.5 mg/ml in sterile PBS pH7.4 (carrier free). The purified recombinant protein was labeled with Biotin (3-5 Biotin per molecule) using the standard procedure.

 

Endotoxin Level: <0.1 EU per 1 μg of purified recombinant protein determined by the LAL method

 

Biological Activity: CDNF is reported to enhance neurite outgrowth of E18 rat embryonic cortical neurons and increases neurite outgrowth when immobilized at 6 ­ - 24 μg/mL on a nitrocellulose­ coated microplate

 

 

 

FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE IN HUMAN.

Restriction: This product is not transferable or re-sellable.  Customer obtain no right to transfer, assign, or sublicense its use rights, or to transfer, resell, package, or otherwise distribute the product, or to use the product for the benefit of any third party or for any commercial purpose.  Customer may only use the product in compliance with applicable local, state and federal laws, regulations and rules.  Customer may not directly or indirectly use the product or allow the transfer, transmission, export or re-export of all or any part of the product in violation of any export control law or regulation of the united states or any other relevant jurisdiction.  Your use of this product constitutes acceptance of the terms of this limited use agreement.  Please refer to our “terms & conditions” for details.  If you are not willing to accept the limitation of this agreement, G&P Biosciences will accept return of the product for a full/partial refund.

 

Storage

 

The product is shipped at 4°C. Upon receipt, centrifuge the product briefly before opening the vial. It is recommended to store small aliquots at the temperature below –20°C for long-term storage and the product is stable for 3 months. The undiluted protein can be stored at 4°C for no more than 2 weeks.

 

 

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.

 

 

 

FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE IN HUMAN.

 

References

 

1.  Develop Neurobiol 70: 360, 2010
2.  Nature 448:73, 2007
3.  Cell Struct. Funct 32:41, 2007
4.   J Cell Biol 179:1193, 2007

 

 

Documentation

 

Product datasheet (pdf) can be downloaded here: FCL0288B-PDS.pdf

 

 

 

Additional supporting documents, including COA and MSDS are available upon request.

 

 

 

FOR RESEARCH USE ONLY. NOT FOR DIAGNOSTIC OR THERAPEUTIC USE IN HUMAN.

Restriction: This product is not transferable or re-sellable.  Customer obtain no right to transfer, assign, or sublicense its use rights, or to transfer, resell, package, or otherwise distribute the product, or to use the product for the benefit of any third party or for any commercial purpose.  Customer may only use the product in compliance with applicable local, state and federal laws, regulations and rules.  Customer may not directly or indirectly use the product or allow the transfer, transmission, export or re-export of all or any part of the product in violation of any export control law or regulation of the united states or any other relevant jurisdiction.  Your use of this product constitutes acceptance of the terms of this limited use agreement.  Please refer to our “terms & conditions” for details.  If you are not willing to accept the limitation of this agreement, G&P Biosciences will accept return of the product for a full/partial refund.