RTN4 Protein, Human, Recombinant (GST Tag)

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RTN4 Protein, Human, Recombinant (GST Tag): Product Information

Purity
> 70 % as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Activity
Measured by its ability to bind recombinant human RTN4R in a functional ELISA.
Protein Construction
A DNA sequence encoding the human RTN4 (NP_065393.1) N-terminal fragment (Met 1-Val 185) was fused with the GST tag at the N-terminus.
Accession#
Expressed Host
E. coli
Species
Human
Predicted N Terminal
Met
Molecule Mass
The recombinant human RTN4/GST chimera consists of 417 amino acids and has a predicted molecular mass of 46.2 kDa. It migrates as an approxiamtely 48 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile 20mM Tris, 150mM NaCl, 1mM DTT, 0.2mM GSH, pH 7.0
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

RTN4 Protein, Human, Recombinant (GST Tag): Images

RTN4 Protein, Human, Recombinant (GST Tag): Alternative Names

ASY Protein, Human; DGU Protein, Human; DKFZp781L1143 Protein, Human; HIGM4 Protein, Human; Nbla00271 Protein, Human; Nbla10545 Protein, Human; NI220/250 Protein, Human; NOGO Protein, Human; NOGO-A Protein, Human; Nogo-B Protein, Human; Nogo-C Protein, Human; NOGOC Protein, Human; NSP Protein, Human; NSP-CL Protein, Human; RTN-X Protein, Human; RTN4-A Protein, Human; RTN4-B1 Protein, Human; RTN4-B2 Protein, Human; RTN4-C Protein, Human; UDG Protein, Human; UNG1 Protein, Human; UNG15 Protein, Human; UNG2 Protein, Human

RTN4 Background Information

Reticulon-4, also known as Foocen, Neurite outgrowth inhibitor, Nogo protein, Neuroendocrine-specific protein, Neuroendocrine-specific protein C homolog, RTN-x, Reticulon-5 and RTN4, is a multi-pass membrane protein which contains onereticulon domain. Isoform1of RTN4 is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform2 of RTN4 is widely expressed except for the liver. Isoform3of RTN4 is expressed in brain, skeletal muscle and adipocytes. Isoform4of RTN4 is testis-specific. Reticulon-4 / RTN4 is a developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Reticulon-4 / RTN4 regulates neurite fasciculation, branching and extension in the developing nervous system. Reticulon-4 / RTN4 is involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. It regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex. Isoform 2 of RTN4 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 of RTN4 inhibit BACE1 activity and amyloid precursor protein processing.
Full Name
reticulon 4
References
  • Yang J., et al., 2000, Cytogenet. Cell Genet. 88:101-102.
  • Prinjha R., et al., 2000, Nature 403: 383-384.
  • Tagami S., et al., 2000, Oncogene 19: 5736-5746.
  • Murayama K.S., et al., 2006, Eur. J. Neurosci. 24: 1237-1244.
  • Daub H., et al., 2008, Mol. Cell 31:438-448.
  • Choudhary C., et al., 2009, Science 325: 834-840.
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