Recombinant Human CNTN3 protein(Met1-Ser1002, 708Asp/Asn), hFc-tagged

• Cat.No.: CNTN3-76H
• Product Overview: Recombinant Human CNTN3 (NP_065923.1) (Met 1-Ser 1002, 708 Asp/Asn) was expressed in HEK293 with the fused Fc region of Human IgG1 at the C-terminus.

Specification

• Species: Human
• Source: HEK293
• Tag: Fc
• Protein Length: 1-1002 a.a.
• Form: Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human CNTN3/Fc chimera consists of 1221 amino acids and has a calculated molecular mass of 134.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhCNTN3/Fc chimera is approximately 160-170 kDa due to glycosylation.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: > 90 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: CNTN3 contactin 3 (plasmacytoma associated) [ Homo sapiens ]
• Official Symbol: CNTN3
• Synonyms: CNTN3; contactin 3 (plasmacytoma associated); PANG; contactin-3; BIG 1; plasmacytoma-associated neuronal glycoprotein; brain-derived immunoglobulin superfamily protein 1; PCS; BIG-1; KIAA1496
• Gene ID: 5067
• mRNA Refseq: NM_020872
• Protein Refseq: NP_065923
• MIM: 601325
• UniProt ID: Q9P232

Case Study

Case 1: Boal F, et al. PLoS One. 2010

Transporting molecules within cells involves proteins that shape membranes. Arf proteins, activated by GEFs, are vital for this process. BIG1 and BIG2, two related Arf-GEFs, have puzzled scientists. Through experiments, we found that removing BIG2 affects endosomes, causing them to tubulate, while losing BIG1 leads to Golgi mini-stacks, still functional for cargo export. Each has distinct roles in cell organization.

Fig1. HeLa cells were transfected without siRNA (Mock), with non-targeting siRNA duplexes (Control), or with siRNA targeting indicated GEF.

Fig2. BIG1 suppression using individual siRNA duplexes was monitored by immunoblotting.

Case 2: Ishizaki R, et al. Mol Biol Cell. 2008

BIG2 and BIG1 are similar GEFs that help ADP-ribosylation factors manage membrane traffic by activating ARFs and recruiting protein complexes like COPI and AP-1. While BIG1 mainly associates with the trans-Golgi network (TGN) and BIG2 with recycling endosomes, it's unclear if they share roles. Our study shows that knocking down both BIG1 and BIG2 causes certain proteins in the TGN and recycling endosomes to mislocalize, disrupting furin's transport from late endosomes to the TGN. Similar disruptions occur when AP-1 is depleted.

Fig1. BIG2+BIG1 and AP-1 knockdown cells show a similar phenotype in terms of retrograde transport of CD4-furin.

Fig2. Presence of TfnR and CD4-furin on the same tubular structures induced by depletion of BIG2 and BIG1.

Application

Recombinant CNTN3 protein offers exciting possibilities in both medical and scientific fields. In neuroscience, CNTN3 is key for neuron connections, affecting learning and memory. By studying this protein, we could develop new treatments for cognitive disorders or brain injuries, offering hope to those with conditions like Alzheimer's or traumatic brain injuries. It's like providing researchers with a new framework to improve or restore brain function. In cancer therapy, CNTN3 might hold answers to controlling tumor behavior. Contactin proteins like CNTN3 affect how cells stick together and communicate, influencing tumor growth and spread. By understanding CNTN3, we might develop targeted therapies that hinder cancer's progress. In essence, recombinant CNTN3 isn't just a subject of study—it's a potential game-changer for therapies in both brain health and cancer management, holding the promise of better and more personalized treatments.

Fig1. Models of retrograde transport pathways of furin in the control cells (A) and in cells knocked down of both BIG1 and BIG2 (B). (Ray Ishizaki, 2008)