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Calnexin (lumenal domain) (human), (recombinant)

 
ADI-SPP-865-D 50 µg 263.00 USD
 
ADI-SPP-865-F 200 µg 599.00 USD
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Product Details

Alternative Name:CNX
 
MW:~74kDa
 
Source:Produced in E. coli.
 
UniProt ID:P27824
 
Formulation:Liquid. In TRIS containing sodium chloride, 5% glycerol, and 5mM calcium chloride.
 
Purity:≥85% (SDS-PAGE; Western blot) (full length protein)
 
Purity Detail:Purified by multi-step chromatography.
 
Applications:WB
 
Application Notes:Western blot control.
 
Shipping:Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:Calnexin (CNX), an abundant ~90 kDa molecular chaperone, is a resident type I transmembrane protein of the endoplasmic reticulum (ER) (ref.1,2). A majority of the calnexin protein resides in the luminal portion of the ER, and is the membrane-bound paralog of the soluble ER protein Calreticulin. In mammalian cells, calnexin and calreticulin (CRT) are lectins that play key roles in glycoprotein folding within the ER, specifically binding oligosaccharide intermediates that contain a single terminal GlcManGlcNAc residue. Calnexin associates with newly synthesized, incompletely folded monomeric glycoproteins as well as numerous oligomeric protein complexes, including
 
Regulatory Status:RUO - Research Use Only
 
Calnexin (lumenal domain) (human), (recombinant) Western blot
Western Blot analysis of Calnexin lumenal domain (Prod. No. ADI-SPP-865) probed with 1:1,000 dilution of Prod. No. ADI-SPA-865. Lane 1: MW marker, Lane 2: 50ng; Lane 3: 100ng
Calnexin (lumenal domain) (human), (recombinant) SDS-PAGE
SDS-PAGE analysis of Calnexin lumenal domain (Prod. No. ADI-SPP-865) stained with Coomassie. Lane 1: MWM, Lane 2: 0.5µg; Lane 3: 1µg; Lane 4: 2µg; Lane 5: 5µg
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Calnexin (lumenal domain) (human), (recombinant) Western blot Calnexin (lumenal domain) (human), (recombinant) SDS-PAGE

Product Literature References

Hsa-miR-30d, secreted by the human endometrium, is taken up by the pre-implantation embryo and might modify its transcriptome: F. Vilella, et al.; Development. 142, 3210 (2015), Application(s): Western Blot, Abstract; Full Text

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