Western Blot: Calnexin Antibody [NBP1-97485] - Analysis: Lane 1: HeLa (heat shocked), Lane 2: Vero (heat shocked), Lane 3: Rat-2 (heat shocked), Lane 4: L-929 (heat shocked).
Immunohistochemistry-Paraffin: Calnexin Antibody [NBP1-97485] - Analysis of human spleen tissue stained with Calnexin, pAb at 10ug/ml.
Product Details
Summary
Reactivity
Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, Dr, Gp, Ha, Pm, Rb, Sh, XpSpecies Glossary
Novus Biologicals Rabbit Calnexin Antibody - BSA Free (NBP1-97485) is a polyclonal antibody validated for use in IHC, WB, Flow, ICC/IF, Simple Western and IP. Anti-Calnexin Antibody: Cited in 12 publications. All Novus Biologicals antibodies are covered by our 100% guarantee.
Immunogen
Synthetic peptide corresponding to the sequence near the C-terminus of canine calnexin.
Marker
Endoplasmic Reticulum Membrane Marker
Isotype
IgG
Clonality
Polyclonal
Host
Rabbit
Gene
CANX
Purity
Protein A purified
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Major histocompatibility complex class I antigen-binding protein p88
P90
Background
Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Calnexin - an ER chaperone that folds the cell's glycoproteins Calnexin is an abundant 90kDa chaperone protein that resides in the membrane of the endoplasmic reticulum. Calnexin and the related calreticulin protein function together to ensure the proper folding of glycoproteins. By binding to partially folded... Read full blog post.
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