Product Name:
Calnexin-NT
Product Number:
ab-nn136-2
Target Full Name: Calnexin
Target Alias: CALX_HUMAN; CANX; CNX; FLJ26570; Histocompatibility complex class I antigen binding protein p88; IP90; Major histocompatibility complex class I antigen-binding protein p88
Product Type Specific: Calcium binding protein pan-specific antibody
Antibody Code: NN136-2
Antibody Target Type: Pan-specific
Protein UniProt: P27824
Protein SigNET: Calnexin
Antibody Type: Polyclonal
Antibody Host Species: Rabbit
Antibody Immunogen Source: A 19 residue Synthetic peptide patterned after dog Calnexin.(NCBI Ref Seq XP_533285)
Production Method: Rabbit antiserum
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Storage Buffer: Rabbit antiserum
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting, Immunoprecipitation, ICC, Immunofluorescence
Antibody Dilution Recommended: 1:5000-10000 (ECL) (WB), 1:100 (IP)
Antibody Potency: Very high potency. Detects a ~90 kDa protein in cell and tissue lysates by Western blotting.
Antibody Species Reactivity: This antibody detects the target protein in the following species due to conservation of amino acid sequence: Human | Monkey | Cow | Dog | Pig | Sheep | Rabbit | Guinea Pig | Rat | Mouse | Hamster | Chicken | Frog.
Antibody Positive Control: A 1:5000 dilution of SPC-127 was sufficient for detection of Calnexin in 20μg of HeLa cell lysate by ECL immunoblot analysis.
Antibody Specificity: Very high
Related Product 1: Calnexin expression antibody (Cat. No.: AB-NN136-4)
Related Product 2: Calnexin expression antibody (Cat. No.: AB-NN136-5)
Scientific Background: Calnexin, an abundant ~90 kDa integral protein of the endoplasmic reticulum (ER), is also referred to as IP90, p88 and p90 (1). It consists of a large 50 kDa N-terminal calcium-binding luminal domain, a single transmembrane helix and a short acidic cytoplasmic tail (2, 3). Unlike its ER counterparts which have a KDEL sequence on their C-terminus to ensure ER retention (4), calnexin has positively charged cytosolic residues that do the same thing (3). Most ER proteins act as molecular chaperones and participate in the proper folding of polypeptides and their assembly into mulitsubunit proteins. It functions as a quality control sensor for newly synthesized glycoproteins. It resides in the ER membrane, binding to monoglucosylated N-linked oligosaccharides to facilitate proper folding and prevent misfolded proteins from exiting the ER.Calnexin together with calreticulin, plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglycosylated glycans (5, 6). Calnexin has also been shown to associate with the major histocompatability complex class I heavy chains, partial complexes of the T cell receptor and B cell membrane immunoglobulin (7). It features a large N-terminal ER-lumenal domain, a single transmembrane segment, and a C-terminal cytosolic tail. It is described as having a globular domain and a proline-rich P-domain, similar to the soluble chaperone calreticulin. Mutations or imbalances in calnexin are associated with neurological problems, as it is involved in the folding of membrane-associated and secreted proteins. This description may include information annotated by UniProt and/or Google AI.