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Anti-Calnexin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

MDL number:

biological source


Quality Level



antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen 90 kDa

species reactivity

canine, mouse, human, rat


antibody small pack of 25 μL


immunoprecipitation (IP): 1:2,000 using whole cell RIPA lysate of the human epitheloid carcinoma HeLa cell line
indirect immunofluorescence: 1:200 using 3% paraformaldehyde-fixed, 0.5% Triton X-100 treated, Madin Darby canine kidney MDCK cell line
microarray: suitable
western blot: 1:2,000 using whole cell RIPA lysate of the human hepatocytoma HepG2 cell line

UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... CANX(821)
mouse ... Canx(12330)
rat ... Canx(29144)

Related Categories

General description

Calnexin contains a long (461 amino acids) N-terminal Ca2+ -binding domain extending into the lumen of the endoplasmic reticulum (ER), a short (22 amino acids) transmembrane segment and an acidic cytosolic domain (96 amino acids).
Calnexin, is a calcium binding type I integral membrane protein present mainly in the endoplasmic reticulum. It plays a pivotal role in quality control processes during protein synthesis and folding. Anti-calnexin antibody (diluted 1: 300) can be used in dual immunofluorescence staining to visualize TG2 transport.


Rabbit anti-calnexin antibody reacts specifically with calnexin (90 kDa) of dog, mouse, rat and human.


Synthetic peptide corresponding to the c-terminus of human calnexin (amino acids 573-592) conjugated to KLH.


Anti-Calnexin antibody produced in rabbit has been used in:
  • western blot analysis
  • immunofluorescence
  • dual immunofluorescence staining

Biochem/physiol Actions

Calnexin binds newly synthesized glycoproteins and misfolded proteins and is believed to play a critical role in quality control processes during protein synthesis and folding. Calnexin acts as a lectin-like chaperone that binds oligosaccharide residues of newly synthesized N-linked glycoproteins. Calnexin has been shown to be associated with several cell surface proteins, including major histocompatibility complex (MHC) class I heavy chain, T-cell receptor (TCR), and B cell membrane immunoglobulin during translocation through the endoplasmic reticulum (ER). It also forms complexes with other resident ER proteins involved in Ca2+ -dependent retention of proteins.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.


Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

12 - Non Combustible Liquids



Certificate of Analysis

Certificate of Origin

Calnexin and calreticulin, molecular chaperones of the endoplasmic reticulum
Calreticulin, 49-62 (2003)
Quality control system of the endoplasmic reticulum and related diseases
Wu JC, et al.
Acta biochimica et biophysica Sinica, 38(4), 219-226 (2006)
I Wada et al.
The Journal of biological chemistry, 266(29), 19599-19610 (1991-10-15)
GTP phosphorylation of rough microsomes in vitro is limited to four integral membrane proteins. Two of these, a phosphoprotein (pp90) and a phosphoglycoprotein (pgp35) were purified as a complex with two nonphosphorylated membrane glycoproteins, gp25H and gp25L. The authenticity of
N Echeverry et al.
Cell death and differentiation, 20(6), 785-799 (2013-02-23)
The pro-apoptotic BCL-2 family member BOK is widely expressed and resembles the multi-BH domain proteins BAX and BAK based on its amino acid sequence. The genomic region encoding BOK was reported to be frequently deleted in human cancer and it
Markus Düchler et al.
Cells, 8(7) (2019-07-05)
Cancer-induced immunosuppression is antigen-specific rather than systemic and the mechanisms for the antigen specificity are incompletely understood. Here we explore the option that tumor-associated antigens (TAAs) may be transferred to antigen-presenting cells (APCs), together with immunosuppressive molecules, through cancer-derived small

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