CANX Antibodies

Background

The CANX gene encodes an endoplasmic reticulum transmembrane chaperone protein called calnexin, which is mainly present in the endoplasmic reticulum of eukaryotic cells. It maintains cellular protein homeostasis by recognizing and binding to newly synthesized glycoproteins, assisting in their correct folding and assembly, and participating in quality control mechanisms to ensure that misfolded proteins are degraded. CANX plays a key role in a variety of cellular processes, especially in immune responses and cell adhesion, as many immune receptors and adhesion molecules rely on it to assist in maturation. This gene was identified in the early 1990s. Its functional research has revealed an important mechanism of the protein processing and quality control pathway in the endoplasmic reticulum, providing an important foundation for understanding protein folding abnormalities related to certain genetic diseases and cancers.

Structure Function Application Advantage Our Products

Structure of CANX

Calnexin, encoded by the CANX gene, is an endoplasmic reticulum transmembrane protein with a molecular weight of approximately 90 kDa. Its molecular weight is highly conserved among different species, which is closely related to its core function in the quality control of protein folding.

Species	Human	Mouse	Bovine	Rat
Molecular Weight (kDa)	90	90	89.5	90
Primary Structural Differences	Contains an N-terminal lectin domain, a single transmembrane region, and a C-terminal cytoplasmic tail	Highly homologous to humans and structurally highly similar	Highly conservative agglutinin structure domain	Consistent with the basic human function structure domain

Calcium-junction proteins contain 592 amino acids, and their primary structure forms a typical type I transmembrane protein. The core of this protein is its N-terminal lectin-like domain, which specifically recognizes and binds to the monosaccharide glucose residue on the newly synthesized glycoprotein. This is the structural basis for it to perform its molecular chaperone function. A single transmembrane helix anchors it to the endoplasmic reticulum membrane, while the cytoplasmic tail at the C-terminal contains endoplasmic reticulum retention signals.

Fig. 1:Simulated interaction between circCANX and P53 transcript. Fig. 1 Simulated interaction between circCANX and P53 transcript.¹

Key structural properties of CANX:

Unique topological structure
Conservative lectin domain
Repeat sequences rich in proline
Transmembrane anchoring and cytoplasmic tail

Functions of CANX

The Calnexin encoded by the CANX gene mainly functions as a molecular chaperone in the endoplasmic reticulum, assisting in the correct folding and assembly of glycoproteins. In addition, it is also deeply involved in key cellular quality control processes such as endoplasmic reticulum associated degradation (ERAD).

Function	Description
Promote glycoprotein folding	Its N-terminal lectin domain specifically recognizes Glc₁Man₉GlcNAc₂glycan on the newly synthesized glycoprotein, binds to it and provides a folding environment.
Quality control monitoring	Synergistic with the co-chaperone ERp57, which repeatedly binds to incompletely folded glycoproteins, ensures that only correctly folded proteins are transported out of the ER.
Target misfolded proteins	Identify and retain proteins that fail to fold, guide them to the endoplasmic reticulum associated degradation (ERAD) pathway for clearance, and prevent the accumulation of incorrect proteins.
Calcium ion homeostasis is maintained	As a calcium-binding protein within the endoplasmic reticulum lumen, its function depends on the concentration of calcium ions and indirectly participates in the regulation of intracellular calcium homeostasis.
Regulation of apoptosis	By affecting the endoplasmic reticulum stress response, it plays a regulatory role in the signaling pathway of cell apoptosis.

The functions of Calreticulin and the homologous protein calreticulin complement each other. However, as a transmembrane protein, calreticulin particularly focuses on the folding monitoring of membrane proteins and some secreted proteins. Its mechanism of action reflects the high specificity and accuracy of the endoplasmic reticulum quality control system.

Applications of CANX and CANX Antibody in Literature

1. Ye, Yuanzheng, et al. "PON2 ameliorates Ang II‐induced cardiomyocyte injury by targeting the CANX/NOX4 signaling pathway." Immunity, Inflammation and Disease 11.2 (2023): e765. https://doi.org/10.1002/iid3.765

This study explored the role of PON2 in angiotensin II-induced myocardial cell injury. It was found that PON2 regulates the NOX4 signaling pathway by targeting CANX, thereby inhibiting oxidative stress, inflammation and cell hypertrophy, and exerting a protective effect on cardiomyocytes.

2. Liu, Xuchen, et al. "Calnexin promotes glioblastoma progression by inducing protective mitophagy through the MEK/ERK/BNIP3 pathway." Theranostics 15.6 (2025): 2624. https://doi.org/10.7150/thno.105591

This study confirmed that the endoplasmic reticulum protein CANX promotes BNIP3-mediated mitochondrial autophagy in glioblastoma by activating the MEK/ERK signaling pathway, thereby enhancing the resistance of tumor cells to temozolomide. Targeting CANX can effectively reverse chemotherapy resistance, suggesting its potential as a new therapeutic target.

3. Chen, Ting‐Ting, et al. "ADAR1‐HNRNPL‐Mediated CircCANX Decline Promotes Autophagy in Chronic Obstructive Pulmonary Disease." Advanced Science 12.18 (2025): 2414211. https://doi.org/10.1002/advs.202414211

This study found that in chronic obstructive pulmonary disease, the expression of circular RNA circCANX is down-regulated. circCANX mediates P53 mRNA degradation by recruiting UPF1, thereby inhibiting autophagy and the formation of stress granules, and exacerbating airway inflammation. circCANX has the potential to be a therapeutic target and biomarker for COPD.

4. Shapiro, Ilja E., et al. "Deleterious knock-outs in the HLA class I antigen processing and presentation machinery induce distinct changes in the immunopeptidome." Molecular & Cellular Proteomics (2025): 100951. https://doi.org/10.1016/j.mcpro.2025.100951

In this study, a HAP1 cell line gene knockout model was constructed to systematically analyze the impact of the absence of key components of the antigen processing and presentation mechanism (APPM) on the immunopeptide group. Research has found that knocking out genes such as CANX can lead to significant alterations in HLA allele-specific presenting peptides, providing a new perspective for understanding antigen presentation deficits in disease conditions.

5. Vélez-López, Omar, et al. "Analysis of Sigma-1 Receptor Antagonist BD1047 Effect on Upregulating Proteins in HIV-1-Infected Macrophages Exposed to Cocaine Using Quantitative Proteomics." Biomedicines 12.9 (2024): 1934. https://doi.org/10.3390/biomedicines12091934

This study explored the role of Sig1R antagonist BD1047 in HIV-infected macrophages exposed to cocaine. The results indicated that pretreatment with BD1047 could up-regulate endoplasmic reticulum transportation-related proteins such as CANX, alleviate mitochondrial damage and CatB-mediated neurotoxicity, and exert protective effects.

Creative Biolabs: CANX Antibodies for Research

Creative Biolabs specializes in the production of high-quality CANX antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom CANX Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our CANX antibodies, custom preparations, or technical support, contact us at email.

Reference

Chen, Ting‐Ting, et al. "ADAR1‐HNRNPL‐Mediated CircCANX Decline Promotes Autophagy in Chronic Obstructive Pulmonary Disease." Advanced Science 12.18 (2025): 2414211. https://doi.org/10.1002/advs.202414211