Recombinant Human Calnexin (CANX)
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Description
Introduction to Recombinant Human Calnexin (CANX)
Recombinant Human Calnexin (CANX) is a laboratory-engineered form of the endoplasmic reticulum (ER) chaperone protein, designed for studying protein folding, quality control mechanisms, and ER-associated degradation pathways . Produced in heterologous expression systems like Escherichia coli or HEK293 cells, it retains functional properties of native calnexin, including calcium-binding and glycoprotein interaction capabilities .
Production and Purification
Recombinant CANX is synthesized using advanced expression systems:
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Expression Hosts:
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Purification: Anti-DDK affinity chromatography followed by ion-exchange or size-exclusion chromatography .
Protein Folding and Quality Control
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Retains misfolded glycoproteins in the ER via interaction with monoglucosylated oligosaccharides .
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Collaborates with ERp57 to catalyze disulfide bond formation in MHC class I molecules .
Disease Mechanisms
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Charcot-Marie-Tooth Disease: Mutant PMP22 proteins sequestered by calnexin fail to traffic to Schwann cells, impairing myelination .
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Multiple Sclerosis (MS): Calnexin regulates T cell transmigration across the blood-brain barrier, as shown in experimental autoimmune encephalomyelitis (EAE) models .
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SARS-CoV-2: Calnexin/calreticulin chaperones facilitate Spike protein maturation; knockout cells show reduced viral entry .
Aging and Cytoprotection
Calnexin levels decline with age, correlating with increased susceptibility to ER stress-related pathologies .
Role in Viral Pathogenesis
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SARS-CoV-2: CANX/CALR knockout 293T cells exhibit reduced Spike protein incorporation into pseudoviruses, highlighting its role in viral assembly .
Autoimmunity
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Mice with T cell-specific Canx deletion develop EAE normally, suggesting calnexin’s role is endothelial-specific .
Future Directions
Emerging studies focus on:
Product Specs
Form
Lyophilized powder
Please note: We prioritize shipping the format currently in stock. However, if you have specific format requirements, please indicate them when placing your order, and we will fulfill your request accordingly.
Please note: We prioritize shipping the format currently in stock. However, if you have specific format requirements, please indicate them when placing your order, and we will fulfill your request accordingly.
Lead Time
Delivery time may vary depending on the purchasing method or location. Please consult your local distributors for specific delivery timeframes.
Note: All our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please inform us in advance as additional fees will apply.
Note: All our proteins are shipped with standard blue ice packs by default. If you require dry ice shipping, please inform us in advance as additional fees will apply.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Reconstitution
We recommend briefly centrifuging this vial prior to opening to ensure the contents settle to the bottom. Reconstitute the protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. We recommend adding 5-50% glycerol (final concentration) and aliquoting for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%, which can be used as a reference.
Shelf Life
Shelf life depends on various factors including storage conditions, buffer ingredients, temperature, and the intrinsic stability of the protein.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is essential for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during the manufacturing process.
The tag type is determined during production. If you have a specific tag type in mind, please inform us, and we will prioritize developing the specified tag.
Synonyms
CANX; Calnexin; IP90; Major histocompatibility complex class I antigen-binding protein p88; p90
Buffer Before Lyophilization
Tris/PBS-based buffer, 6%
Trehalose.
Datasheet
Please contact us to get it.
Expression Region
21-592
Protein Length
full length protein
Species
Homo sapiens (Human)
Target Names
Target Protein Sequence
HDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
Uniprot No.
Target Background
Function
Calnexin is a calcium-binding protein that interacts with newly synthesized glycoproteins within the endoplasmic reticulum (ER). Its function may involve assisting protein assembly and/or retaining unassembled protein subunits within the ER. It plays a crucial role in the ER quality control apparatus by retaining misfolded proteins. Calnexin is associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, potentially functioning as a signaling complex that regulates thymocyte maturation. Additionally, it may contribute to receptor-mediated endocytosis at the synapse.
Gene References Into Functions
- In summary, ER retention of pathogenic VLDLR mutants involves binding to calnexin, increased endoplasmic reticulum stress, and delayed degradation that is dependent on SEL1L. PMID: 29371607
- Elevated calnexin levels in tumor proteins may hold prognostic significance in colorectal cancer, suggesting calnexin as a potential target for future therapeutic strategies. PMID: 27369741
- FUNDC1 integrates mitochondrial fission and mitophagy at the interface of the ER-mitochondrial contact site by working in conjunction with DRP1 and calnexin under hypoxic conditions in mammalian cells. PMID: 27145933
- Further analyses using a CNX mutant suggest that ERp29 and ERp57 recognize the same domain of CNX, although their mode of interaction with CNX might differ somewhat. PMID: 28456374
- Inhibition of the interaction between HIV-1 Nef and Calnexin could reverse HIV-induced lipid accumulation and prevent atherosclerosis. PMID: 27470515
- Endogenous NOX4 forms macromolecular complexes with calnexin, which are essential for the proper maturation, processing, and function of NOX4 in the ER. PMID: 26861875
- To investigate the principles underlying dynamics and regulation of palmitoylation, the ER chaperone calnexin, which requires dual palmitoylation for its function, was studied. PMID: 26900856
- These observations highlight a previously unrecognized contribution of calnexin to the retention of NMT1 at the ER membrane. PMID: 26603938
- Charcot-Marie-Tooth disease-related PMP22 is trapped in the ER by calnexin-dependent retention and Rer1-mediated early Golgi retrieval systems, and is partially degraded by the Hrd1-mediated ER-associated degradation system. PMID: 25385046
- Data indicate that protein tyrosine phosphatase 1B (PTP1B) association with calnexin is dependent on ubiquitin conjugating enzyme 9 (UBC9). PMID: 25586181
- H-ERG trafficking was impaired by H2O2 after 48 h treatment, accompanied by reciprocal changes in expression between miR-17-5p seed miRNAs and several chaperones (Hsp70, Hsc70, CANX, and Golga20). PMID: 24386440
- Nef regulates the activity of calnexin to stimulate its interaction with gp160 at the expense of ABCA1. PMID: 25170080
- The impact of CANX genetic variants on heart rate was discovered. PMID: 24680774
- Soluble calnexin may perform functions similar to calreticulin. PMID: 24056258
- Calnexin modulates cellular responses to epidermal growth factor receptor in a manner that depends on the health status of the ER. PMID: 23932718
- These findings demonstrated that calnexin strictly monitors the maturation of the S protein by direct binding, resulting in the conferral of infectivity on severe acute respiratory syndrome coronavirus. PMID: 22915798
- The data suggest that patients with low or defective TAP1 or calnexin in primary breast cancers may be at higher risks of developing brain metastasis due to defects in T cell-based immunosurveillance. PMID: 22065046
- Cysteine residues within calnexin are crucial for its structure and function. PMID: 21842374
- The findings revealed that calnexin is a stable component of the ribosome-translocon complex in a manner that is highly dependent on calnexin's palmitoylation status. PMID: 22314232
- HLA-I, TAP1, CNX, LMP7, Erp57, Tapasin and ERAP1 were down-regulated in 68%, 44%, 48%, 40%, 52%, 32% and 20% of esophageal squamous cell carcinoma lesions, respectively. PMID: 21362330
- Nixin/ZNRF4 appears to be central for the regulation of calnexin turnover. PMID: 21205830
- Results indicate that the P-domain functions as a unique protein-protein interaction domain and implicate a peptidyl prolyl isomerase as a new element in the calnexin cycle. PMID: 20801878
- Calnexin can bind PrP both in vitro and in vivo; calnexin prevents caspase-3-mediated cytotoxicity induced by PrP. PMID: 20506117
- Transmembrane segments prevent surface expression of sodium channel Nav1.8 and promote calnexin-dependent channel degradation. PMID: 20720009
- The human delta opioid receptor (hdeltaOR) exists in a ternary complex with SERCA2b and the ER molecular chaperone calnexin. PMID: 20528919
- Env interacts with intracellular CNX and extracellular PDI via discrete, largely nonoverlapping, regions. PMID: 20202930
- Results show that the phosphorylation of calnexin is linked to the efficiency of secretion of the cargo glycoprotein, in this case, alpha1-antitrypsin. PMID: 19815548
- Data show that demonstrate that Cnx preferentially associates with misfolded mutant opsins associated with retinitis pigmentosa. PMID: 19801547
- EDEM appeared to function in the ERAD (endoplasmic reticulum-associated degradation) pathway by accepting substrates from calnexin. PMID: 12610305
- EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. PMID: 12610306
- Data show that calnexin associates with newly synthesized proteolipid protein (PLP) molecules, binding stably to misfolded PLP. PMID: 12805210
- Calnexin down-regulation may contribute to the metastatic phenotype of melanoma cells in vivo. PMID: 14732231
- Calnexin provides long-term protection of wild-type Shaker protein from ER-associated degradation. PMID: 15161937
- The contribution of both the b and b' domains to the binding with CNX and calreticulin was revealed. PMID: 15236594
- Results support emerging models for a glycan-independent chaperone role for calnexin and for the mechanism of retention of misfolded membrane proteins in the ER. PMID: 15537650
- Calnexin decreases with aging and might contribute to cytoprotection in a variety of human age-related diseases. PMID: 15557823
- Data show that the major degradation pathway of the cystic fibrosis transmembrane conductance regulator with F508 deletion from the ER is independent of calnexin. PMID: 15923638
- Calnexin associates with the neonatal Fc receptor for IgG (FcRn) heavy chain before it associates noncovalently with beta 2-microglobulin. PMID: 16002696
- Polypeptide substrate recognition by CANX requires specific conformations of the CANX protein. PMID: 16061483
- We characterized a molecular mechanism by which calnexin regulates ER-stress-mediated apoptosis in a manner independent of its chaperone functions but dependent on its binding to Bap31. PMID: 16858427
- Here, we have observed that NCT N-linked oligosaccharides mediated specific interactions with the secretory pathway lectins calnexin and ERGIC-53. PMID: 16938437
- A proportion of the human and the rat WT gonadotropin-releasing hormone receptor appears to be retained in the ER by calnexin, an effect that decreases GnRHR signaling capacity. PMID: 17170088
- These results suggest that MCF-7 resistance to ER stress-induced apoptosis is partially mediated by the expression level of calnexin, which in turn controls its sub-cellular localization, and its association with Bap31. PMID: 17203246
- D1 and D2 dopamine receptor expression is regulated by direct interaction with the chaperone protein calnexin. PMID: 17395585
- ER chaperones stabilize nicotinic receptor subunits and regulate receptor assembly. PMID: 17728248
- Interaction with calnexin led to accumulation of GAT1 in concentric bodies corresponding to previously described multilamellar ER-derived structures. PMID: 18367207
- The phosphorylation state of the calnexin cytosolic domain and its interaction with PACS-2 sort the chaperone between domains of the ER and the plasma membrane. PMID: 18417615
- A dependence on calnexin for proper assembly of CFTR's membrane spanning domains was identified. PMID: 18716059
- ERp57 must be physically associated with the calnexin cycle to catalyze isomerization reactions with most of its substrates. PMID: 19054761
- alphaIIb interacts with calnexin via its N15-linked glycan, and alphaIIbbeta3 biogenesis is partially controlled by engagement of alphaIIb in the calnexin cycle. PMID: 16304048
Database Links
Protein Families
Calreticulin family
Subcellular Location
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Melanosome.
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