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Validated All-in-One™ qPCR Primer for CANX(NM_001746.3) Search again
Product ID:
HQP058449
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CNX, IP90, P90
Gene Description:
calnexin
Target Gene Accession:
NM_001746.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation.
Gene References into function
- Data show that CD1d associates in the ER with both calnexin and calreticulin and with the thiol oxidoreductase ERp57 in a manner dependent on glucose trimming of its N-linked glycans.
- EDEM appeared to function in the ERAD (endoplasmic reticulum-associated degradation)pathway by accepting substrates from calnexin.
- EDEM was shown to extract misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle
- Data show that calnexin associates with newly synthesized proteolipid protein (PLP) molecules, binding stably to misfolded PLP.
- calnexin-downregulation may contribute to the metastatic phenotype of melanoma cells in vivo
- Calnexin provides long-term protection of wild-type Shaker protein from ER-associated degradation.
- the contribution of both the b and b' domains to the binding with CNX and calreticulin was revealed
- results support emerging models for a glycan-independent chaperone role for calnexin and for the mechanism of retention of misfolded membrane proteins in the endoplasmic reticulum
- Calnexin decreases with aging and might contribute to a cytoprotection in a variety of human age-related diseases.
- Data show that the major degradation pathway of the cystic fibrosis transmembrane conductance regulator with F508 deletion from the endoplasmic reticulum is independent of calnexin.
- Calnexin associates with the neonatal Fc receptor for IgG (FcRn) heavy chain before it associates noncovalently with beta 2-microglobulin.
- Polypeptide substrate recognition by CANX requires specific conformations of the CANX protein.
- alphaIIb interacts with calnexin via its N15-linked glycan, and alphaIIbbeta3 biogenesis is partially controlled by engagement of alphaIIb in the calnexin cycle.
- We characterized a molecular mechanism by which calnexin regulates ER-stress-mediated apoptosis in a manner independent of its chaperone functions but dependent of its binding to Bap31.
- Here, we have observed that NCT N-linked oligosaccharides mediated specific interactions with the secretory pathway lectins calnexin and ERGIC-53
- proportion of the human and the rat WT gonadotropin-releasing hormone receptor appears to be retained in the endoplasmic reticulum by calnexin, an effect that decreases GnRHR signaling capacity
- These results suggest that MCF-7 resistance to endoplasmic reticulum 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.
- D1 and D2 dopamine receptor expression is regulated by direct interaction with the chaperone protein calnexin
- Endoplasmic reticulum chaperones stabilize nicotinic receptor subunits and regulate receptor assembly.
- Interaction with calnexin led to accumulation of GAT1 in concentric bodies corresponding to previously described multilamellar ER-derived structures.
- 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
- A dependence on calnexin for proper assembly of CFTR's membrane spanning domains, was identified.
- ERp57 must be physically associated with the calnexin cycle to catalyze isomerization reactions with most of its substrates