Recombinant Human Calnexin protein
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Recombinant Human Calnexin protein is a Human Fragment protein, in the 21 to 481 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
Calnexin, IP90, Major histocompatibility complex class I antigen-binding protein p88, p90, CANX
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Calnexin facilitates the proper folding of newly synthesized proteins by forming a complex with another chaperone protein called ERp57. This interaction helps in creating the correct disulfide bonds in glycoproteins which is essential for their stability and functionality. The complex often referred to as the calnexin cycle is critical in preventing the aggregation and misfolding of proteins within the ER. This process ensures that only correctly folded proteins proceed to the Golgi apparatus for further processing and transport.
Pathways
Calnexin plays an important role in the ER-associated degradation (ERAD) pathway and the unfolded protein response (UPR). In these pathways calnexin ensures that misfolded proteins are retained in the ER or targeted for degradation preventing cellular stress. Calnexin is associated with proteins such as calreticulin another chaperone protein with a similar function in the ER. Together they maintain proteostasis within cells and protect against the accumulation of improperly folded proteins.
Specifications
Form
Liquid
Additional notes
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
General info
Function
Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Sequence similarities
Belongs to the calreticulin family.
Post-translational modifications
Phosphorylated at Ser-564 by MAPK3/ERK1. Phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity).. Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins.. Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4.
Target data
Product promise
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