Analytical Data
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Gene name
Calnexin
- Application
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Alternative Names
rHuCalnexin, His; Calnexin; IP90; Major Histocompatibility Complex Class I Antigen-Binding Protein p88; CANX
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27824
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Expression Region
H21-P481
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AA Sequence
HDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPHHHHHH
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Protein Length
Lumenal Domain
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Molecular Weight
70.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Calnexin is a membrane-associated chaperone protein predominantly found in the endoplasmic reticulum (ER), playing a critical role in the proper folding and quality control of newly synthesized glycoproteins. Its unique structure, featuring a lectin domain that recognizes specific carbohydrate moieties on nascent glycoproteins, enables it to assist in their proper folding and prevent aggregation. Research has shown that Calnexin interacts with a variety of client proteins, influencing their stability, functionality, and transport to the Golgi apparatus. Given its essential role in the protein maturation process, Calnexin has garnered significant interest in studies related to various diseases, including neurodegenerative disorders, where protein misfolding is a key feature. Additionally, its involvement in the immune response and cellular stress response pathways underscores its importance in maintaining cellular homeostasis. Research on recombinant Calnexin has advanced our understanding of its mechanistic functions and potential therapeutic roles, paving the way for novel strategies to address diseases associated with protein misfolding and ER stress. By investigating the protein's structure-function relationships and interaction networks through recombinant expression systems, researchers aim to develop targeted therapeutics that can modulate Calnexin's activity, thereby enhancing protein folding processes in pathological conditions.
