Analytical Data
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Gene name
CNX
- Application
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Alternative Names
CNX；Gap junction alpha-4 Protein
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
21-481aa
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AA Sequence
HDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVY FADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGL VLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSK TPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAK RPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPV NPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKP EGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQ RPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFS AIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVV GQMIEAAEERPVDHHHHHH
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Molecular Weight
54 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
CNX, or Calnexin, is a molecular chaperone predominantly located in the endoplasmic reticulum (ER) that plays a critical role in the proper folding and quality control of glycoproteins. Research on CNX has gained significant momentum due to its essential function in ensuring that newly synthesized proteins achieve their correct conformation before they are transported to their final destinations. Misfolded proteins can lead to various diseases, including neurodegenerative disorders and certain cancers, making CNX a promising therapeutic target. The characterization of CNX recombinant proteins has provided insights into its mechanisms of action, particularly its interaction with glycoproteins and the folding process. Utilizing recombinant DNA technology, researchers can produce CNX in large quantities, facilitating detailed biochemical studies and structural analysis. This understanding is crucial for developing potential treatments that can enhance protein folding and mitigate the effects of folding-related diseases. Moreover, CNX's involvement in ER stress response pathways has implications for cellular health, further emphasizing the need to explore its role in various physiological and pathological conditions. As researchers continue to unravel the complexities of CNX, its potential as a biomarker for disease and a target for therapeutic intervention grows, paving the way for novel strategies in disease management.
