Analytical Data
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Gene name
CHIP
- Application
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Alternative Names
CHIP；CHIP；E3 ubiquitin-Protein ligase CHIP
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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
Q9UNE7
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Expression Region
1-303aa
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AA Sequence
MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYG RAITRNPLVA VYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHF FLGQCQLEMESYDEAIANLQRA YSLAKEQRLNFGDDIPSALRIAKKKR WNSIEERRIHQESELHSYLSRLIAAERERELEEC QRNHEGDEDDSHVR AQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELM RE PCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDA FISENGWV EDY
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Molecular Weight
37 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
The study of CHIPs (C-terminal Hsp70-interacting proteins) has garnered significant attention in recent years due to their pivotal role in various cellular processes, particularly in the regulation of protein quality control and degradation. CHIPs function as E3 ubiquitin ligases that facilitate the ubiquitination and subsequent proteasomal degradation of misfolded or damaged proteins, thereby maintaining cellular homeostasis. Dysregulation of CHIP activity has been implicated in a range of diseases, including neurodegenerative disorders, cancers, and cardiovascular diseases. Research into CHIP recombinant proteins allows for the elucidation of their structure-function relationships and the mechanisms by which they interact with heat shock proteins (Hsp70), other chaperones, and substrates. By producing these proteins in a recombinant system, scientists can investigate their functional properties, binding affinities, and the effects of specific mutations. Understanding the nuances of CHIP's interactions and regulatory mechanisms not only sheds light on fundamental biological processes but also opens avenues for therapeutic interventions aimed at enhancing protein quality control systems. Such insights are crucial for developing strategies to mitigate the pathological consequences of protein misfolding and aggregation, thus underscoring the importance of continued research into CHIP and its recombinant forms.
