Analytical Data
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Gene name
CHORDC1
- Application
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Alternative Names
CHORD containing Protein 1; Chord domain containing Protein 1; CHORD domain-containing Protein 1; CHORD-containing Protein 1; CHORDC1; CHP-1; CHP1; CHRD1_HUMAN; Cysteine and histidine rich domain (CHORD) containing 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UHD1
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Expression Region
1-332aa
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AA Sequence
MALLCYNRGCGQRFDPETNSDDACTYHPGVPVFHDALKGWSCCKRRTTDFSDFLSIVGCTKGRHNSEKPPEPVKPEVKTTEKKELCELKPKFQEHIIQAPKPVEAIKRPSPDEPMTNLELKISASLKQALDKLKLSSGNEENKKEEDNDEIKIGTSCKNGGCSKTYQGLESLEEVCVYHSGVPIFHEGMKYWSCCRRKTSDFNTFLAQEGCTKGKHMWTKKDAGKKVVPCRHDWHQTGGEVTISVYAKNSLPELSRVEANSTLLNVHIVFEGEKEFDQNVKLWGVIDVKRSYVTMTATKIEITMRKAEPMQWASLELPAAKKQEKQKDATTD
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Molecular Weight
63.9 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
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Protein Description
CHORDC1, a member of the CHORD protein family, has garnered significant research interest due to its potential roles in cellular stress responses and disease mechanisms. Initially identified as a co-chaperone in the cytosol, CHORDC1 is known to interact with heat shock proteins, facilitating protein folding and stability under stress conditions. Its expression is often upregulated in various pathological states, including cancer and neurodegenerative disorders, suggesting it may play a crucial role in cellular survival and adaptation. Recent studies have shown that CHORDC1 functions in regulating oxidative stress and apoptosis, indicating its potential as a therapeutic target. Moreover, its involvement in maintaining mitochondrial integrity and function highlights its significance in energy metabolism and cellular homeostasis. As researchers continue to explore the multifaceted roles of CHORDC1, understanding its molecular mechanisms could lead to novel strategies for combating diseases associated with protein misfolding and oxidative damage. Thus, CHORDC1 is not only a key player in cellular stress response pathways but also holds promise for developing innovative treatments for a range of diseases.
