Analytical Data
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Gene name
CH1
- Application
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Alternative Names
(AG4)(Allergen Cat-1)(Allergen Fel d I-A)(Allergen FdI)(Allergen Fel dI)(allergen Fel d 1-A)
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Species
Cat
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P30438
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Expression Region
23-92aa
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Molecular Weight
15.3 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
CH1, a key component of various proteins, has attracted considerable attention in the field of protein engineering and biotechnology due to its significant role in influencing protein structure and function. This protein domain is primarily recognized for its involvement in chaperone activities, wherein it assists in the correct folding and assembly of other proteins, thereby contributing to cellular homeostasis. Research has revealed that CH1 plays a crucial role in various biological processes, such as stress responses, signaling pathways, and even in the development of diseases. The ability to understand and manipulate CH1's function opens avenues for therapeutic applications, particularly in treating protein misfolding disorders, such as Alzheimer's and Parkinson's disease. Moreover, the recombinant production of CH1 offers opportunities for high-yield synthesis, facilitating detailed studies on its interactions and functionalities. Scientists are exploring various expression systems to optimize the yield and activity of CH1, employing techniques such as site-directed mutagenesis to enhance its chaperone properties. Given its extensive implications in both fundamental and applied research, CH1 is becoming a focal point in the ongoing quest to harness protein engineering techniques for innovative solutions in medicine and industry. Overall, the investigation of CH1 recombinant proteins not only expands our understanding of protein dynamics but also holds promise for significant advancements in therapeutic development and biotechnology applications.
