Analytical Data
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Gene name
TRAP1
- Application
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Alternative Names
Hsp75; Hspc5
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Species
Rat; Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5XHZ0
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Expression Region
S61-H706
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Protein Length
Full Length of Mature Protein
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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
TRAP1 (Tumor Necrosis Factor Receptor-Associated Protein 1) is a mitochondrial chaperone that plays a crucial role in cellular stress responses and mitochondrial function. It is part of the heat shock protein (HSP) family and is involved in folding proteins, preventing aggregation, and assisting in the proper assembly of mitochondrial complexes. Emerging research has linked TRAP1 to various diseases, particularly cancers, where its expression levels are often altered. Increased TRAP1 expression has been associated with tumor cell survival and resistance to apoptosis, making it a potential therapeutic target. Understanding the structure and function of recombinant TRAP1 proteins is essential for elucidating their role in cellular metabolism and stress responses. Studies involving the production and characterization of recombinant TRAP1 help to clarify its functional mechanisms and interactions with other molecular players within the mitochondria. By analyzing TRAP1's structure-function relationship, researchers aim to develop targeted therapies that can modulate its activity, potentially leading to novel treatments for cancer and other diseases linked to mitochondrial dysfunction. Furthermore, as mitochondrial health is crucial for overall cellular homeostasis, TRAP1's role in mitigating oxidative stress highlights its importance in aging and neurodegenerative diseases. The ongoing exploration of TRAP1 at the molecular level promises to uncover new insights into cellular biology and pave the way for innovative therapeutic strategies.
