Analytical Data
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Gene name
STIP1
- Application
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Alternative Names
STIP1；Stress-induced-phosphoProtein 1
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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
P31948
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Expression Region
1-543aa
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AA Sequence
MEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAK KGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLK HEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDP TYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPP PPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDK AKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIA KAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQE RLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNR AACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDV YQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMS DPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR
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Molecular Weight
63 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
STIP1 (Stress-Independent Partner 1), also known as HSP70-HSP90 organizing protein, plays a crucial role in the regulation of molecular chaperones, particularly HSP70 and HSP90, which are vital for protein folding, stabilization, and degradation. The study of STIP1 recombinant proteins has gained significant attention due to their involvement in various cellular processes and diseases, including cancer, neurodegenerative disorders, and stress responses. Researchers have been particularly interested in understanding STIP1's mechanism of action and its interactions with different client proteins within the cellular environment, as alterations in STIP1 function can influence disease progression and therapeutic outcomes. By generating recombinant STIP1 proteins, scientists aim to elucidate its structural properties, interactome, and the downstream effects of STIP1-mediated chaperone regulation. This research could pave the way for novel therapeutic strategies targeting STIP1 and related pathways, making it a potential biomarker or therapeutic target in various pathological conditions. The ongoing advancements in recombinant protein technology and structural biology techniques are expected to enhance our understanding of STIP1's biological significance, ultimately contributing to the development of innovative approaches to treat diseases associated with protein misfolding and stress responses.
