Analytical Data
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Gene name
PHB
- Application
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Alternative Names
PHB1;PHB;Prohibitin 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
P35232
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Expression Region
1-272aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
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Molecular Weight
32 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
PHB (Prohibitin) is a highly conserved protein that plays a crucial role in various cellular processes, including cell proliferation, differentiation, and apoptosis. Recent research has highlighted its involvement in mitochondrial function and cellular signaling pathways, making it an attractive target for therapeutic interventions in diseases such as cancer and neurodegenerative disorders. PHB exists in multiple forms, including cytosolic and mitochondrial localizations, and has been shown to interact with various molecular partners, influencing cell fate decisions. The study of recombinant PHB proteins offers insights into their structure-function relationships and regulatory mechanisms. With advances in recombinant DNA technology, scientists can produce PHB in a controlled environment, facilitating detailed investigations into its biological roles and potential applications in drug development. Understanding the dynamics of PHB through recombinant approaches may pave the way for novel strategies in treating diseases associated with its dysregulation, making it a subject of significant interest in both basic and applied biomedical research.











