Analytical Data
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Gene name
SPEB
- Application
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Alternative Names
speB; Streptopain; EC 3.4.22.10; Exotoxin type B; SPE B; Streptococcal cysteine proteinase; Streptococcus peptidase A; SPP
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Species
Others
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Source
E. coli
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Tag
N-6*His;N-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0C0J0
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Expression Region
Q146-P398
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AA Sequence
QPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP
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Protein Length
Full Length of Mature Protein
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Molecular Weight
40-45 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
SPEB (Spermine/Bis(5'-phospho)-dihydrocaffeic acid-binding protein) is a restructured protein that has garnered increasing interest in the field of molecular biology and biochemistry due to its unique binding properties and potential applications in therapeutic solutions. Historically, proteins involved in the regulation of cellular functions like growth, differentiation, and apoptosis have been crucial in understanding various biological processes. SPEB is particularly significant because of its role in binding polyamines, which are vital for cellular function and stability. Researchers have focused on characterizing its structure, understanding its interaction mechanisms, and exploring its implications in diseases characterized by dysregulated polyamine metabolism, such as cancer and neurodegenerative disorders. Investigations into SPEB’s structural dynamics and binding affinities have revealed insights into its functional mechanisms, paving the way for novel biomolecular applications. Furthermore, the development of SPEB as a recombinant protein allows for enhanced studies into its functionality and potential for therapeutic interventions. The continued exploration of SPEB promises to unveil critical information regarding its role in cellular processes and contribute to advancements in targeted treatments for related diseases, thereby solidifying its importance in modern biochemistry research.
