Analytical Data
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Gene name
ibpA
- Application
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Alternative Names
ibpA；Cell division control Protein 42 homolog
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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
P0C054
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Expression Region
1-137aa
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AA Sequence
MRNFDLSPLY RSAIGFDRLF NHLENNQSQS NGGYPPYNVE LVDENHYRIA IAVAGFAESE LEITAQDNLL VVKGAHADEQ KERTYLYQGI AERNFERKFQ LAENIHVRGA NLVNGLLYID LERVIPEAKK PRRIEIN
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Molecular Weight
15.7 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
The study of the IBP (Ice-Binding Protein) A recombinant protein has gained significant attention due to its unique ability to bind to ice crystals, which plays a crucial role in the survival of certain microorganisms in extreme cold environments. These proteins are known for their potential applications in various fields, including food preservation, cryopreservation of cells and tissues, and enhancing the freeze tolerance of crops. IBP A, specifically, has been identified in certain psychrophilic bacteria that thrive in cold habitats, making it an interesting subject for research aimed at understanding its structural characteristics and functional mechanisms. By utilizing recombinant DNA technology, researchers can produce IBP A in model organisms, allowing for detailed biochemical analysis. Studies on this protein not only advance our knowledge of cold adaptation in organisms but also offer insights into potential biotechnological applications. For instance, the ability of IBP A to inhibit ice crystal growth can lead to new methods for improving the storage and quality of perishable food items, as well as developing innovative strategies for preserving biological materials under freezing conditions. Consequently, the exploration of IBP A and other ice-binding proteins is paving the way for novel solutions to tackle challenges in food security, agriculture, and biotechnology, highlighting the relevance of this research in both fundamental science and practical applications.
