Analytical Data
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Gene name
serB2
- Application
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Alternative Names
Phosphoserine phosphatase SerB2; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; 3.1.3.16; serB2; Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv); Hydrolase; 3.1.3.3
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O53289
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Expression Region
M1-D409
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Protein Length
Full Length
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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
SerB2, an enzyme belonging to the serine racemase family, plays a crucial role in the metabolism of serine, a non-essential amino acid significant for protein synthesis, neurotransmission, and various metabolic pathways. Research on SerB2 has gained attention due to its involvement in maintaining serine homeostasis and its implications in neurodevelopmental disorders and metabolic diseases. Previous studies have indicated that dysregulation of serine levels can lead to severe consequences, including cognitive deficits and increased susceptibility to neurological disorders. As such, understanding the structure, function, and regulation of SerB2 is of paramount importance. Recombinant protein technology has enabled researchers to produce SerB2 in a controlled environment, facilitating in-depth studies on its enzymatic activity, substrate specificity, and interaction with other biomolecules. These insights are critical for developing potential therapeutic strategies targeting SerB2-related pathways. The ongoing exploration of SerB2’s properties, along with its potential roles in human health and disease, underscores the enzyme's importance and the need for comprehensive research in this area.
