Analytical Data
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Gene name
frmA
- Application
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Alternative Names
frmA;FERM domain-containing Protein A
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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
Q1RFI7
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Expression Region
1-369aa
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AA Sequence
MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFELARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAGSGQEISTRPFQLVTGRVWKGSAFGGVKGRSQLPGMVEDAMKGDIDLEPFVTHTMSLDEINDAFDLMHEGKSIRTVIRY
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Molecular Weight
46.8 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
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Protein Description
frmA recombinant protein, derived from the frmA gene, plays a crucial role in various biological and biotechnological studies. This gene encodes a protein that is involved in metabolic processes, contributing to the understanding of cellular functions and mechanisms. Researchers have increasingly focused on frmA due to its potential applications in the production of biofuels, pharmaceuticals, and bioremediation. The expression and purification of frmA recombinant protein allow scientists to study its structure and function in detail, providing insights into enzyme kinetics and interaction with substrates. Additionally, investigations into the physiological role of frmA in different organismal contexts enhance our understanding of evolutionary biology and metabolic diversity. Advances in recombinant DNA technology have facilitated the generation of frmA proteins in host systems, yielding high purity and activity essential for experimental purposes. Overall, the study of frmA recombinant protein contributes significantly to the fields of molecular biology, biotechnology, and environmental science.











