Analytical Data
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Gene name
AFM
- Application
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Alternative Names
AFM；ALB2；ALBA；Afamin
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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
P43652
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Expression Region
1-599aa
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AA Sequence
MKLLKLTGFIFFLFFLTESLTLPTQPRDIENFNSTQKFIEDNIEYITIIA FAQYVQEATF EEMEKLVKDMVEYKDRCMADKTLPECSKLPNNVLQEKI CAMEGLPQKHNFSHCCSKVDAQ RRLCFFYNKKSDVGFLPPFPTLDPEE KCQAYESNRESLLNHFLYEVARRNPFVFAPTLLT VAVHFEEVAKSCCE EQNKVNCLQTRAIPVTQYLKAFSSYQKHVCGALLKFGTKVVHFIYI AI LSQKFPKIEFKELISLVEDVSSNYDGCCEGDVVQCIRDTSKVMNHICSKQ DSISSKIK ECCEKKIPERGQCIINSNKDDRPKDLSLREGKFTDSENVC QERDADPDTFFAKFTFEYSR RHPDLSIPELLRIVQIYKDLLRNCCNTE NPPGCYRYAEDKFNETTEKSLKMVQQECKHFQ NLGKDGLKYHYLIRLT KIAPQLSTEELVSLGEKMVTAFTTCCTLSEEFACVDNLADLVFG ELCG VNENRTINPAVDHCCKTNFAFRRPCFESLKADKTYVPPPFSQDLFTFHAD MCQSQN EELQRKTDRFLVNLVKLKHELTDEELQSLFTNFANVVDKCCK AESPEVCFNEESPKIGN
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Molecular Weight
96 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
Atomic Force Microscopy (AFM) has emerged as a powerful tool in the study of recombinant proteins due to its ability to provide high-resolution, three-dimensional images of molecular structures at the nanoscale. Recombinant proteins, produced through recombinant DNA technology, are essential in various biomedical applications, including drug development, vaccine production, and enzyme engineering. The characterization of these proteins is vital for understanding their function, stability, and interactions. Traditional techniques, such as X-ray crystallography and NMR spectroscopy, although widely used, may not fully capture the dynamic nature of proteins in their native environments. AFM, on the other hand, allows for the visualization of protein conformations and interactions in real-time, under physiological conditions. This unique capability has opened new avenues for studying protein folding, aggregation, and binding events, providing insights that are critical for the design of more effective therapeutics. Recent advancements in AFM techniques, such as high-speed imaging and force spectroscopy, have further enhanced the resolution and applicability of this approach in protein research. As a result, researchers are increasingly turning to AFM to complement conventional methodologies, aiming to unravel the complexities of recombinant proteins and accelerate the development of innovative solutions in medicine and biotechnology.
