Analytical Data
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Gene name
IgM
- Application
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Alternative Names
IgM；CD40L；TNFSF5；TRAP；CD40 ligand
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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
P01871
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Expression Region
1-474aa
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AA Sequence
MNYYWGQRTLVTVSSGSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLP DSITFSWKYKNNSDISSTRGFPSVLRGGKYAATSQVLLPSKDVMQGTDEH VVCKVQHPNGNKEKNVPLPVIAELPPKVSVFVPPRDGFFGNPRKSKLICQ ATGFSPRQIQVSWLREGKQVGSGVTTDQVQAEAKESGPTTYKVTSTLTIK ESDWLGQSMFTCRVDHRGLTFQQNASSMCVPDQDTAIRVFAIPPSFASIF LTKSTKLTCLVTDLTTYDSVTISWTRQNGEAVKTHTNISESHPNATFSAV GEASICEDDWNSGERFTCTVTHTDLPSPLKQTISRPKGVALHRPDVYLLP PAREQLNLRESATITCLVTGFSPADVFVQWMQRGQPLSPEKYVTSAPMPE PQAPGRYFAHSILTVSEEEWNTGETYTCVVAHEALPNRVTERTVDKSTEG EVSADEEGFENLWATASTFIVLFLLSLFYSTTVTLFKVK
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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
Immunoglobulin M (IgM) is the first antibody produced in response to an infection, playing a critical role in the immune system. Its distinctive pentameric structure allows for efficient binding to pathogens and activation of the complement system, thus facilitating opsonization and neutralization of invaders. Recent advancements in biotechnology have enabled the recombinant production of IgM proteins, offering significant advantages over classical methods, such as improved yield, enhanced purity, and the ability to introduce specific modifications for research and therapeutic purposes. The study of recombinant IgM proteins has become increasingly important in understanding the antibody's functional mechanisms, exploring its interactions with various antigens, and developing novel diagnostic tools and vaccines. Furthermore, recombinant IgM can be engineered for targeted drug delivery or used as a platform for developing new immunotherapies, particularly in combating infectious diseases and enhancing the efficacy of cancer treatments. As researchers continue to delve into the complexities of IgM structure and function, the recombinant approach serves as a powerful tool to unlock its full potential in both basic research and clinical applications.
