Analytical Data
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Gene name
IGHG2
- Application
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Alternative Names
IGHG2；Immunoglobulin heavy constant gamma 2
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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
P01859
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Expression Region
99-326aa
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AA Sequence
ERKCCVECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHE DPEVQFNWYVDGVEVHNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEY KCKVSNKGLPAPIEKTISKTKGQPREPQVYTLPPSREEMTKNQVSLTCLV KGFYPSDISVEWESNGQPENNYKTTPPMLDSDGSFFLYSKLTVDKSRWQQ GNVFSCSVMHEALHNHYTQKSLSLSPGK
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Molecular Weight
26 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
Recombinant IGHG2 protein, a subclass of immunoglobulin G (IgG), plays a pivotal role in the immune response by providing a mechanism for the recognition and neutralization of pathogens. The study of IGHG2 is particularly significant due to its involvement in various immunological processes and diseases, including autoimmune disorders and infections. Research has increasingly focused on the production of recombinant IGHG2 proteins to advance therapeutic applications, such as developing monoclonal antibodies for targeted therapies. The ability to produce IGHG2 in a recombinant form allows for the exploration of its structure-function relationships and the optimization of its properties for better efficacy and reduced immunogenicity. Furthermore, understanding the biophysical characteristics and binding affinities of recombinant IGHG2 can facilitate vaccine development and enhance diagnostic assays. As the demand for therapeutic antibodies rises, the study of IGHG2 continues to offer valuable insights that could lead to innovative biomedical applications, highlighting its importance in both basic research and clinical settings.
