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Recombinant Human IgG2A Protein (RPT0005)

Bioactivityvalidated

Datasheet

Overview

Product nameRecombinant Human IgG2A Protein
Catalog No.RPT0005
DescriptionRecombinant Human IgG2A Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Glu99-Lys326) of human IgG2A (Accession #) fused with and NO-tag at the C-terminus.
Bio-ActivityMeasured by its binding ability in a functional ELISA.Immobilized Human CD32a (Catalog: RP00081) at 2 μg/mL (100 μL/well) can bind Human IgG2 (Catalog: RPT0005) with a linear range of 1.2-338 ng/mL.
Purity> 97% by SDS-PAGE.
Endotoxin<0.1EU/μg
FormulationLyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
SpeciesHuman
Calculated MW25.72 kDa
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens
SynonymIGHG2; Immunoglobulin heavy constant gamma 2; IgG2
Expression HostHEK293 cells
TagNO-tag
Swiss-Prot
Gene ID
StorageStore at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt.
After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
ReconstitutionCentrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.

* For research use only. Not for therapeutic or diagnostic purposes.

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