HEK-293 Cells IgG2 Isotype Control
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- Antigène Tous les produits IgG2
- IgG2
- Reactivité
- Humain
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Hôte
- HEK-293 Cells
- Application
- Isotype Control (IsoC)
- Attributs du produit
- This protein carries no "tag". The protein has a calculated MW of 25.7 kDa. The protein migrates as 33-35 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
- Pureté
- >95 % as determined by SDS-PAGE.
- Stérilité
- 0.22 μm filtered
- niveau d'endotoxine
- Less than 1.0 EU per μg by the LAL method.
- Isotype
- IgG2
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- Indications d'application
- Optimal working dilution should be determined by the investigator.
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
- Buffer
- 50 mM Tris, 100 mM Glycine, pH 7.5
- Conseil sur la manipulation
- Avoid repeated freeze-thaw cycles.
- Stock
- -20 °C
- Stockage commentaire
- No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
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- Antigène
- IgG2
- Abstract
- IgG2 Produits
- Synonymes
- FCGR2B Isotype Control, Fc fragment of IgG, low affinity IIb, receptor (CD32) Isotype Control, FCGR2B Isotype Control
- Classe de substances
- Antibody
- Sujet
- Immunoglobulin G2 (IgG2) is a member of many immunoglobulin G developed and secreted by effective B cells. In wake of cutting by pepsin, IgG is divided into two F(ab)s with one antigen binding site and a high conserved Fc segment. The Fc segment bears a highly conserved N-glycosylation site. There are two members of IgG2: IgG2a and IgG2b. It was found that IgG2a was superior to IgG1 in activating complement. The glycosylation of the circulating immunoglobulin-γ (IgG) antibody molecules changes in rheumatoid arthritis. Ig gamma-2 chain Fc region contains two constant regions of IgG2 H chain (CH2, CH3).
- Poids moléculaire
- 25.7 kDa
- UniProt
- P01859
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