Species : |
Human |
Source : |
HEK293 |
Tag : |
Fc |
Protein Length : |
1-247 a.a. |
Description : |
Interferon-gamma (IFN-gamma) is a pleotropic cytokine expressed predominantly by naïve and activated CD8+ and TH1 CD4+ T cells, and natural killer (NK) cells and, as such, promotes both innate and adaptive immune responses. |
Amino Acid Sequence : |
SQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYRVQFKYTDSKWFTADIMSIGVNCTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPENIEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPSRVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQGSSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK. |
Molecular Mass : |
IFN-gamma R2 – Fc Chimera migrates as a broad band between 65 and 75 kDa on SDS-PAGE due to post-translation modifications, in particular glycosylation. This compares with the unmodified IFN-gamma R2 - Fc Chimera that has a predicted molecular mass of 52 kDa. |
pI : |
IFN-gamma R2 – Fc Chimera separates into a number of glycoforms with a pI between 5.5 and 8 on 2D PAGE due to post-translational modifications, in particular glycosylation. |
% Carbohydrate : |
Purified IFN-gamma R2 – Fc Chimera consists of 20-30% carbohydrate by weight. |
Glycosylation : |
IFN-gamma R2 – Fc Chimera has N- and possibly O-linked oligosaccharides. |
Purity : |
>95%, as determined by SDS-PAGE and visualized by Coomassie Brilliant Blue. |
Formulation : |
When reconstituted in 0.5 ml sterile phosphate-buffered saline, the solution will contain 1% human serum albumin (HSA) and 10% trehalose. |
Reconstitution : |
It is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. |
Storage : |
Lyophilized products should be stored at 2 to 8°C. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. Repeated freeze thawing is not recommended. |