Summary:
Recombinant human FICD protein
Cat：P02724
| 【Derived From】： E.coli |
| 【Endotoxin】： Not measured |
| 【Amino Acid】： 131-450aa |
| 【Purity】： ≥85% by SDS-PAGE. |
| 【Name】： FICD |
| 【Full Name】： FIC domain containing |
| 【Uniprot】： Q9BVA6 |
| 【Gene ID】： 11153 |
| 【Species Reactivity】： Human Mouse Rat (Zebrafish) |
| 【Mol Mass】： 35kDa |
| 【Application】： Immunology research |
| 【Purification】： NI-NTA affinity purification |
| 【Bioactive】： N0 |
| 【Tag】： With a 6×His tag at the N/C-terminus. |
| 【Concentration】： 1mg/ml by SDS-PAGE. |
Store:
| 【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.) |
| 【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks， stored at < -20℃ for 1 year. |
| 【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0. |
Background:
Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity).The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity).Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:25601083).In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity).In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity).Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (PubMed:19362
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