|Other Accession||NP_009007.2, 11153, 231630 (mouse), 288741 (rat)|
|Predicted||Human, Mouse, Rat, Pig, Dog, Cow|
|Calculated MW||51778 Da|
|Other Names||Adenosine monophosphate-protein transferase FICD, 2.7.7.n1, AMPylator FICD, FIC domain-containing protein, Huntingtin yeast partner E, Huntingtin-interacting protein 13, HIP-13, Huntingtin-interacting protein E, FICD, HIP13, HYPE|
|Format||0.5 mg/ml in Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HYPE / FICD Antibody (internal region) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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:19362538, PubMed:25601083).|
|Cellular Location||Endoplasmic reticulum membrane; Single-pass type II membrane protein|
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Provided below are standard protocols that you may find useful for product applications.
The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark Genome research 2003 Oct 13 (10): 2265-70. PMID: 12975309
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