|Other Names||Insulin-induced gene 1 protein, INSIG-1, INSIG1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8940a was selected from the N-term region of human INSIG1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Mediates feedback control of cholesterol synthesis by controlling SCAP and HMGCR. Functions by blocking the processing of sterol regulatory element-binding proteins (SREBPs). Capable of retaining the SCAP-SREBF2 complex in the ER thus preventing it from escorting SREBPs to the Golgi. Initiates the sterol-mediated ubiquitin-mediated endoplasmic reticulum-associated degradation (ERAD) of HMGCR via recruitment of the reductase to the ubiquitin ligase, AMFR/gp78. May play a role in growth and differentiation of tissues involved in metabolic control. May play a regulatory role during G0/G1 transition of cell growth.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein|
|Tissue Location||Expressed in all tissues tested with highest expression in the liver.|
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Provided below are standard protocols that you may find useful for product applications.
INSIG1 is an insulin-induced protein. This protein encodes an endoplasmic reticulum (ER) membrane protein that plays a critical role in regulating cholesterol concentrations in cells. This protein binds to the sterol-sensing domains of SREBP cleavage-activating protein (SCAP) and HMG CoA reductase, and is essential for the sterol-mediated trafficking of the two proteins.
Smith,E.M., et.al., J. Lipid Res. 51 (4), 701-708 (2010)Liu,X., et.al., Atherosclerosis 208 (2), 421-426 (2010)
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