Synthesized peptide derived from human SREBP-2 (Phospho-Ser455)

This antibody detects endogenous levels of SREBP-2 (Phospho-Ser455) at Human, Mouse,Rat.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):PGsPL

SREBF2 BHLHD2 SREBP2

SREBP-2 (Phospho-Ser455)

SRBP2 ;
Sterol regulatory element-binding protein 2 ;
SREBP-2 ;
Class D basic helix-loop-helix protein 2 ;
bHLHd2 ;
Sterol regulatory element-binding transcription factor 2 ;
[Cleaved into: Processed sterol regulatory element-binding protein 2]

This gene encodes a member of the a ubiquitously expressed transcription factor that controls cholesterol homeostasis by regulating transcription of sterol-regulated genes. The encoded protein contains a basic helix-loop-helix-leucine zipper (bHLH-Zip) domain and binds the sterol regulatory element 1 motif. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013],

Function:Transcriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes.,PTM:At low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7.,similarity:Belongs to the SREBP family.,similarity:Contains 1 basic helix-loop-helix (bHLH) domain.,subcellular location:Moves from the endoplasmic reticulum to the Golgi in the absence of sterols.,subunit:Forms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA.,tissue specificity:Ubiquitously expressed in adult and fetal tissues.,

[Sterol regulatory element-binding protein 2]: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Golgi apparatus membrane ; Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane ; Multi-pass membrane protein . At high sterol concentrations, the SCAP-SREBP is retained in the endoplasmic reticulum (PubMed:32322062). Low sterol concentrations promote recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi, where it is processed (PubMed:32322062). .; [Processed sterol regulatory element-binding protein 2]: Nucleus . Transported into the nucleus with the help of importin-beta. Dimerization of the bHLH domain is a prerequisite for importin beta-dependent nuclear import. .