Mouse Anti-NFE2L1 Recombinant Antibody (CBYJT-1495) (CBMAB-T0526-YJ)

Mouse

Human

CBYJT-1495

IgG2a

WB

NRF1 antibody detects endogenous levels of NRF1 and does not cross-react with related proteins

Human

IgG2a

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

100 mM Tris-glycine, 150 mM NaCl, pH 7.4, 0.1% BSA, 50% Glycerol

0.2% Sodium Azide

Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Nuclear Factor, Erythroid 2 Like 1

NFE2L1 is a protein that is involved in globin gene expression in erythrocytes. Confusion has occurred in bibliographic databases due to the shared symbol of NRF1 for NFE2L1, NFE2L1, and for "nuclear respiratory factor 1" which has an official symbol of NRF1.

Nuclear Factor, Erythroid 2 Like 1; Nuclear Factor, Erythroid Derived 2, Like 1; Locus Control Region-Factor 1; Transcription Factor LCR-F1; Transcription Factor HBZ17; NF-E2-Related Factor 1; NFE2-Related Factor 1; TCF-11; TCF11

Endoplasmic reticulum membrane sensor NFE2L1:
Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (PubMed:20932482, PubMed:24448410).

Constitutes a precursor of the transcription factor NRF1 (By similarity).

Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (PubMed:20932482).

In response to stress, it is released from the endoplasmic reticulum membrane following cleavage by the protease DDI2 and translocates into the nucleus to form the transcription factor NRF1 (By similarity).

Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal, such as CD36 (By similarity).

Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (PubMed:20932482).

Transcription factor NRF1:
CNC-type bZIP family transcription factor that translocates to the nucleus and regulates expression of target genes in response to various stresses (PubMed:8932385, PubMed:9421508).

Heterodimerizes with small-Maf proteins (MAFF, MAFG or MAFK) and binds DNA motifs including the antioxidant response elements (AREs), which regulate expression of genes involved in oxidative stress response (PubMed:8932385, PubMed:9421508).

Activates or represses expression of target genes, depending on the context (PubMed:8932385, PubMed:9421508).

Plays a key role in cholesterol homeostasis by acting as a sensor of cholesterol excess: in low cholesterol conditions, translocates into the nucleus and represses expression of genes involved in defense against cholesterol excess, such as CD36 (By similarity).

In excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal (By similarity).

Critical for redox balance in response to oxidative stress: acts by binding the AREs motifs on promoters and mediating activation of oxidative stress response genes, such as GCLC, GCLM, GSS, MT1 and MT2 (By similarity).

Plays an essential role during fetal liver hematopoiesis: probably has a protective function against oxidative stress and is involved in lipid homeostasis in the liver (By similarity).

Involved in proteasome homeostasis: in response to proteasome inhibition, mediates the 'bounce-back' of proteasome subunits by translocating into the nucleus and activating expression of genes encoding proteasome subunits (PubMed:20932482).

Also involved in regulating glucose flux (By similarity).

Together with CEBPB; represses expression of DSPP during odontoblast differentiation (PubMed:15308669).

In response to ascorbic acid induction, activates expression of SP7/Osterix in osteoblasts.

Anatomical structure morphogenesis Source: ProtInc
Cell redox homeostasis Source: UniProtKB
Cellular response to cholesterol Source: UniProtKB
Cellular response to oxidative stress Source: UniProtKB
Cholesterol homeostasis Source: UniProtKB
Cholesterol metabolic process Source: UniProtKB-KW
Heme biosynthetic process Source: ProtInc
Integrated stress response signaling Source: ComplexPortal
Lipid homeostasis Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Negative regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Positive regulation of transcription from RNA polymerase II promoter in response to stress Source: UniProtKB
Regulation of odontoblast differentiation Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central

Endoplasmic reticulum membrane sensor NFE2L1:
Endoplasmic reticulum
Endoplasmic reticulum membrane
Note: In normal conditions, probably has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (PubMed:24448410). Following cellular stress, it is rapidly and efficiently retrotranslocated to the cytosolic side of the membrane, a process dependent on p97/VCP, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (PubMed:24448410). Retrotranslocated proteins are normally rapidly degraded by the proteasome and active species do not accumulate (PubMed:24448410). However, retrotranslocated protein NFE2L1 escapes degradation and is cleaved at Leu-104 by DDI2, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus (PubMed:24448410).
Transcription factor NRF1:
Nucleus
Note: Translocates into the nucleus following cleavage of Endoplasmic reticulum membrane sensor NFE2L1 by aspartyl protease DDI2.

Helical: 7-24

Endoplasmic reticulum membrane sensor NFE2L1:
Cleaved at Leu-104 by the aspartyl protease DDI2 following retrotranslocation, releasing the protein from the endoplasmic reticulum membrane and forming the transcription factor NRF1 that translocates into the nucleus (PubMed:24448410, PubMed:27676297, PubMed:27676298, PubMed:27528193). Ubiquitination is prerequisite for cleavage by aspartyl protease DDI2 (PubMed:27676298).
Endoplasmic reticulum membrane sensor NFE2L1:
N-glycosylated in normal conditions, when it has a single-pass type II membrane protein topology, with the DNA-binding domain facing the endoplasmic reticulum lumen (PubMed:20932482, PubMed:24998528, PubMed:24448410, PubMed:27528193). Deglycosylated during retrotranslocation to the cytosolic side of the membrane, to have a single-pass type III membrane protein topology with the major part of the protein facing the cytosol (PubMed:20932482, PubMed:24998528, PubMed:24448410).
Endoplasmic reticulum membrane sensor NFE2L1:
Ubiquitinated by the SCF(FBXW7) complex and SYVN1/HRD1, leading to its degradation by the proteasome (PubMed:20932482). Ubiquitinated during retrotranslocation to the cytosolic side of the membrane: ubiquitination does not lead to degradation and is required for processing by the aspartyl protease DDI2 and subsequent release from the endoplasmic reticulum membrane (PubMed:24998528, PubMed:27676298).
Transcription factor NRF1:
Phosphorylation by CK2 at Ser-528 inhibits transcription factor activity, possibly by affecting DNA-binding activity (By similarity). Phosphorylation at Ser-599 is required for interaction with CEBPB (PubMed:15308669).
Transcription factor NRF1:
Ubiquitinated by the SCF(BTRC) complex in the nucleus, leading to its degradation by the proteasome.