Summary
Application
WB, IP, IF, ELISA
Basic Information
Immunogen
Amino acids 29-54 near the N-terminus of mouse LZIP.
Clonality
Monoclonal Antibody
Application Notes
Application | Note |
WB | 1:100-1:1,000 |
IP | 1-2 µg per 100-500 µg of total
protein (1 ml of cell lysate) |
IF(ICC) | 1:50-1:500 |
ELISA | 1:100-1:1,000 |
Formulations & Storage [For reference only, actual COA shall prevail!]
Preservative
0.09% sodium azide
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
Target
Full Name
CAMP Responsive Element Binding Protein 3
Function
Endoplasmic reticulum (ER)-bound sequence-specific transcription factor that directly binds DNA and activates transcription (PubMed:9271389, PubMed:19779205, PubMed:10984507, PubMed:15845366, PubMed:16940180).
Plays a role in the unfolded protein response (UPR), promoting cell survival versus ER stress-induced apoptotic cell death (PubMed:15845366, PubMed:16940180).
Also involved in cell proliferation, migration and differentiation, tumor suppression and inflammatory gene expression. Acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration (PubMed:19779205, PubMed:15001559, PubMed:17296613).
Associates with chromatin to the HERPUD1 promoter (PubMed:16940180).
Also induces transcriptional activation of chemokine receptors (PubMed:18587271, PubMed:17296613).
Processed cyclic AMP-responsive element-binding protein 3:
This is the transcriptionally active form that translocates to the nucleus and activates unfolded protein response (UPR) target genes during endoplasmic reticulum (ER) stress response. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many promoters to activate transcription of the genes. Binds to the unfolded protein response element (UPRE) consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3').
Isoform 2:
Functions as a negative transcriptional regulator in ligand-induced transcriptional activation of the glucocorticoid receptor NR3C1 by recruiting and activating histone deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the acetylation level of histone H4. Does not promote the chemotactic activity of leukocyte cells.
(Microbial infection) Plays a role in human immunodeficiency virus type 1 (HIV-1) virus protein expression.
Isoform 1:
(Microbial infection) Plays a role in herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestering host cell factor-1 HCFC1 in the ER membrane of sensory neurons, thereby preventing the initiation of the replicative cascade leading to latent infection.
Isoform 1:
(Microbial infection) May play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HCV) core protein.
Processed cyclic AMP-responsive element-binding protein 3:
(Microbial infection) Activates transcription of genes required for reactivation of the latent HSV-1 virus. It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator protein VP16. Binds DNA to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral promoters.
Processed cyclic AMP-responsive element-binding protein 3:
(Microbial infection) It's transcriptional activity is inhibited by CREBZF in a HCFC1-dependent manner, by the viral transactivator HCV core protein.
Biological Process
Chemotaxis Source: UniProtKB-KW
Cytoplasmic sequestering of transcription factor Source: UniProtKB
Endoplasmic reticulum unfolded protein response Source: Reactome
Establishment of viral latency Source: UniProtKB
Induction of positive chemotaxis Source: UniProtKB
Negative regulation of cell cycle Source: UniProtKB
Negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Positive regulation of calcium ion transport Source: UniProtKB
Positive regulation of cell migration Source: UniProtKB
Positive regulation of deacetylase activity Source: UniProtKB
Positive regulation of defense response to virus by host Source: UniProtKB
Positive regulation of monocyte chemotaxis Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: ParkinsonsUK-UCL
Regulation of apoptotic process Source: UniProtKB
Regulation of cell growth Source: UniProtKB
Regulation of cell population proliferation Source: UniProtKB
Regulation of transcription by RNA polymerase II Source: GO_Central
Release from viral latency Source: UniProtKB
Response to endoplasmic reticulum stress Source: UniProtKB
Transcription, DNA-templated Source: UniProtKB
Viral process Source: UniProtKB-KW
Cellular Location
Isoform 1: Endoplasmic reticulum membrane; Golgi apparatus. Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia (PubMed:10623756). Colocalizes with DCSTAMP in the ER membrane of immature dendritic cell (DC) (PubMed:20546900). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane (PubMed:10623756).
Isoform 2: Cytoplasm; Nucleus. Predominantly in the nucleus (PubMed:19779205). Not associated with membranes (PubMed:19779205).
Processed cyclic AMP-responsive element-binding protein 3: Nucleus. Upon RIP activation the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form translocates into the nucleus. Detected in the nucleus upon dendritic cell maturation and RIP activation. Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF in promyelocytic leukemia protein nuclear bodies (PML-NB).
Isoform 1: Cytoplasm. (Microbial infection) Sequestered into the cytoplasm by the HCV core protein.
Topology
Cytoplasmic: 1-230
Helical: 231-247
Lumenal: 248-371
PTM
First proteolytically cleaved by site-1 protease (S1P) that generates membrane-associated N-terminus and a luminal C-terminus forms. The membrane-associated N-terminus form is further proteolytically processed probably by the site-2 protease (S2P) through a regulated intramembrane proteolysis (RIP), releasing the transcriptional active processed cyclic AMP-responsive element-binding protein 3 form, which is transported to the nucleus. The proteolytic cleavage is strongly induced during dendritic cell (DC) maturation and inhibited by DCSTAMP. That form is rapidly degraded.
N-glycosylated.