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Mouse Anti-CREB3 Recombinant Antibody (CBFYC-2195) (V2LY-1206-LY1101)

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Summary

Host Animal
Mouse
Specificity
Mouse
Clone
CBFYC-2195
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 29-54 near the N-terminus of mouse LZIP.
Host Species
Mouse
Specificity
Mouse
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
0.1% gelatin
Preservative
0.09% sodium azide
Concentration
0.2 mg/ml
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
Entrez Gene ID
UniProt ID
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.
More Infomation

Yu, M., Tan, L., Li, Y., Chen, J., Zhai, Y., Rao, J., ... & Shen, Q. (2020). Intrauterine low-protein diet aggravates developmental abnormalities of the urinary system via the Akt/Creb3 pathway in Robo2 mutant mice. American Journal of Physiology-Renal Physiology, 318(1), F43-F52.

Zhao, F., Liu, H., Wang, N., Yu, L., Wang, A., Yi, Y., & Jin, Y. (2020). Exploring the role of Luman/CREB3 in regulating decidualization of mice endometrial stromal cells by comparative transcriptomics. BMC genomics, 21(1), 1-14.

Hu, Y., Chu, L., Liu, J., Yu, L., Song, S. B., Yang, H., & Han, F. (2019). Knockdown of CREB3 activates endoplasmic reticulum stress and induces apoptosis in glioblastoma. Aging (Albany NY), 11(19), 8156.

Wang, L., Lu, M., Zhang, R., Guo, W., Lin, P., Yang, D., ... & Jin, Y. (2019). Inhibition of Luman/CREB3 expression leads to the upregulation of testosterone synthesis in mouse Leydig cells. Journal of Cellular Physiology, 234(9), 15257-15269.

Sampieri, L., Di Giusto, P., & Alvarez, C. (2019). CREB3 transcription factors: ER-Golgi stress transducers as hubs for cellular homeostasis. Frontiers in cell and developmental biology, 7, 123.

Sabaratnam, K., Renner, M., Paesen, G., Harlos, K., Nair, V., Owens, R. J., & Grimes, J. M. (2019). Insights from the crystal structure of the chicken CREB3 bZIP suggest that members of the CREB3 subfamily transcription factors may be activated in response to oxidative stress. Protein Science, 28(4), 779-787.

Oh‐hashi, K., Takahashi, K., & Hirata, Y. (2019). Regulation of the ER‐bound transcription factor Luman/CREB3 in HEK293 cells. FEBS letters, 593(19), 2771-2778.

Wu, K., Huang, J., Xu, T., Ye, Z., Jin, F., Li, N., & Lv, B. (2019). MicroRNA-181b blocks gensenoside Rg3-mediated tumor suppression of gallbladder carcinoma by promoting autophagy flux via CREBRF/CREB3 pathway. American journal of translational research, 11(9), 5776.

Zhao, X., Li, P., An, K., Jia, X., Cheng, Y., & Jia, T. (2017). Chlamydia pneumoniae inclusion membrane protein Cpn0147 interacts with host protein CREB3. Plos one, 12(9), e0185593.

Greenwood, M. P., Greenwood, M., Gillard, B. T., Chitra Devi, R., & Murphy, D. (2017). Regulation of cAMP responsive element binding protein 3-Like 1 (Creb3l1) expression by orphan nuclear receptor Nr4a1. Frontiers in molecular neuroscience, 10, 413.

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For research use only. Not intended for any clinical use.

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