|Application ||WB, E|
|Calculated MW||43917 Da|
|Antigen Region||66-94 aa|
|Other Names||Cyclic AMP-responsive element-binding protein 3, CREB-3, cAMP-responsive element-binding protein 3, Leucine zipper protein, Luman, Transcription factor LZIP-alpha, Processed cyclic AMP-responsive element-binding protein 3, N-terminal Luman, Transcriptionally active form, CREB3, LZIP|
|Target/Specificity||This CREB3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 66-94 amino acids from the N-terminal region of human CREB3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CREB3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Endoplasmic reticulum (ER)-bound transcription factor that plays a role in the unfolded protein response (UPR). Involved in cell proliferation and migration, tumor suppression and inflammatory gene expression. Plays also a role in the human immunodeficiency virus type 1 (HIV-1) virus protein expression and in the herpes simplex virus-1 (HSV-1) latent infection and reactivation from latency. Isoform 2 plays a role in the unfolded protein response (UPR). Isoform 2 acts as a positive regulator of LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell migration. Isoform 2 may play a role as a cellular tumor suppressor that is targeted by the hepatitis C virus (HSV) core protein. Isoform 2 represses the VP16-mediated transactivation of immediate early genes of the HSV-1 virus by sequestring 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 3 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). Isoform 3 decreases the acetylation level of histone H4. Isoform 3 does not promote the chemotactic activity of leukocyte cells.|
|Cellular Location||Isoform 2: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Membrane. Note=Colocalizes with HCFC1 in neuronal cell bodies of the trigeminal ganglia (By similarity). Colocalizes with TM7SF4 in the ER membrane of immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1 in the ER membrane. Sequestred into the cytoplasm by the HCV core protein. Processed cyclic AMP-responsive element- binding protein 3: Nucleus. Note=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)|
|Tissue Location||Expressed in dendritic cells (DC). Weakly expressed in monocytes (at protein level). Ubiquitous|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-response element and regulates cell proliferation. The protein interacts with host cell factor C1, which also associates with the herpes simplex virus (HSV) protein VP16 that induces transcription of HSV immediate-early genes. This protein and VP16 both bind to the same site on host cell factor C1. It is thought that the interaction between this protein and host cell factor C1 plays a role in the establishment of latency during HSV infection. This protein also plays a role in leukocyte migration, tumor suppression, and endoplasmic reticulum stress-associated protein degradation. Additional transcript variants have been identified, but their biological validity has not been determined.
Kim, H.C., et al. Cell. Mol. Life Sci. 67(20):3499-3510(2010)
Eleveld-Trancikova, D., et al. Mol. Immunol. 47 (11-12), 1963-1973 (2010) :
Kang, H., et al. Mol. Endocrinol. 23(11):1746-1757(2009)
Mamdani, F., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (4), 500-504 (2008) :
Audas, T.E., et al. Mol. Cell. Biol. 28(12):3952-3966(2008)
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