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Rabbit Anti-CEBPB Recombinant Antibody (CBXC-1674) (CBMAB-C4559-CQ)

This product is a rabbit antibody that recognizes CEBPB. The antibody CBXC-1674 can be used for immunoassay techniques such as: ICC, IF, IP, WB.
See all CEBPB antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Rat
Clone
CBXC-1674
Antibody Isotype
IgG
Application
ICC, IF, IP, WB

Basic Information

Immunogen
Synthetic peptide corresponding to residues in the C-terminus of rat C/EBP beta
Specificity
Human, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Buffer
PBS, pH 7.2, 0.05% BSA, 50% glycerol
Preservative
0.01% sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
C-Term

Target

Full Name
CCAAT/Enhancer Binding Protein Beta
Introduction
This intronless gene encodes a transcription factor that contains a basic leucine zipper (bZIP) domain. The encoded protein functions as a homodimer but can also form heterodimers with CCAAT/enhancer-binding proteins alpha, delta, and gamma. Activity of this protein is important in the regulation of genes involved in immune and inflammatory responses, among other processes. The use of alternative in-frame AUG start codons results in multiple protein isoforms, each with distinct biological functions.
Entrez Gene ID
Human1051
Rat24253
UniProt ID
HumanP17676
RatP21272
Alternative Names
CCAAT/Enhancer Binding Protein Beta; CCAAT/Enhancer Binding Protein (C/EBP), Beta; Interleukin 6-Dependent DNA-Binding Protein; Nuclear Factor Of Interleukin 6; Transcription Factor 5; Nuclear Factor NF-IL6; TCF5; Liver-Enriched Transcriptional Activator Protein; CCAAT/Enhancer-Binding Protein Beta; Liver-Enriched Inhibitory Protein;
Function
Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:1741402, PubMed:9374525, PubMed:12048245, PubMed:18647749).
Plays also a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant functions with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Plays also a role in intracellular bacteria killing (By similarity).
During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347).
Essential for female reproduction because of a critical role in ovarian follicle development (By similarity).
Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity).
Isoform 2:
Essential for gene expression induction in activated macrophages. Plays a major role in immune responses such as CD4+ T-cell response, granuloma formation and endotoxin shock. Not essential for intracellular bacteria killing.
Isoform 3:
Acts as a dominant negative through heterodimerization with isoform 2 (PubMed:11741938).
Promotes osteoblast differentiation and osteoclastogenesis (By similarity).
Biological Process
Acute-phase response Source: ProtInc
Brown fat cell differentiation Source: Ensembl
Cellular response to amino acid starvation Source: Reactome
Cellular response to amino acid stimulus Source: Ensembl
Cellular response to interleukin-1 Source: Ensembl
Cellular response to lipopolysaccharide Source: Ensembl
Cellular response to organic cyclic compound Source: Ensembl
Defense response to bacterium Source: UniProtKB
Embryonic placenta development Source: Ensembl
Granuloma formation Source: UniProtKB
Hepatocyte proliferation Source: UniProtKB
Immune response Source: ProtInc
Inflammatory response Source: ProtInc
Intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Liver regeneration Source: UniProtKB
Mammary gland epithelial cell differentiation Source: Ensembl
Mammary gland epithelial cell proliferation Source: Ensembl
Memory Source: Ensembl
Negative regulation of neuron apoptotic process Source: Ensembl
Negative regulation of T cell proliferation Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Neuron differentiation Source: Ensembl
Ovarian follicle development Source: UniProtKB
Positive regulation of biomineral tissue development Source: MGI
Positive regulation of cold-induced thermogenesis Source: YuBioLab
Positive regulation of fat cell differentiation Source: UniProtKB
Positive regulation of inflammatory response Source: Ensembl
Positive regulation of interleukin-4 production Source: UniProtKB
Positive regulation of osteoblast differentiation Source: Ensembl
Positive regulation of sodium-dependent phosphate transport Source: MGI
Positive regulation of transcription, DNA-templated Source: MGI
Positive regulation of transcription by RNA polymerase II Source: MGI
Positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Regulation of cell differentiation Source: GO_Central
Regulation of dendritic cell differentiation Source: Ensembl
Regulation of eIF2 alpha phosphorylation by heme Source: Reactome
Regulation of interleukin-6 production Source: Ensembl
Regulation of odontoblast differentiation Source: UniProtKB
regulation of osteoclast differentiation Source: UniProtKB
regulation of transcription, DNA-templated Source: UniProtKB
regulation of transcription by RNA polymerase II Source: UniProtKB
regulation of transcription initiation from RNA polymerase II promoter Source: Reactome
response to endoplasmic reticulum stress Source: UniProtKB
T-helper 1 cell activation Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus. Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity).
PTM
Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-235.
Sumoylated by polymeric chains of SUMO2 or SUMO3 (PubMed:12810706). Sumoylation at Lys-174 is required for inhibition of T-cells proliferation. In adipocytes, sumoylation at Lys-174 by PIAS1 leads to ubiquitination and subsequent proteasomal degradation. Desumoylated by SENP2, which abolishes ubiquitination and stabilizes protein levels (By similarity).
Ubiquitinated, leading to proteasomal degradation.
Phosphorylated at Thr-235 by MAPK and CDK2, serves to prime phosphorylation at Thr-226 and Ser-231 by GSK3B and acquire DNA-binding as well as transactivation activities, required to induce adipogenesis. MAPK and CDK2 act sequentially to maintain Thr-235 in the primed phosphorylated state during mitotical cloning expansion and thereby progression of terminal differentiation. Phosphorylation at Thr-266 enhances transactivation activity. Phosphorylation at Ser-325 in response to calcium increases transactivation activity. Phosphorylated at Thr-235 by RPS6KA1 (PubMed:11684016).
O-glycosylated, glycosylation at Ser-227 and Ser-228 prevents phosphorylation on Thr-235, Ser-231 and Thr-226 and DNA binding activity which delays the adipocyte differentiation program.
Acetylated. Acetylation at Lys-43 is an important and dynamic regulatory event that contributes to its ability to transactivate target genes, including those associated with adipogenesis and adipocyte function. Deacetylation by HDAC1 represses its transactivation activity. Acetylated by KAT2A and KAT2B within a cluster of lysine residues between amino acids 129-133, this acetylation is strongly induced by glucocorticoid treatment and enhances transactivation activity.

Zhang, X., Wu, Z., Bu, M., Hu, R., Zhang, X., Li, W., & Chen, L. (2021). The CCAAT/Enhancer Binding Protein Beta (cebpb) is essential for the development of enveloping layer (EVL) in zebrafish. Aquaculture and Fisheries.

Lala‐Tabbert, N., AlSudais, H., Marchildon, F., Fu, D., & Wiper‐Bergeron, N. (2021). CCAAT/enhancer‐binding protein beta promotes muscle stem cell quiescence through regulation of quiescence‐associated genes. STEM CELLS, 39(3), 345-357.

Lee, G., Jang, E., & Youn, J. (2020). CCAAT/enhancer binding protein β Induces post-switched B cells to produce Blimp1 and differentiate into plasma cells. Immune Network, 20(5).

Merrett, J. E., Bo, T., Psaltis, P. J., & Proud, C. G. (2020). Identification of DNA response elements regulating expression of CCAAT/enhancer-binding protein (C/EBP) β and δ and MAP kinase-interacting kinases during early adipogenesis. Adipocyte, 9(1), 427-442.

Yang, H., Kang, M. J., Hur, G., Lee, T. K., Park, I. S., Seo, S. G., ... & Lee, K. W. (2020). Sulforaphene suppresses adipocyte differentiation via induction of post-translational degradation of CCAAT/Enhancer binding protein beta (C/EBPβ). Nutrients, 12(3), 758.

AlSudais, H., & Wiper-Bergeron, N. (2019). Contaminating reactivity of a monoclonal CCAAT/Enhancer Binding Protein β antibody in differentiating myoblasts. BMC research notes, 12(1), 1-6.

AlSudais, H., Lala-Tabbert, N., & Wiper-Bergeron, N. (2018). CCAAT/Enhancer Binding Protein β inhibits myogenic differentiation via ID3. Scientific reports, 8(1), 1-10.

Simpson-Abelson, M. R., Hernandez-Mir, G., Childs, E. E., Cruz, J. A., Poholek, A. C., Chattopadhyay, A., ... & McGeachy, M. J. (2017). CCAAT/Enhancer-binding protein β promotes pathogenesis of EAE. Cytokine, 92, 24-32.

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

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