AEBP1
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Official Full Name
AE binding protein 1
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Overview
The adipocyte enhancer binding protein 1 is a transcriptional repressor with carboxypeptidase (CP) activity. This protein binds to a regulatory sequence, adipocyte enhancer 1 (AE-1), located in the proximal promoter region of the adipose P2 (aP2) gene, which encodes the adipocyte fatty-acid binding protein. It is characterized as a member of the regulatory B-like CP family. This protein seems to be activated by a novel mechanism, whereby the direct binding of DNA enhances its protease activity. Adipocyte-enhancer binding protein 1 may play a role in differentiated vascular smooth muscle cells. -
Synonyms
AEBP1; AE binding protein 1; adipocyte enhancer-binding protein 1; ACLP; adipocyte enhancer binding protein 1; aortic carboxypeptidase like protein; AE-binding protein 1; aortic carboxypeptidase-like protein; FLJ33612;
- Recombinant Proteins
- Protein Pre-coupled Magnetic Beads
- Native Proteins
- Human
- Mouse
- Rat
- S.cerevisiae
- E.coli
- E.Coli or Yeast
- HEK293
- Mammalian Cell
- S.cerevisiae
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- His|SUMO
- SUMO
- N/A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Human | AEBP1-394H | Recombinant Human AEBP2 Protein, GST-tagged | Wheat Germ | GST | ||
Mouse | AEBP1-1393M | Recombinant Mouse Aebp1 protein, His/sumo-tagged | E.coli | His/SUMO | ||
Mouse | Aebp1-4526M | Recombinant Mouse Aebp1 protein, His-SUMO-tagged | E.coli | His-SUMO | 26-370aa | |
Rat | Aebp1-3196R | Recombinant Rat Aebp1, His-tagged | E.Coli or Yeast | His | 1128 | |
Rat | AEBP1-550R | Recombinant Rat AEBP1 Protein | Mammalian Cell | His | ||
Rat | AEBP1-206R-B | Recombinant Rat AEBP1 Protein Pre-coupled Magnetic Beads | HEK293 | |||
Rat | AEBP1-206R | Recombinant Rat AEBP1 Protein, His (Fc)-Avi-tagged | HEK293 | His (Fc)-Avi | ||
S.cerevisiae | AEBP1-8321S | Native S. cerevisiae AEBP1 | S.cerevisiae | N/A |
- Involved Pathway
- Protein Function
- Interacting Protein
- AEBP1 Related Research Area
AEBP1 involved in several pathways and played different roles in them. We selected most pathways AEBP1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with AEBP1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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AEBP1 has several biochemical functions, for example, DNA binding, RNA polymerase II regulatory region sequence-specific DNA binding, calmodulin binding. Some of the functions are cooperated with other proteins, some of the functions could acted by AEBP1 itself. We selected most functions AEBP1 had, and list some proteins which have the same functions with AEBP1. You can find most of the proteins on our site.
Function | Related Protein |
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DNA binding | TCF15;MYRFL;HIST1H4C;TFAP2C;IKZF1;EHF;NFYB;PURG;NKX2-5 |
RNA polymerase II regulatory region sequence-specific DNA binding | DMRT2;GLIS1;FOXC1;ZFP551;LMO2;MNT;ATF2;POU3F4;TFAP2E |
calmodulin binding | CALD1B;MKNK2A;SLC8A2;CAMK1G;EEF2K;EPB41;REM1;MARCKSL1;MARCKSA |
carboxypeptidase activity | AGBL4;NAALAD2;CPB1;NAALADL1;CPM;BLMH;CNDP1;CPA2;CTSA |
metallocarboxypeptidase activity | CPA6;AGTPBP1;CPA5;CPB1;CPA2;CPDB;AGBL5;AGBL2;CPO |
transcription corepressor activity | MYBBP1A;NFIL3;TRIM22;ATF7IP;RLIM;BRD7;TBL1X;HDAC7A;ZHX2 |
transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding | CHCHD3;CDX2;HES6;ZNF350;FERD3L;CSDA;FEZF2;ZC3H8;E2F7 |
zinc ion binding | ZCCHC17;HLTF;FAM90A1;EHMT2;RANBP2;GCM1;TCEA3;KDM2AA;ZMIZ2 |
AEBP1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with AEBP1 here. Most of them are supplied by our site. Hope this information will be useful for your research of AEBP1.
- Q&As
- Reviews
Q&As (10)
Ask a questionThe structural features or domains of Aebp1 protein, including the DNA-binding domain and regions involved in protein-protein interactions, are critical for its function and interaction with other molecules in cellular processes.
The tissue-specific expression patterns of Aebp1 protein vary across different organs and cell types. Factors regulating its expression levels include transcriptional control and signaling pathways.
Post-translational modifications, such as phosphorylation or acetylation, and regulatory factors modulate the activity or stability of Aebp1 protein, impacting its function and cellular responses.
Genetic variations or mutations in the Aebp1 gene may impact the expression or function of Aebp1 protein, potentially contributing to altered cellular processes and disease susceptibility.
Dysregulation or dysfunction of Aebp1 protein can disrupt cellular processes, such as adipogenesis or glucose metabolism, and contribute to the development of metabolic disorders or obesity-related diseases.
Aebp1 protein interacts with other proteins, such as transcription factors or co-regulators, forming protein complexes that influence gene expression and cellular processes.
Aebp1 protein exhibits DNA-binding activity, recognizing specific DNA sequences or binding motifs that regulate the expression of target genes involved in adipocyte differentiation and metabolic regulation.
The subcellular localization of Aebp1 protein is determined by specific mechanisms and targeting sequences, which facilitate its transport and localization to specific cellular compartments.
Experimental techniques such as gene expression analysis, chromatin immunoprecipitation, knockdown or overexpression studies, and functional assays have been employed to investigate the functional significance of Aebp1 protein.
Aebp1 protein plays a role in various cellular processes, including adipogenesis, glucose metabolism, and cell differentiation, by regulating target gene expression and interacting with signaling pathways.
Customer Reviews (3)
Write a reviewCharacterizing protein-protein interactions involved in immune checkpoint regulation.
Exploring protein-protein interactions involved in cell cycle checkpoints.
Determining protein-protein interaction interfaces using isothermal titration calorimetry.
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