acyl-binding

Ag85A Protein, Mycobacterium tuberculosis, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 44.6 kDa and the accession number is P9WQP2.

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. DBI Protein, Human, Recombinant (aa 2-104, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 15.7 kDa and the accession number is P07108.

The diazepam binding inhibitor (DBI), alternatively known as the acyl-CoA binding protein (ACBP), is involved in multiple biological actions. The polypeptide binds to the peripheral, or mitochondrial, benzodiazepine receptor and facilitates transport of cholesterol to the inner membrane to stimulate steroid synthesis. Through this action, DBI indirectly modulates gamma-aminobutyric acid (GABA)-mediated inhibitory neurotransmission. DBI can be postulated as a candidate gene for psychiatric phenotypes including anxiety, mood, and psychotic disorders. Diazepam Binding Inhibitor (DBI), also called acyl-CoA binding protein (ACBP), is a ubiquitously expressed protein originally identified based on its ability to displace diazepam from its binding site on the GABAA receptor. The mutant allele of the DBI was one of the risk factors for alcohol dependence as for the rs2276596 polymorphism.

Aspartoacylase 3, also known as ACY3, N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming), Acylase III, Aminoacylase-3, Aspartoacylase-2, Aspartoacylase-2, HCV core-binding protein 1 and ASPA2, is a member of the Aspartoacylase subfamily. ACY3 plays an important role in deacetylating mercapturic acids in kidney proximal tubules and acts on N-acetyl-aromatic amino acids.ACY3 is located in the cytoplasm of S2 and S3 proximal tubules and the apical domain of S1 proximal tubules. ACY3 protein is also expressed at low levels in stomach, testis, heart, brain, lung and liver, and may function as an HCV (Hepatitis C virus) core binding protein.

Ag85B Protein, Mycobacterium tuberculosis, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.2 kDa and the accession number is P9WQP0.

Ag85B Protein, Mycobacterium tuberculosis, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 32.7 kDa and the accession number is P9WQP0.

FbpB Protein, Mycobacterium kansasii, Recombinant (His & Myc & SUMO) is expressed in E. coli expression system with N-10xHis-SUMO and C-Myc tag. The predicted molecular weight is 50.6 kDa and the accession number is P21160.

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. ACB1 Protein, S. cerevisiae, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 12.1 kDa and the accession number is P31787.

ACBD7, acyl-CoA-binding domain-containing protein 7, is a small (1 Kd) protein that contains 1 ACB (acyl-CoA-binding) domain. The ACB domain consists of four alpha-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. The ligand is bound through specific interactions with residues on the protein, most notably several conserved positive charges that interact with the phosphate group on the adenosine-3'phosphate moiety, and the acyl chain is sandwiched between the hydrophobic surfaces of CoA and the protein. Other proteins containing an ACB domain include: ACBP (acyl-CoA-binding protein), ACBD3, ACBD4, ACBD5, ACBD6.

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. DBI Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 16.9 kDa and the accession number is P31786.

Ag85A Protein, Mycobacterium tuberculosis, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 34.1 kDa and the accession number is P9WQP2.

Ag85C Protein, Mycobacterium tuberculosis, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 36.1 kDa and the accession number is P9WQN8.

Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor. DBI Protein, Rat, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 16.9 kDa and the accession number is P11030.

Human acyl-coenzyme A binding domain-containing member 6 (ACBD6) is a modular protein that carries an acyl-CoA binding domain at its N terminus and two ankyrin motifs at its C terminus. In mammals, there are six members of the acyl-CoA binding domain-containing (ACBD) family, and their annotation is not uniform. All six ACBD proteins contain an ACB domain at the N terminus, but they do not share significant homology at the C-terminal region. ACBD6 is a 32 kDa protein that is predicted by sequence analysis to carry an ACB domain between residues 42 and 125 and two ANK motifs at its C terminus. This protein binds long-chain acyl-CoAs with a strong preference for unsaturated, C18:1-CoA and C20:4-CoA, over saturated, C16:0-CoA, acyl species. ACBD6 is not a ubiquitous protein, but it is expressed in hematopoietic tissues and appears to be restricted to primitive stem cells present in those tissues with functions in blood and vessel development. ACBD6 was detected in bone marrow, spleen, placenta, cord blood, circulating CD34+ progenitors, and embryonic-like stem cells derived from placenta. In placenta, the protein was only detected in CD34+ progenitor cells present in blood and CD31+ endothelial cells surrounding the blood vessels. These cells were also positive for the marker CD133, and they probably constitute hemangiogenic stem cells, precursors of both blood and vessels. We propose that human ACBD6 represents a cellular marker for primitive progenitor cells with functions in hematopoiesis and vascular endothelium development.

Group IIE secretory phospholipase A2, also known as GIIE sPLA2, sPLA2-IIE, Phosphatidylcholine 2-acylhydrolase 2E and PLA2G2E is a secreted protein that belongs to the phospholipase A2 family. Mammalian secretory phospholipase A2s (sPLA2s) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site. PLA2G2E catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids.

Transglutaminases (TGase) are a family of calcium-dependent acyl-transfer enzymes ubiquitously expressed in mammalian cells and responsible for catalyzing covalent cross-links between proteins or peptides. Transglutaminase 3 (TGM3) is a member of a family of Ca2+-dependent enzymes that catalyze covalent cross-linking reactions between proteins or peptides. TGM3 isoform is widely expressed and is important for epithelial barrier formation. It is a zymogen, requiring proteolysis for activity. Calcium-activated TGM3 can bind, hydrolyze, and is inhibited by GTP, despite lacking structural homology with other GTP binding proteins. TGM3 displays a diffuse cytoplasmic distribution in vitro consistent with its proposed role in the early phase of cornified cell envelope assembly in the cytoplasm. TGM3-driven specific isopeptide bonds between intermediate filaments and KAPs participate to the progressive scaffolding of the hair shaft. Additionally, TGM3 may be a novel prognostic biomarker for esophageal squamous cell carcinoma (ESCC).

Group XIIB secretory phospholipase A2-like protein, also known as Group XIII secretory phospholipase A2-like protein, GXIII sPLA2-like, sPLA2-GXIIB, GXIIB, PLA2G13 and PLA2G12B, is a secreted protein that belongs to the phospholipase A2 family. PLA2G12B / PLA2G13 is strongly expressed in liver, small intestine and kidney. Mammalian secretory phospholipase A2s ( sPLA2s ) form a family of structurally related enzymes that are involved in a variety of physiological and pathological processes via the release of arachidonic acid from membrane phospholipids or the binding to specific membrane receptors. Phospholipases A2 / PLA2 are enzymes that release fatty acids from the second carbon group of glycerol. This particular phospholipase specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Phospholipases A2 / PLA2 are commonly found in mammalian tissues as well as insect and snake venom. Venom from both snakes and insects is largely composed of melittin, which is a stimulant of Phospholipases A2 / PLA2. Due to the increased presence and activity of Phospholipases A2 / PLA2 resulting from a snake or insect bite, arachidonic acid is released from the phospholipid membrane disproportionately. As a result, inflammation and pain occur at the site.