Supplier: Bioss

Members of the WD repeat protein family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis and gene regulation. BRWD3 (bromodomain and WD repeat-containing protein 3) is a 1,802 amino acid protein expressed in fetal liver and most adult tissues. Existing as five alternatively spliced isoforms, BRWD3 contains two bromo domains, nine WD repeats and is thought to play a role in transcription by modifying chromatin. Mutations in the gene encoding BRWD3 are the cause of mental retardation X-linked type 93 (MRX93), which is also known as mental retardation X-linked with macrocephaly (XLMR). MRX93 is characterized by mild intellectual disability, macrocephaly, a prominent forehead and large cupped ears.

Supplier: Bioss

Members of the WD repeat protein family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis and gene regulation. BRWD3 (bromodomain and WD repeat-containing protein 3) is a 1802 amino acid protein expressed in fetal liver and most adult tissues. Existing as five alternatively spliced isoforms, BRWD3 contains two bromo domains, nine WD repeats and is thought to play a role in transcription by modifying chromatin. Mutations in the gene encoding BRWD3 are the cause of mental retardation X-linked type 93 (MRX93), which is also known as mental retardation X-linked with macrocephaly (XLMR). MRX93 is characterised by mild intellectual disability, macrocephaly, a prominent forehead and large cupped ears.

Supplier: ProSci Inc.

MITF (microphthalmia transcription factor) is a transcription factor that regulates the expression of genes with essential roles in cell differentiation, proliferation and survival. Binds to symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoters of target genes, such as BCL2 and tyrosinase (TYR). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium. [UniProt].

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialised form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Bioss

MEGF10 is a 1,140 amino acid protein encoded by the human gene MEGF10. MEGF10 belongs to the MEGF family and contains fifteen EGF-like domains and one EMI domain. The engulfment of dying cells is a specialized form of phagocytosis that is highly conserved across evolution and is mediated by the concerted action of several molecules. MEGF10 is an engulfment receptor protein that localizes to the plasma membrane in a punctuated pattern. The MEGF10 protein shares structural similarities with nematode engulfment receptor cell death abnormal-1 (CED-1). MEGF10 function is modulated by the ATP binding cassette transporter ABCA1, which is an ortholog to CED-7. It is expressed at the cell surface in clusters around cell corpses during engulfment, and during the engulfment of apoptotic thymocytes is recruited to the bottom of the forming phagocytic cup.

Supplier: Biosensis

FUNCTION: Required for autophagy. Conjugates to ATG12 and associates with isolation membrane to form cup-shaped isolation membrane and autophagosome. The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. FUNCTION: May play an important role in the apoptotic process, possibly within the modified cytoskeleton. Its expression is a relatively late event in the apoptotic process, occurring downstream of caspase activity. SUBCELLULAR LOCATION: Cytoplasm. Colocalizes with nonmuscle actin. ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells. INDUCTION: By apoptotic stimuli. PTM: Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane. SIMILARITY: Belongs to the ATG5 family.

Supplier: VWR Collection

Designed to hold multiple test tubes, test tube racks, vials or cylinders. Vortexing action is created by securing the top of the vessel in place while allowing the bottom to move freely in a defined orbit. Two stainless steel posts hold the support plate securely in place for quiet, rattle-free mixing. The support plate is easily adjustable by loosening knobs and moving the support plate up and down. The circular groove around the top of the taller post allows the support plate to be swung away from the tray for easy removal of samples. The suction cup feet dampen motion and prevent the unit from moving along the work bench. Made from stainless steel with corrosion resistant paint. Equipped with a powerful, permanent magnet motor with sealed ball bearings. Motor is rated for continuous duty.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organisation and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organisation and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: Bioss

Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those GTPases (By similarity). Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3-mediated adhesion. Does not affect integrin beta-1-mediated adhesion.

Supplier: AbFrontier

14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(β, γ, ε, η, ζ, σ and τ/θ) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most 14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.

Supplier: AbFrontier

14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(β, γ, ε, η, ζ, σ and τ/θ) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most 14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.

Supplier: AbFrontier

14-3-3, a family of acidic and soluble proteins, highly conserved in amino acid sequences from yeast to mammals, is expressed in all eukaryotic cells. Seven isoforms(beta, gamma, epsilon, eta, zeta, sigma and tau/phi) encoded by seven distinct genes are identified in mammals and forms homo- and hetero- dimeric cup-shaped structures. As 14-3-3 is interacted with more than 100 binding partners, it regulates key proteins involved in various biological processes such as signal trans-duction, cell cycle, transcriptional control, cell proliferation, apoptosis, and ion channel physiology. Most  14-3-3 requires phosphorylation of serine or threonine residues in the target sequence. This protein is abundantly expressed in the brain and has been detected in the cerebrospinal fluid of patients with different neurological disorders.