"Virginiamycin+complex&amp"

Supplier: Bioss

Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

Supplier: Bioss

The BTB (Broad-Complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and Zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. ZBTB1 (zinc finger and BTB domain containing 1), also known as KIAA0997, is a 713 amino acid nuclear protein that contains one BTB (POZ) domain and 8 C2H2-type zinc fingers. ZBTB2 is a 514 amino acid nuclear protein that contains one BTB (POZ) domain and 4 C2H2-type zinc fingers. ZBTB25, also known as ZNF46 or KUP, is a 435 amino acid nuclear protein that is expressed mainly in hematopoietic cells and testis and contains one BTB (POZ) domain and 2 C2H2-type zinc fingers.

Supplier: Bioss

The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system (SCS). The SCS contains over 30 glycoproteins that influence physiological mechanisms of the body in response to immune complex (the classical pathway), carbohydrate (the lectin pathway) or bacterial (alternative pathway) initiation. C1q binding protein (C1QBP), also designated gC1q-R, p32 (p33) or HABP1 (hyaluronan-binding protein 1), is known to bind the globular heads of C1q molecules and inhibit C1 activation. C1QBP has been described as a complement receptor for C1q on B cells, neutrophils and mast cells. The C1QBP protein may form homodimers. C1QBP is expressed in vascular endothelial cells and has been found to be a multifunctional protein interacting with elements of complement, coagulation and kinin systems. In addition, C1QBP is a subunit of pre-mRNA splicing factor SF2/ASF.

Supplier: Bioss

The regulated oscillation of protein expression is an essential mechanism of cell cycle control. The SCF class of E3 ubiquitin ligases is involved in this process by targeting cell cycle regulatory proteins for degradation by the proteasome, with the F-box subunit of the SCF specifically recruiting a given substrate to the SCF core. NIPA (nuclear interaction partner of ALK) is a human F-box-containing protein that defines an SCF-type E3 ligase (SCFNIPA) controlling mitotic entry. Assembly of this SCF complex is regulated by cell-cycle-dependent phosphorylation of NIPA, which restricts substrate ubiquitination activity to interphase. Nuclear cyclin B1 is a substrate of SCFNIPA. Inactivation of NIPA by RNAi results in nuclear accumulation of cyclin B1 in interphase, activation of cyclin B1-Cdk1 kinase activity, and premature mitotic entry. Thus, SCFNIPA-based ubiquitination may regulate S-phase completion and mitotic entry in the mammalian cell cycle.

Supplier: Bioss

The BTB (Broad-Complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and Zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. ZBTB1 (zinc finger and BTB domain containing 1), also known as KIAA0997, is a 713 amino acid nuclear protein that contains one BTB (POZ) domain and 8 C2H2-type zinc fingers. ZBTB2 is a 514 amino acid nuclear protein that contains one BTB (POZ) domain and 4 C2H2-type zinc fingers. ZBTB25, also known as ZNF46 or KUP, is a 435 amino acid nuclear protein that is expressed mainly in hematopoietic cells and testis and contains one BTB (POZ) domain and 2 C2H2-type zinc fingers.

Supplier: Bioss

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.

Supplier: Bioss

This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009].

Supplier: Bioss

The BTB (Broad-Complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and Zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. ZBTB1 (zinc finger and BTB domain containing 1), also known as KIAA0997, is a 713 amino acid nuclear protein that contains one BTB (POZ) domain and 8 C2H2-type zinc fingers. ZBTB2 is a 514 amino acid nuclear protein that contains one BTB (POZ) domain and 4 C2H2-type zinc fingers. ZBTB25, also known as ZNF46 or KUP, is a 435 amino acid nuclear protein that is expressed mainly in hematopoietic cells and testis and contains one BTB (POZ) domain and 2 C2H2-type zinc fingers.

Supplier: Bioss

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.

Supplier: Bioss

Cyclin dependent kinase 5 (Cdk5) is a key regulator of cell cycle progression in neuronal differentiation that physically associates with and is activated by the neuron-specific protein p35. CDK5RAP1 (CDK5 regulatory subunit-associated protein 1) specifically inhibits Cdk5 activation by p35 through formation of a dimer that inhibits kinase activity. CDK5RAP2, also known as Centrosome-associated protein 215, is a 1893 amino acid centrosomal protein that regulates activity of CDK5 through complex formation with CDK5RAP1. Expressed in placenta, liver, pancreas, heart, skeletal muscle, lung, brain and kidney, CDK5RAP2 associates with centrosomes throughout the cell cycle. Mutations in the gene encoding CDK5RAP2 results in primary microencephaly autosomal recessive type 3, which is characterized by markedly reduced head size, brain weight and significant neurological deficits. There are four isoforms of CDK5RAP2 that are produced as a result of alternative splicing events.

Supplier: Bioss

Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects golgi structure, and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

Supplier: Bioss

The BTB (Broad-Complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and Zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. ZBTB1 (zinc finger and BTB domain containing 1), also known as KIAA0997, is a 713 amino acid nuclear protein that contains one BTB (POZ) domain and 8 C2H2-type zinc fingers. ZBTB2 is a 514 amino acid nuclear protein that contains one BTB (POZ) domain and 4 C2H2-type zinc fingers. ZBTB25, also known as ZNF46 or KUP, is a 435 amino acid nuclear protein that is expressed mainly in hematopoietic cells and testis and contains one BTB (POZ) domain and 2 C2H2-type zinc fingers.

Supplier: Bioss

This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

Supplier: Bioss

This gene encodes a 105 kD protein which can undergo cotranslational processing by the 26S proteasome to produce a 50 kD protein. The 105 kD protein is a Rel protein-specific transcription inhibitor and the 50 kD protein is a DNA binding subunit of the NF-kappa-B (NFKB) protein complex. NFKB is a transcription regulator that is activated by various intra- and extra-cellular stimuli such as cytokines, oxidant-free radicals, ultraviolet irradiation, and bacterial or viral products. Activated NFKB translocates into the nucleus and stimulates the expression of genes involved in a wide variety of biological functions. Inappropriate activation of NFKB has been associated with a number of inflammatory diseases while persistent inhibition of NFKB leads to inappropriate immune cell development or delayed cell growth. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009].

Supplier: Bioss

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires ATP-dependent activation of the Ub C-terminus and assembly of multi-Ub chains by a Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2U (ubiquitin-conjugating enzyme E2U) is a 321 amino acid E2 ubiquitin conjugating enzyme that catalyzes the covalent attachment of ubiquitin to other proteins. Existing as two alternatively spliced isoforms, UBE2U is encoded by a gene located on human chromosome 1, which spans 260 million base pairs, contains over 3,000 genes and comprises nearly 8% of the human genome.