You Searched For: Pentamethylcyclopentadienyliron+dicarbonyl+dimer


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Catalog Number: (10493-694)
Supplier: Bioss
Description: The Isocitrate dehydrogenase cytoplasmic enzyme is a homodimer of 416 residues that belongs to the isocitrate and isopropylmalate dehydrogenases family. IDHC catalyzes the third step of the citric acid cycle, which involves the oxidative decarboxylation of isocitrate, forming ?ketoglutarate and CO2 in a two step reaction. The first step involves the oxidation of isocitrate to the intermediate oxalosuccinate, while the second step involves the production of ?ketoglutarate. During this process, either NADH or NADPH is produced along with CO2. Ca2+ can bind to IDHC as a complex with isocitrate, acting as a competitive inhibitor of Mg2+. The IDHC enzyme is inactivated by phosphorylation at Ser-113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock. IDHC is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle.


Catalog Number: (10412-982)
Supplier: Bioss
Description: E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.


Catalog Number: (10412-920)
Supplier: Bioss
Description: E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.


Catalog Number: (10412-918)
Supplier: Bioss
Description: E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.


Catalog Number: (10412-426)
Supplier: Bioss
Description: E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.


Catalog Number: (10412-420)
Supplier: Bioss
Description: E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.


Catalog Number: (10083-228)
Supplier: Proteintech
Description: ATF2, also named as CREB2 and CREBP1, contains one bZIP domain and one C2H2-type zinc finger. It belongs to the bZIP family. ATF2 binds to the cAMP-responsive element(CRE), an octameric palindrome. It forms a homodimer or a heterodimer with c-Jun and stimulates CRE-dependent transcription. It is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus it may represent a class of sequence-specific factors that activate transcription by direct effects on chromatin components. ATF2 binds DNA as a dimer and can form a homodimer in the absence of DNA. It binds through its N-terminal region to UTF1 which acts as a coactivator of ATF2 transcriptional activity. This antibody is a rabbit polyclonal antibody raised against a peptide mapping within human ATF2.


Catalog Number: (10088-062)
Supplier: Proteintech
Description: The hemoglobin molecule is a tetramer consisting of two alpha- and two beta-globin-like chains. HBA1 (hemoglobin alpha chain) protein is a alpha-type chain of hemoglobin encoded by two independent genes (HBA1 and HBA2) whose coding sequences are identical. Two alpha chains coupled with two beta chains constitute the adult hemoglobin (HbA or α2β2). HBA1 is also the component of fetal hemoglobin (HbF or α2γ2). This antibody detects a major band around 14-16 kDa in the western blot analysis of heart tissue and K-562 cells. A higher band around 26-27 kDa can also be observed occasionally, which may represents the dimer form of HBA1 (20836851). The antibody is specific to HBA1and has no cross reaction to other globin member.


Catalog Number: (76107-958)
Supplier: Bioss
Description: The Isocitrate dehydrogenase cytoplasmic enzyme is a homodimer of 416 residues that belongs to the isocitrate and isopropylmalate dehydrogenases family. IDHC catalyzes the third step of the citric acid cycle, which involves the oxidative decarboxylation of isocitrate, forming ketoglutarate and CO₂ in a two step reaction. The first step involves the oxidation of isocitrate to the intermediate oxalosuccinate, while the second step involves the production of ketoglutarate. During this process, either NADH or NADPH is produced along with CO₂. Ca²⁺ can bind to IDHC as a complex with isocitrate, acting as a competitive inhibitor of Mg²⁺. The IDHC enzyme is inactivated by phosphorylation at Ser-113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock. IDHC is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle.


Catalog Number: (76077-872)
Supplier: Bioss
Description: The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described.


Catalog Number: (76080-204)
Supplier: Bioss
Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.


Catalog Number: (10351-674)
Supplier: Bioss
Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.


Catalog Number: (10413-430)
Supplier: Bioss
Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.


Catalog Number: (10230-040)
Supplier: Bioss
Description: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.


Catalog Number: (10351-668)
Supplier: Bioss
Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.


Catalog Number: (10748-750)
Supplier: Prosci
Description: ACVR1 Antibody: Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I and two type II receptors. Unlike ACVR1B and ACVR1C, ACVR1, also known as activin receptor-like kinase 2 (ALK2), can not transduce activin-mediated signaling, but will transduce BMP and Mullerian inhibiting substance (MIS) group signaling. It is thought that ACVR1 also inhibits activin signaling by blocking the binding of activin to its type II receptor. Recent studies indicate that genetic variation in ACVR1 is associated with polycystic ovary syndrome, suggesting that ACVR1 signaling contributes to disturbed folliculogenesis in these patients.


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