You Searched For: Cyclopentadienylmolybdenum+tricarbonyl+dimer

Catalog Number: (76101-360)

Supplier: Bioss

Description: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization.

Catalog Number: (76101-358)

Supplier: Bioss

Description: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization.

Catalog Number: (10388-480)

Supplier: Bioss

Description: MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.

Catalog Number: (10388-482)

Supplier: Bioss

Description: MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.

Catalog Number: (10388-484)

Supplier: Bioss

Description: MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.

Catalog Number: (10104-760)

Supplier: Prosci

Description: The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. The FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation.The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. As such, the FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation.

Catalog Number: (89359-422)

Supplier: Genetex

Description: The epidermal growth factor (EGF) family of receptor tyrosine kinases consists of four receptors, EGFR (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. Members of the EGFR family contain 3 domains: an extracellular domain that is involved in ligand binding and receptor dimerization, a single transmembrane domain and a cytoplasmic domain. EGF exerts its actions by binding to the EGFR, a 170 kDa protein. Activation of EGFR initiates diverse cellular pathwaysIn response to toxic environmental stimuli, or to EGF binding to the receptor, the EGFR forms homo- or heterodimers with other family members. Each dimeric receptor complex initiates a distinct signaling pathway by recruiting different Src homology 2 (SH2) containing effector proteins.

Catalog Number: (76079-874)

Supplier: Bioss

Description: ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Catalog Number: (10106-544)

Supplier: Prosci

Description: ARNTL is a general dimerization partner for a subset of the basic-helix-loop-helix (bHLH)-PER-ARNT-SIM (PAS) superfamily of transcriptional regulators.

Catalog Number: (89359-806)

Supplier: Genetex

Description: NF-kB is silenced in the cytoplasm by an inhibitory protein, IkB. Synthesis of IkBa is autoregulated. IkB proteins are phosphorylated by IkB kinase complex consisting of at least three proteins, IKK1/a, IKK2/b, and IKK3/g. External stimuli such as tumor necrosis factor or other cytokines results in phosphorylation and degradation of IkB releasing NF-kB dimers. NF-kB dimer subsequently translocates to the nucleus and activates target genes. Six members of IkB family members have been identified. One of the first genes induced following NF-kB activation is IkBa. Recently, two proteins, kB-Ras1 and kB-Ras2 have been identified. These two proteins interact with PEST domains of IkBa and IkBb and decrease their rate of degradation.

Supplier: Enzo Life Sciences

Description: The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Supplier: Biotium

Description: Eukaryotic histones are basic and water-soluble nuclear proteins. They form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation.

Catalog Number: (75794-436)

Supplier: Prosci

Description: Stem cell factor (SCF), also known as cKit ligand (KL), mast cell growth factor (MGF) and steel factor (SLF), is a widely expressed 28-40 kDa type I transmembrane glycoprotein. It promotes the survival, differentiation and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell and melanocyte progenitors. SCF is a primary growth and activation factor for mast cells and eosinophils. Noncovalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF R/cKit to trigger receptor dimerization and signaling. SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels.

Catalog Number: (75794-550)

Supplier: Prosci

Description: Stem cell factor (SCF), also known as cKit ligand (KL), mast cell growth factor (MGF), and steel factor (SLF), is a widely expressed 28-40 kDa type I transmembrane glycoprotein. It promotes the survival, differentiation, and mobilization of multiple cell types including myeloid, erythroid, megakaryocytic, lymphoid, germ cell, and melanocyte progenitors. SCF is a primary growth and activation factor for mast cells and eosinophils. Noncovalent dimers of transmembrane or soluble SCF interact with the receptor tyrosine kinase SCF R/cKit to trigger receptor dimerization and signaling. SCF assists in the recovery of cardiac function following myocardial infarction by increasing the number of cardiomyocytes and vascular channels.

Catalog Number: (10355-688)

Supplier: Bioss

Description: The Fos gene family consists of 4 members: FOS, FOSB, FOSL1, and FOSL2. These genes encode leucine zipper proteins that can dimerize with proteins of the JUN family, thereby forming the transcription factor complex AP-1. As such, the FOS proteins have been implicated as regulators of cell proliferation, differentiation, and transformation. [provided by RefSeq].

Catalog Number: (75794-162)

Supplier: Prosci

Description: NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.