You Searched For: Pentamethylcyclopentadienyliron+dicarbonyl+dimer

Catalog Number: (10375-472)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

Supplier: Prosci

Description: GDNF is a disulfide-linked homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRalpha (alpha1-alpha4) receptors. GDNF specifically promotes dopamine uptake and survival and morphological differentiation of midbrain neurons. Using Parkinson's disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. Both the functional human and rat GDNF ligand is a disulfide-linked homodimer, of two 15 kDa polypeptide chains called monomers. The functional murine GDNF ligand is a disulfide-linked homodimer, of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, one of which (Cys 101) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.

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: (10490-494)

Supplier: Bioss

Description: Hemostasis following tissue injury involves the deployment of essential plasma procoagulants (Prothrombin and Factors X, IX, V and VIII), which are involved in a blood coagulation cascade that leads to the formation of insoluble Fibrin clots and the promotion of platelet aggregation. Coagulation Factor X (Stuart Prower factor, FX, F10) is a vitamin K-dependent, single chain serine protease that is synthesized in the liver and circulates as an inactive precursor. The mature form of Factor X (Factor X A) is generated by Factor IX A- or Factor VII A-mediated cleavage at the tripeptide sequence, Arg-Lys-Arg, to yield a disulfide linked dimer. Together with the cofactor Factor V A and Ca2+ on the surface of platelets or endothelial cells, Factor X A coordinates as part of the prothrombinase complex, which mediates proteolysis of Prothrombin into active Thrombin. Mutations at the Factor X locus resulting in Factor X deficiencies can contribute to hemorrhagic diathesis.

Catalog Number: (10495-796)

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: (10481-088)

Supplier: Bioss

Description: 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: Biotium

Description: CD309, also known as VEGFR2, KDR3, and Flk-1 (mouse), is a type I transmembrane glycoprotein. It is a member of the CSF-1/PDGF receptor family of type III tyrosine kinase receptors. Human VEGFR2 is mainly expressed by endothelial cells, embryonic tissues, and megakaryocytes. It plays an important role in the regulation of angiogenesis, vasculogenesis, and vascular permeability. The ligands of VEGFR2 include VEGF-A, VEGF-C, VEGF-D, and VEGF splice isoforms. Ligation of VEGFR2 with its ligands results in the receptor dimerization and auto-phosphorylation, stimulating endothelial cell proliferation and migration.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.

Catalog Number: (10451-836)

Supplier: Bioss

Description: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor.

Catalog Number: (10749-636)

Supplier: Prosci

Description: SIGIRR Antibody: SIGIRR is a member of the Toll-like receptor-interleukin 1 receptor superfamily. Members of this family are defined by the presence of an intracellular Toll-IL-1R (TIR) domain. The Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SIGIRR was originally identified through database analysis and was shown to have only one Ig domain as opposed to the normal three Ig folds seen in the TIR family. Similar to ST2, another TIR family member, it has been shown to negatively regulate IL-1 receptor and Toll-like receptor signaling. However, SIGIRR inhibits TLR-IL-1R signaling by dimerizing with TLR4, TLR5, TLR9, and IL-1R. It also associates with the down-stream TLR signaling proteins IRAK and TRAF6 in an IL-1-dependent fashion.

Supplier: Peprotech

Description: GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRalpha (alpha1-alpha4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson's disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional rat GDNF ligand is a disulfide-linked homodimer consisting of two 15 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine-knot configuration. The calculated molecular weight of Recombinant Rat GDNF is 30.0 kDa.

Supplier: Peprotech

Description: GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRα (α1-α4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.

Catalog Number: (76084-594)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

Catalog Number: (10375-476)

Supplier: Bioss

Description: Talin, a multifunctional constituent of cell-substratum attachment sites, is a high molecular weight protein (225-270 kDa) found in variety of tissues and cell types. It is localized at a subset of adherens junctions, specialized cell-cell and cell-matrix associations that are characterized by the presence of filamentous actin at the cytoplasmic face of the junctional complex. In cultured cells, talin is absent from cell-cell junctions and found predominantly at adhesion plaques and in fibrillar streaks underlying cell surface fibronectin. Talin interacts with at least two other proteins that are localized at adhesion plaques, vinculin and integrin. Talin and vinculin have been shown to interact with each other and both have been proposed to be involved in generating the transmembrane connection, between the extracellular matrix and the cytoskeleton, that occurs at adhesion plaques. At physiological ionic strength, talin is an elongate, flexible, monomeric protein with the ability to self-associate into dimers at higher protein concentrations.

Catalog Number: (76100-950)

Supplier: Bioss

Description: Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways.

Catalog Number: (10083-746)

Supplier: Proteintech

Description: RNF17 also termed as ring finger protein 17 is a 1623 amino acid protein, which contains 1 ring type zinc finger and 4 tudor domains. RNF17 is specifically expressed in testis. The RING finger motif presents in many ubiquitin E3 ligases. RNF17 interacts with all four members of the Mad family (Mad1, Mxi1, Mad3 and Mad4), which are basic-helix-loop-helix-leucine zipper transcription factors of the Myc oncoprotein network. RNF17 is component of the tectonic-like complex, which is required for ciliogenesis and sonic hedgehog/SHH signaling. RNF17 is able to form dimers or polymers both in vitro and in vivo, indicating that it may play a role in the assembly of RNF17 granules. RNF17 encodes a novel key regulator of spermiogenesis.

Catalog Number: (76116-352)

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 CASP10. 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. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.