You Searched For: Cyclopentadienylmolybdenum+tricarbonyl+dimer

Catalog Number: (10493-690)

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: (89417-268)

Supplier: Prosci

Description: INCA1 Antibody: INCA1 was isolated through a yeast triple hybrid approach to identify interaction partners of the cyclin A1-CDK2 heterodimer. INCA1 is evolutionarily conserved and has no homology to any known proteins. Like Cyclin A1, INCA1 is highly expressed in testis with highest levels observed at various points of testis maturation. It has been suggested that the complex of INCA1 and the cyclinA1-CDK2 dimer plays a role in several signaling pathways important for cell cycle control and meiosis. Recent experiments have shown that INCA1 also interacts with the testis protein RSB-66 and this interaction takes place in the cytoplasm.

Catalog Number: (10493-924)

Supplier: Bioss

Description: MuRF1, is a nuclear protein that interacts with SMT3b and the large myofibrillar protein Titin. In muscle cells, MuRF2 (RFN29) regulates gene expression and protein turnover. It localizes to the cytoplasm, but under atrophic conditions it is detected in the nucleus. MuRF2 can form oligomers with various other proteins, including Titin and Myosin. MuRF3, also designated tripartite motif-containing 54 (TRIM54) or ring finger protein 30 (RNF30), interacts with tubulin and stabilizes microtubules duing myotube formation. It is a cytoplasmic protein the localizes to the Z-lines in skeletal muscles, while MuRF2 localizes to the sarcomeric M-band in cardiomyocytes. MuRF3 shares 77% and 65% sequence identity with MuRF1 and MuRF2, respectively. MuRF1-3 share a conserved N-terminal RING domain and zinc-binding B-box motif, and two coiled-coil dimerization motif boxes, in their central regions.

Catalog Number: (10090-914)

Supplier: Proteintech

Description: NQO1, also named as DIA4, NMOR1, DTD and QR1, belongs to the NAD(P)H dehydrogenase (quinone) family. This enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. It is known to be involved in benzene metabolism. In human studies of ozone exposure, polymorphisms in oxidative stress genes (NQO1, GSTM1, GSTP1) modify respiratory symptoms, lung function, biomarkers and risk of asthma. This antibody recognizes all the three isoforms (26-27 kDa and 31 kDa) of NQO1 and the homo-dimer form (66-70 kDa) of NQO1.

Catalog Number: (10782-736)

Supplier: Biosensis

Description: FUNCTION: Functions as an E1 enzyme essential for multisubstrates such as GABARAPL1 and ATG12. Forms intermediate conjugates with GABARAPL1 (GABARAPL2, GABARAP or MAP1ALC3). Formation of the final GABARAPL1-PE conjugate is essential for autophagy. SUBUNIT: Homodimer (By similarity). Interacts with ATG3 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. SUBCELLULAR LOCATION: Cytoplasm (Probable). ALTERNATIVE PRODUCTS: 2 named isoforms produced by alternative splicing. TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver, lymph nodes and bone marrow. DOMAIN: The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12. SIMILARITY: Belongs to the ATG7 family. In yeast, ATG7 appears to be required for fusion of peroxisomal and vaculuolar membranes.

Catalog Number: (10098-330)

Supplier: Prosci

Description: Interleukin 31 (IL-31) is a recently discovered T-cell cytokine closely related to IL-6 type cytokines and is preferentially produced by T helper type 2 cells. IL-31 activity is mediated through the ligand-induced oligomerization of a dimeric receptor complex containing IL-31 receptor A and oncostatin M receptor. In response to IL-31 binding, these proteins activate the JAK/STAT and the AKT signaling pathways. RNA levels of IL-31 receptor A and oncostatin M receptor are induced in activated monocytes but are expressed constitutively in epithelial cells. IL-31, when overexpressed in transgenic mice, results in the development of pruritis, alopecia and skin lesions, and in humans may result in atopic dermatitis, suggesting that IL-31 may represent a novel target for antipruritic drug development.

Supplier: Biotium

Description: This antibody recognizes an oncofetal glycoprotein with a single chain of 70 kDa, which is identified as alpha fetoprotein (AFP). This MAb is highly specific to AFP and shows no cross-reaction with other oncofetal antigens or serum albumin. The yolk sac and the liver produce AFP during fetal life. AFP expression in adults is often associated with hepatoma or teratoma. However, hereditary persistence of alpha-fetoprotein may also be found in individuals with no obvious pathology. The protein is thought to be the fetal counterpart of serum albumin, and the AFP and albumin genes are present in tandem in the same transcriptional orientation on chromosome 4. AFP is found in monomeric as well as dimeric and trimeric forms, and binds copper, nickel, fatty acids and bilirubin. The level of AFP in amniotic fluid is used to measure renal loss of protein to screen for spinal bifida and anencephaly.

Catalog Number: (75794-206)

Supplier: Prosci

Description: CD27 (TNFRSF7) is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD70 on lymphocytes and dendritic cells. The CD27-CD70 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B cell differentiation, activation and immunoglobulin synthesis. The CD27 receptor transduces signals and subsequently leads to the activation of NF-kappaB and MAPK8/JNK, mediated by the adaptor proteins TRAF2 and TRAF5. In addition, the proapoptotic protein SIVA is capable of binding the cytoplasmic tail of CD27 and exerts action in the process of apoptosis.

Catalog Number: (10668-284)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

Catalog Number: (10668-282)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

Catalog Number: (10412-428)

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: (10413-400)

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: (10412-422)

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: (75788-818)

Supplier: Prosci

Description: Human beta -Nerve Growth Factor ( beta -NGF) was initially isolated in the mouse submandibular gland. It is composed of three non-covalently linked subunits alpha, beta , and gamma ; it exhibits all the biological activities ascribed to NGF. It is structurally related to BDNF, NT-3 and NT-4 and belongs to the cysteine-knot family of growth factors that assume stable dimeric structures. beta -NGF is a neurotrophic factor that signals through its receptor beta -NGF, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems. beta -NGF also acts as a growth and differentiation factor for B lymphocytes and enhances B-cell survival. These results suggest that beta -NGF is a pleiotropic cytokine, which in addition to its neurotropic activities may have an important role in the regulation of the immune system. Human beta -NGF shares 90% sequence similarity with mouse protein and shows cross-species reactivity.

Catalog Number: (89158-460)

Supplier: Enzo Life Sciences

Description: Fibronectins are high molecular weight, disulphide-linked, dimeric cell adhesion glycoproteins found in basement membranes and in the interstitial connective tissue matrix. A single fibronectin gene is subject to alternative splicing in a cell-type-, development- and age-regulated manner which gives rise to multiple molecular forms. In addition to their prominent role in adhesion, fibronectins have been reported to mediate various aspects of cellular interaction, including migration during development and wound-healing, haemostasis, and the regulation of cell growth and differentiation. Cellular fibronectins (cFn) are found in low amounts in normal human plasma and tissues, but they are abundant in the plasma of carcinoma patients and in the stroma of various carcinomas. In contrast, a soluble form of fibronectin produced by hepatocytes is readily detectable in plasma and becomes deposited in pericellular matrices and within tissues. This form of fibronectin, referred to as ‘plasma fibronectin’ (pFn), differs from cFn by the absence of an amino acid sequence, known as extra domain A1.

Catalog Number: (77438-364)

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.