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Major Vault Protein (MVP) [1032]
Description Recognizes a protein of 104kDa-110kDa, characterized as major vault protein (MVP). Vaults are large ribonucleoprotein particles (RNPs) present in all eukaryotic cells. They have a complex morphology, including several small molecules of RNA, but a single protein species. The MVP accounts for >70% of their mass. Their shape is reminiscent of the nucleopore central plug. Treatment of cells with estradiol increases the amount of MVP in nuclear extract. The hormone-dependent interaction of vaults with ER is prevented in vitro by sodium molybdate. Antibodies to estrogen, progesterone and glucocorticoid receptors are able to co-immunoprecipitate the MVP. MVP is overexpressed in many neoplastic tissues and cell lines. Expression of MVP predicts a poor response to chemotherapy. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Rat -
MAP3K3/MEKK3 (Mitogen-Activated Protein Kinase Kinase Kinase 3) [5C1]
Description MEKKs (Mitogen activated protein kinase kinase kinases) are serine-threonine kinases that act as the first tier of cellular MAP kinase pathways by activation of MAP/ERK kinases, or MEKs. Many enzymes with MEKK activity have been identified, including MEKK1-4, Raf, MLK3, TAK, and DLK. MEKKs generally display little similarity outside of their catalytic kinase domains. MEKK1-4 are nearly 50% identical within their catalytic domains, and are known to regulate Erk, Jnk, and p38 MAP kinase pathways. MEKK2 and MEKK3 bind MEK5 via conserved PB1 domains, leading to downstream activation of Erk5. (Shipping Cost: €200.00) Host Rabbit Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat -
MCM2 [MD32R]
Description Minichromosome maintenance protein 2 (MCM2), also known as DNA replication licensing factor MCM2, is a member of the MCM family that regulates mammalian DNA replication. This family is composed of six related subunits, called the hexameric MCM2-7 complex, that are conserved in all eukaryotes. It functions as a replicative helicase, the molecular motor that both unwinds duplex DNA and powers fork progression during DNA replication. MCM2 acts as a factor to license DNA for one and only one round of replication per cell cycle. In the cell cycle, levels of the MCM family gradually increase in a variable manner from G0 into the G1/S phase. In the G0 stage, the amounts of MCM2 and MCM5 proteins are much lower than that of MCM7 and MCM3 proteins, so some of them participate in cell cycle regulation. MCM2 is localized in the nucleus throughout interphase. It is required for entry into the S phase and cell division. Anti-MCM2 labels proliferating cells in normal and tumor tissue. MCM2 has been Host Rabbit Application Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat, Monkey -
MCM2 [MD32R]
Description Minichromosome maintenance protein 2 (MCM2), also known as DNA replication licensing factor MCM2, is a member of the MCM family that regulates mammalian DNA replication. This family is composed of six related subunits, called the hexameric MCM2-7 complex, that are conserved in all eukaryotes. It functions as a replicative helicase, the molecular motor that both unwinds duplex DNA and powers fork progression during DNA replication. MCM2 acts as a factor to license DNA for one and only one round of replication per cell cycle. In the cell cycle, levels of the MCM family gradually increase in a variable manner from G0 into the G1/S phase. In the G0 stage, the amounts of MCM2 and MCM5 proteins are much lower than that of MCM7 and MCM3 proteins, so some of them participate in cell cycle regulation. MCM2 is localized in the nucleus throughout interphase. It is required for entry into the S phase and cell division. Anti-MCM2 labels proliferating cells in normal and tumor tissue. MCM2 has been Host Rabbit Application Chromatin Immunoprecipitation (ChIP), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat, Monkey -
MDM2 [SMP14]
Description p53 is the most commonly mutated gene in human cancer identified to date. Expression of p53 leads to inhibition of cell growth by preventing progression of cells from G1 to S phase of the cell cycle. Most importantly, p53 functions to cause arrest of cells in the G1 phase of the cell cycle following any exposure of cells to DNAdamaging agents. The MDM2 (murine double minute-2) protein was initially identified as an oncogene in a murine transformation system. MDM2 functions to bind p53 and block p53-mediated transactivation of cotransfected reporter constructs. The MDM2 gene is amplified in a high percentage of human sarcomas that retain wt p53 and tumor cells that overexpress MDM2 can tolerate high levels of p53 expression. These findings argue that MDM2 overexpression represents at least one mechanism by which p53 function can be abrogated during tumorigenesis. MDM2 is useful in differentiating liposarcoma from other types of sarcomas. (Shipping Cost: €200.00) Host Mouse Application Immunohistochemistry (IHC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
MDM2 [SMP14]
Description p53 is the most commonly mutated gene in human cancer identified to date. Expression of p53 leads to inhibition of cell growth by preventing progression of cells from G1 to S phase of the cell cycle. Most importantly, p53 functions to cause arrest of cells in the G1 phase of the cell cycle following any exposure of cells to DNAdamaging agents. The MDM2 (murine double minute-2) protein was initially identified as an oncogene in a murine transformation system. MDM2 functions to bind p53 and block p53-mediated transactivation of cotransfected reporter constructs. The MDM2 gene is amplified in a high percentage of human sarcomas that retain wt p53 and tumor cells that overexpress MDM2 can tolerate high levels of p53 expression. These findings argue that MDM2 overexpression represents at least one mechanism by which p53 function can be abrogated during tumorigenesis. MDM2 is useful in differentiating liposarcoma from other types of sarcomas. (Shipping Cost: €200.00) Host Mouse Application Immunohistochemistry (IHC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Moesin [MSN491]
Description The ezrin, radixin and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling and microvilli formation. ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers. Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin), which disrupts their amino- and carboxy-terminal association, may play a key role in modulating the conformation and function of ERM proteins. Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogeneinduced transformation. Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Rat -
Moesin [MSN491]
Description The ezrin, radixin and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling and microvilli formation. ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers. Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin), which disrupts their amino- and carboxy-terminal association, may play a key role in modulating the conformation and function of ERM proteins. Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogeneinduced transformation. Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Rat -
MyoD1 (Rhabdomyosarcoma Marker) [5.8A]
Description Recognizes a phosphor-protein of 45kDa, identified as MyoD1. The epitope of this antibody maps between amino acid 180-189 in the C-terminal of mouse MyoD1 protein. It does not cross react with myogenin, Myf5, or Myf6. Antibody to MyoD1 labels the nuclei of myoblasts in developing muscle tissues. MyoD1 is not detected in normal adult tissue, but is highly expressed in the tumor cell nuclei of rhabdomyosarcomas. Occasionally nuclear expression of MyoD1 is seen in ectomesenchymoma and a subset of Wilm s tumors. Weak cytoplasmic staining is observed in several non-muscle tissues, including glandular epithelium and also in rhabdomyosarcomas, neuroblastomas, Ewing s sarcomas and alveolar soft part sarcomas. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat, Chicken -
Myosin Skeletal Heavy Chain Fast/MYH1 [MY-32]
Description Myosin, a 480kD protein that interacts with actin in muscle and non muscle cells, is composed of 2 identical heavy chains (about 200kD each) and 4 light chains (about 20kD each). Conventional myosin molecules consist of two major regions: tail (rod) and globular heads; they aggregate into filaments through the tail region and interact with actin and with adenosine triphosphate (ATP) through the head region. Multiple forms of myosin heavy chains exist in skeletal, smooth and cardiac muscle and in non-muscle tissues. A spectrum of skeletal muscle fiber types is found in adult skeletal muscles. The two major skeletal muscle fiber types are type I (slow-twitch) and type II (fast-twitch). Skeletal muscle type II fibers can be further subdivided into types IIa (fast red) and IIb (fast white). (Shipping Cost: €200.00) Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat, Rabbit, Chicken, Guinea Pig, Bovine