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Histone H3 Tri-Methyl Lys27/H3K27Me3 [MD48R]
Description The Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4). In contrast, a more diverse set of histone lysine methyltransferases have been identified, all but one of which contain a conserved catalytic SET domain origin Host Rabbit Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Monkey -
HLA-A (MHC I) [C6]
Description HLA-A, with HLA-B and HLA-C, belongs to major histocompatibility complex (MHC) class I antigens and expresses constitutively on all nucleated cells. MHC class I antigens play a role in class I MHC-associated antigen presentation, inhibition of NK cell cytotoxicity, tumor surveillance, and tissue allotransplantation. This antibody is useful for HLA molecular typing of peripheral blood leukocytes as well as a large number of leukemic cell lines. It reacts with an intralocus determinant present on a limited number of HLA-A locus-encoded gene products (HLA-A2, -A3, -A28, -A29, -A30, -A31 and -Aw33). Its epitope maps between aa65-to-aa80 of the 1 domain of the HLA-A. This antibody recognizes an intralocus determinant present on a limited number of HLA-A locus-encoded gene products (HLA-A2, -A3, A28, -A29, -A30, -A31 and -Aw33). Furthermore, by testing its reactivity with HLA-A2 natural variants and mutants, the importance of amino acid residues 79 and/or 80 of the α1 domain was demonstrated Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
HPV 16 [CAMVIR-1]
Description The antibody reacts with a 56 kDa protein in cells infected with L1-vaccinia virus, the protein being present in a predominantly nuclear location. The antibody reacts very strongly with biopsy specimins containing HPV-16 or -33; very weak reactions were occasionally observed with biopsy specimens or smears containing HPV-6 or HPV-11. Cross-reacts with HPV37.L1 is a major capsid protein of type 16 human papilloma virus. Infection with specific types of HPV has been associated with an increased risk of developing cervical neoplasia. HPV types 6 and 11 have been associated with relatively benign diseases such as genital warts but types 16 and 18 are strongly associated with cervical, vaginal, and vulvar malignancies. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
HPV 16 [CAMVIR-1]
Description The antibody reacts with a 56 kDa protein in cells infected with L1-vaccinia virus, the protein being present in a predominantly nuclear location. The antibody reacts very strongly with biopsy specimins containing HPV-16 or -33; very weak reactions were occasionally observed with biopsy specimens or smears containing HPV-6 or HPV-11. Cross-reacts with HPV37.L1 is a major capsid protein of type 16 human papilloma virus. Infection with specific types of HPV has been associated with an increased risk of developing cervical neoplasia. HPV types 6 and 11 have been associated with relatively benign diseases such as genital warts but types 16 and 18 are strongly associated with cervical, vaginal, and vulvar malignancies. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
IDH1-R132H [IHC132]
Description A member of this family, IDH1, is the human cytoplasmic NADP-specific enzyme. Its subcellular localization was shown to be in both peroxisomes and the cytoplasm. Although the function and structure of the protein has been well characterized, mutations in the gene have only recently been implicated in cancer after a genome-wide mutation study of giloblastomas, acute myeloid leukemias (AML) and chondrosarcomas. Mutations in IDH1 are specific to Arg132 (R132) and endow them with the function of generating 2-hydroxyglutarate (2HG) instead of aKG. This product alters gene transcription through effects on DNA and histone methylation. Several IDH1 mutations exist, including R132H, R132C, R132S, R132G and R132L. Each may result in different tumor type with varied malignant progression. The most frequent known mutation (>90%) is the alteration of arginine to histidine (R132H). Hence, antibodies that recognize the IDH1R132H mutation can be useful for the detection of mutation-bearing tumors like Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
IDH1-R132H [IHC132]
Description A member of this family, IDH1, is the human cytoplasmic NADP-specific enzyme. Its subcellular localization was shown to be in both peroxisomes and the cytoplasm. Although the function and structure of the protein has been well characterized, mutations in the gene have only recently been implicated in cancer after a genome-wide mutation study of giloblastomas, acute myeloid leukemias (AML) and chondrosarcomas. Mutations in IDH1 are specific to Arg132 (R132) and endow them with the function of generating 2-hydroxyglutarate (2HG) instead of aKG. This product alters gene transcription through effects on DNA and histone methylation. Several IDH1 mutations exist, including R132H, R132C, R132S, R132G and R132L. Each may result in different tumor type with varied malignant progression. The most frequent known mutation (>90%) is the alteration of arginine to histidine (R132H). Hence, antibodies that recognize the IDH1R132H mutation can be useful for the detection of mutation-bearing tumors like Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
IPO-38 (Proliferation Marker) [IPO38]
Description Recognizes a protein of 14-16kDa, which is a novel nuclear antigen of proliferating cells. IPO-38 antigen is present in the nuclei of proliferating cells such as Hodgkin s disease and non-Hodgkin s lymphomas, different forms of leukemias, breast and colorectal carcinomas, and PHA-stimulated lymphocytes. It is not expressed in the cells of non-stimulated lymphocytes and granulocytes. IPO-38 may be a useful marker of cell proliferation during monitoring of tumor progression. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Laminin Alpha 2/Merosin [5H2]
Description Laminins are essential and abundant structural non-collagenous glycoproteins localizing to basement membranes. Basement membranes (cell-associated extracellular matrices (ECMs)) are polymers of laminins with stabilizing Type IV Collagen networks, Nidogen and several proteoglycans. Basement membranes are found under epithelial layers, around the endothelium of blood vessels, and surrounding muscle, peripheral nerve and fat cells. Formation of basement membranes influences cell proliferation, phenotype, migration, gene expression and tissue architecture. Each laminin is a heterotrimer of α, β and γ chain subunits that undergoes cell-secretion and incorporation into the ECM. Laminins can self-assemble and bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan and cognate laminin receptors. The human Laminin α-2 gene is necessary for sustenance of mature muscle cells. The Laminin α-2 gene is associated with congenita. (Shipping Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Monkey, Rabbit -
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 -
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