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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 -
Langerin/CD207 [H4]
Description Langerhans cells (LCs) are a subset of immature dendritic cells (DCs) that specifically localize in the epidermis and other mucosal epithelia. Epidermal LCs possess strong immunostimulatory capacity and play a central role in the initiation and regulation of immune responses. Langerin (CD207) is a Ca2+-dependent, C-type lectin domain-containing, type II transmembrane protein that induces epidermal LCs to differentiate into Birbeck granules (BG). BGs are organelles with superimposing and zippering membranes that influence proper class I type antigen presentation to the circulating T-cells. Human spleen, lymph node, thymus, liver, lung and heart express langerin protein. Langerin protein expression has utility in differentiating Langerhans cell histiocytosis from other non-Langerhans cell histiocytic proliferations. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Langerin/CD207 [H4]
Description Langerhans cells (LCs) are a subset of immature dendritic cells (DCs) that specifically localize in the epidermis and other mucosal epithelia. Epidermal LCs possess strong immunostimulatory capacity and play a central role in the initiation and regulation of immune responses. Langerin (CD207) is a Ca2+-dependent, C-type lectin domain-containing, type II transmembrane protein that induces epidermal LCs to differentiate into Birbeck granules (BG). BGs are organelles with superimposing and zippering membranes that influence proper class I type antigen presentation to the circulating T-cells. Human spleen, lymph node, thymus, liver, lung and heart express langerin protein. Langerin protein expression has utility in differentiating Langerhans cell histiocytosis from other non-Langerhans cell histiocytic proliferations. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Leptin/Obesity [F-3]
Description Although there is substantial evidence that body weight is physiologically regulated, the molecular basis of obesity is unknown. Five single-gene mutations in mice that result in an obese phenotype have been identified. The first such recessive obesity mutation, the obese mutation (Ob), was identified in 1950. Mutation of Ob results in profound obesity and type II diabetes as part of a syndrome that resembles morbid obesity in humans. It has been postulated that the Ob gene product may function as a component of a signaling pathway in adipose tissue that functions to regulate body fat depot size. The cloning and sequence analysis of the mouse Ob gene and its human homolog have been described. Ob encodes an adipose tissue-specific mRNA with a highly conserved 167 amino acid open reading frame. The predicted amino acid sequence is 84% identical between human and mouse and has the features of a secreted protein. A nonsense mutation in codon 105 has been found in the original congenic C57B Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
Leptin/Obesity [F-3]
Description Although there is substantial evidence that body weight is physiologically regulated, the molecular basis of obesity is unknown. Five single-gene mutations in mice that result in an obese phenotype have been identified. The first such recessive obesity mutation, the obese mutation (Ob), was identified in 1950. Mutation of Ob results in profound obesity and type II diabetes as part of a syndrome that resembles morbid obesity in humans. It has been postulated that the Ob gene product may function as a component of a signaling pathway in adipose tissue that functions to regulate body fat depot size. The cloning and sequence analysis of the mouse Ob gene and its human homolog have been described. Ob encodes an adipose tissue-specific mRNA with a highly conserved 167 amino acid open reading frame. The predicted amino acid sequence is 84% identical between human and mouse and has the features of a secreted protein. A nonsense mutation in codon 105 has been found in the original congenic C57B Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
L-FABP (Liver Fatty Binding Protein) [F9]
Description Fatty acid-binding proteins, designated FABPs, are a family of homologous cytoplasmic proteins that are expressed in a highly tissue-specific manner and play an integral role in the balance between lipid and carbohydrate metabolism. FABPs mediate fatty acid (FA) and/or hydrophobic ligand uptake, transport and targeting within their respective tissues. The mechanisms underlying these actions can give rise to both passive diffusional uptake and protein-mediated transmembrane transport of FAs. FABPs are expressed in adipocytes (A-FABP), brain (B-FABP), epithelium (E-FABP, psoriasis-associated FABP, PA-FABP), striated muscle and heart (H-FABP, mammary-derived growth inhibitor or MDGI), intestine (I-FABP), liver (L-FABP), myelin (M-FABP) and testis (T-FABP). Liver-specific FABP (L-FABP) expression is modulated by developmental, hormonal, dietary and pharmacological factors, and is required for cholesterol synthesis and metabolism. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human -
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 -
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 -
MDR1/ABCB1/P-Glycoprotein [D-11]
Description Multi-Drug Resistance Marker (P-Glycoprotein) is a 170 kD cell membrane protein of the multi-drug resistance gene, MDR-1. Studies have linked the presence of P-Glycoprotein with resistance to a wide variety of chemotherapeutic agents. P-Glycoprotein is also found in various concentrations in most normal tissues, suggesting that the primary role for this protein is in normal secretion of physiological metabolites. (Shipping Cost: €200.00) Host Mouse Application ELISA (solid phase), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human