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Laminin Receptor/RPSA [MD164]
Description Laminins, a family of extracellular matrix glycoproteins, are the major non-collagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. This gene encodes a high-affinity, non-integrin family, laminin receptor 1. Reportedly, level of laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell line than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. (Shipping Cost: €200.00) Host Mouse Application Immunohistochemistry (IHC) Reactivity Human -
Langerin/CD207 [12D6]
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 Immunohistochemistry (IHC) Reactivity Human -
Langerin/CD207 [12D6]
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 Immunohistochemistry (IHC) 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 -
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 -
LHRH Receptor/GnRHR [F1G4[
Description Gonadotropin-releasing hormone (GnRH) is released in a pulsatile manner that varies with the reproductive cycle. This hypothalamic hormone is transported to the pituitary, where it binds to specific receptors and regulates the synthesis and release of luteinizing hormone (LH) and follicle-stimulating hormone (FSH). The GnRH receptor (GnRHR), like most G protein-coupled receptors, contains a seven transmembrane domain. However, unlike most G protein-coupled receptors, the GnRHR lacks an intracellular C-terminal domain. The GnRHR gene is thought to be regulated by GnRH and activin A, and has been shown to undergo alternative splicing. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat -
LHRH Receptor/GnRHR [F1G4]
Description Gonadotropin-releasing hormone (GnRH) is released in a pulsatile manner that varies with the reproductive cycle. This hypothalamic hormone is transported to the pituitary, where it binds to specific receptors and regulates the synthesis and release of luteinizing hormone (LH) and follicle-stimulating hormone (FSH). The GnRH receptor (GnRHR), like most G protein-coupled receptors, contains a seven transmembrane domain. However, unlike most G protein-coupled receptors, the GnRHR lacks an intracellular C-terminal domain. The GnRHR gene is thought to be regulated by GnRH and activin A, and has been shown to undergo alternative splicing. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat