Results for Other Proteins ( 64690 )
Recombinant Human/Murine/Rat Irisin (Legacy Tebubio ref. 167100-65). Irisin is a proteolytic hormone released into circulation by skeletal muscle tissue during acute exercise, and is a derivative of the cleaved plasma membrane protein Fibronectin type III domain-containing protein 5 (FNDC5). Found in muscle tissue, FNDC5 is synthesized at increased levels during exercise as a result of the overexpression of the exercise-responsive transcriptional co-activator PGC-1alpha (peroxisome proliferator-activated receptor-gamma co-activator-1alpha). Like its parent polypeptide, Irisin can induce the browning of subcutaneous adipocytes, or the conversion of white adipose tissue (WAT or white fat) into brown (or beige) adipose tissue (BAT or brown fat). Given that brown fat can undergo thermogenesis, or the physiologic process of heat production, Irisin contributes to the metabolic process by increasing thermogenic function and glucose homeostasis. Irisin, thus, represents a link between exercise
Recombinant Human/Murine/Rat Irisin (Legacy Tebubio ref. 167100-65). Irisin is a proteolytic hormone released into circulation by skeletal muscle tissue during acute exercise, and is a derivative of the cleaved plasma membrane protein Fibronectin type III domain-containing protein 5 (FNDC5). Found in muscle tissue, FNDC5 is synthesized at increased levels during exercise as a result of the overexpression of the exercise-responsive transcriptional co-activator PGC-1alpha (peroxisome proliferator-activated receptor-gamma co-activator-1alpha). Like its parent polypeptide, Irisin can induce the browning of subcutaneous adipocytes, or the conversion of white adipose tissue (WAT or white fat) into brown (or beige) adipose tissue (BAT or brown fat). Given that brown fat can undergo thermogenesis, or the physiologic process of heat production, Irisin contributes to the metabolic process by increasing thermogenic function and glucose homeostasis. Irisin, thus, represents a link between exercise
Recombinant Human FGF-BP-1 (Legacy Tebubio ref. 167100-66). The Fibroblast Growth Factor (FGF) Superfamily is comprised of multifunctional proteins that serves to regulate several complex biological processes related to the development, restoration, and/or redistribution of prenatal and postnatal tissue, as well as angiogenesis, wound healing, nerve regeneration, chronic inflammation, and cancer growth. Members of the FGF Superfamily function through paracrine, autocrine and intracrine pathways to promote spatial and temporal integrations of several cell responses, such as proliferation, growth, differentiation, and migration. Fibroblast growth factor binding protein 1 (FGF-BP-1) is a secreted glycoprotein, which contains both a heparin-binding domain and a distinct FGF-binding region, that is shed into circulation where it acts as a chaperone molecule for FGFs, most notably FGF-acidic and FGF-basic. Once secreted, FGF-BP-1 can bind FGFs in a reversible manner to mobilize them from ina
Recombinant Human FGF-BP-1 (Legacy Tebubio ref. 167100-66). The Fibroblast Growth Factor (FGF) Superfamily is comprised of multifunctional proteins that serves to regulate several complex biological processes related to the development, restoration, and/or redistribution of prenatal and postnatal tissue, as well as angiogenesis, wound healing, nerve regeneration, chronic inflammation, and cancer growth. Members of the FGF Superfamily function through paracrine, autocrine and intracrine pathways to promote spatial and temporal integrations of several cell responses, such as proliferation, growth, differentiation, and migration. Fibroblast growth factor binding protein 1 (FGF-BP-1) is a secreted glycoprotein, which contains both a heparin-binding domain and a distinct FGF-binding region, that is shed into circulation where it acts as a chaperone molecule for FGFs, most notably FGF-acidic and FGF-basic. Once secreted, FGF-BP-1 can bind FGFs in a reversible manner to mobilize them from ina
Recombinant Human sCD14 (Legacy Tebubio ref. 167110-01). CD14 is a cell surface-anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappaB. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor. The calculated molecular weight of Recombinant Human sCD14 is 35.6 kDa.
Recombinant Human sCD14 (Legacy Tebubio ref. 167110-01). CD14 is a cell surface-anchored glycoprotein that is expressed predominantly by monocytes and tissue macrophages. CD14 associates with MD-2 (LY-96) and TLR4 to form a receptor complex, which signals specifically in response to bacterial lipopolysaccharide (LPS) binding. The CD14/MD-2/TLR4 receptor complex signals via MyD88, TIRAP, and TRAF6, and ultimately activates NF-kappaB. CD14 also exists in a soluble form, designated as sCD14, which is capable of specifically binding LPS in the extracellular space. Recombinant sCD14 is a 331 amino acid glycoprotein comprising the extracellular portion of the CD14 receptor. The calculated molecular weight of Recombinant Human sCD14 is 35.6 kDa.
Recombinant Human p16-INK4a (Legacy Tebubio ref. 167110-02). p16-INK4a is a nuclear protein that regulates the cell cycle by inhibiting cyclin-dependent kinase-4 (CDK4) and CDK6. p16-INK4a inhibits CDK activity by binding to the CDK molecules in a manner that interferes with their ability to interact with cyclin D. This activity has the effect of suppressing tumor formation and growth, and of inducing replicative senescence in various normal cells, including stem cells. The expression of p16-INK4a steadily increases with age, and tends to accumulate in stem cell compartments. The deletion, rearrangement, or mutation of the p16-INK4a gene is frequently found in melanomas, as well as in certain other types of cancer. Recombinant Human p16-INK4a is a 16.5 kDa protein containing 156 amino acid residues. Kim, W.Y. and Sharpless, N.E. (2006)Cell 127(2):265-75.
Recombinant Human p16-INK4a (Legacy Tebubio ref. 167110-02). p16-INK4a is a nuclear protein that regulates the cell cycle by inhibiting cyclin-dependent kinase-4 (CDK4) and CDK6. p16-INK4a inhibits CDK activity by binding to the CDK molecules in a manner that interferes with their ability to interact with cyclin D. This activity has the effect of suppressing tumor formation and growth, and of inducing replicative senescence in various normal cells, including stem cells. The expression of p16-INK4a steadily increases with age, and tends to accumulate in stem cell compartments. The deletion, rearrangement, or mutation of the p16-INK4a gene is frequently found in melanomas, as well as in certain other types of cancer. Recombinant Human p16-INK4a is a 16.5 kDa protein containing 156 amino acid residues. Kim, W.Y. and Sharpless, N.E. (2006)Cell 127(2):265-75.
Recombinant Human p16-INK4a-TAT (Legacy Tebubio ref. 167110-02T). p16-INK4a is a nuclear protein that regulates the cell cycle by inhibiting cyclin-dependent kinase-4 (CDK4) and CDK6. p16-INK4a inhibits CDK activity by binding to the CDK molecules in a manner that interferes with their ability to interact with cyclin D. This activity has the effect of suppressing tumor formation and growth, and of inducing replicative senescence in various normal cells, including stem cells. The expression of p16-INK4a steadily increases with age, and tends to accumulate in stem cell compartments. The deletion, rearrangement, or mutation of the p16-INK4a gene is frequently found in melanomas, as well as in certain other types of cancer. p16-INK4a and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other nuclea