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Index / Biovend / Human, Zinc-Alpha-2-Glycoprotein , Rec. Prot. /Product Detail : RD172093100 Human, Zinc-Alpha-2-Glycoprotein , Rec. Prot.
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Human, Zinc-Alpha-2-Glycoprotein , Rec. Prot.

 Price: 521   EUR
591   USD
404   GBP

Product name : Human, Zinc-Alpha-2-Glycoprotein , Rec. Prot.

Catalog number : RD172093100

Quantity: 0.1 mg

Availability: Yes

Supplier name : Biovend

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Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal or breast cyst fluids. When it is part of an amino acid sequence, it is identical to the tumor-derived lipid mobilizing factor (LMF) a protein associated with the dramatic loss of adipose body stores in cancer cachexia, and has been shown to stimulate lipolysis by adipocytes in vivo and in vitro. It might influence the regulation of body weight and age-dependent changes in genetically influenced obesity. It also regulates melanin production via normal and malignant melanocytes. It has been classified as a novel adipokine, because it is produced by both white and brown fat adipocytes and may influence local autocrine by reducing the adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexia-inducing conditions. Its role in body fat store homeostasis is important and should be studied further. ZAG exhibits a class I major histocompatibility complex (MHC) fold, but is a soluble protein rather than being anchored to plasma membranes. ZAG does not associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG has an open apical groove and X-ray crystallography of human-derived ZAG revealed an unidentifiable electron density in a similar position to that occupied by antigenic peptides in classical MHC proteins in isoforms of CD1. This presumptive ligand is not a peptide and the groove is too small to hold a glycolipid such as is presented by CD1 isoforms. Occupancy by a ligand is probably crucial to ZAG's biological function. Despite all of the structural and biochemical evidence that ZAG binds a ligand, none has so far been found by extraction from protein isolated from biological fluids. This difficulty could be due to the lability of the ligand, heterogeneous, or readily lost during purification procedures. Knowing more about how ZAG interacts with the compounds it has been found to bind, both natural and artificial, will inform searches for the elusive ligand(s) and its/their role in ZAG's signaling function. 

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