Zinc-Alpha-2-Glycoprotein (ZA2G)

Zinc-alpha-2-glycoprotein (ZAG) is found in body fluids such as serum, sweat, and seminal and breast cyst fluids. It is identical in amino acid sequence to 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. A role for ZAG has been proposed in the regulation of body weight, and age- dependent changes in genetically influenced obesity, and also it regulates melanin production by normal and malignant melanocytes. It has also recently been classified as a novel adipokine in that it is produced by both white and brown fat adipocytes and may act in a local autocrine fashion in the reduction of adiposity in cachexia. Controlling ZAG/LMF's activity could be life-saving in the management of certain cancers and other cachexia-inducing conditions, and its possible normal role in body fat store homeostasis is deserving of understanding in its own right. ZAG exhibits a class I major histocompatibility complex (MHC) fold but is a soluble protein rather than being anchored to plasma membranes and 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 and glycolipids 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. By analogy with all other MHC class I-related proteins that have an open apical groove [some do not ], 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 because the ligand is labile, 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. \n\nApplications:\nSuitable for use in ELISA and Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stabillty:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

Z0133-01

Size

100ug

Applications

ELISA, WB

Hosts

Rabbit

Reactivities

Hum

Form

Supplied as a lyophilized powder in PBS, pH 7.2. No preservative added. Reconstitute with 100ul sterile dH2O. Let the lyophilized pellet dissolve completely.

P Type

Pab

Purity

Purified by Immunoaffinity chromatography.

Isotype

igG

References

1. Brettschneider J, Mogel H, Lehmensiek V, Ahlert T, Sussmuth S, Ludolph AC, Tumani H. Proteome \nAnalysis of Cerebrospinal Fluid in Amyotrophic Lateral Sclerosis (ALS). Neurochem Res. 2008 \nMay 15; \nPage 2 of 4 (VERSION: 2009-10-23)\n2. Sanchez, L. M., LopezOtin, C., and Bjorkman, P. J. Biochemical characterization and \ncrystalization of human Zn-alpha(2)-glycoprotein, a soluble class I major histocompatibility \ncomplex homolog. \n3. Burmeister, W. P., Gastinel, L. N., Simister, N. E., Blum, M. L., and Bjorkman, P. J. Crystal structure \nat 2.2

Additional Info

Recognizes human ZA2G.