AZGP1 Human, HEK

Zinc-alpha-2-glycoprotein (ZAG), present in bodily fluids like serum, sweat, and fluids from seminal vesicles and breast cysts, shares its amino acid sequence with tumor-derived lipid mobilizing factor (LMF). LMF is linked to significant fat loss in cancer cachexia. ZAG has been observed to promote the breakdown of fats (lipolysis) by fat cells both in living organisms and laboratory settings. Studies suggest ZAG's role in body weight control, age-related changes in genetically linked obesity, and regulation of melanin production in normal and cancerous pigment cells. Classified as an adipokine, it is produced by both white and brown fat cells, potentially acting locally to reduce fat mass in cachexia. ZAG/LMF activity control could be crucial for managing certain cancers and cachexia-inducing conditions. Understanding its potential role in regulating body fat storage is important. ZAG structurally resembles a class I major histocompatibility complex (MHC) molecule but exists as a soluble protein, not bound to cell membranes, and doesn't associate with alpha-2-microglobulin in humans. Like antigen-presenting MHC class I proteins, ZAG possesses an open groove. X-ray crystallography of human ZAG revealed an unknown electron density in a location similar to where antigenic peptides bind in MHC proteins and glycolipids in CD1 isoforms. This potential binding partner is not a peptide, and the groove is too small for a CD1-presented glycolipid. Similar to other MHC class I-related proteins with an open groove, ligand binding is likely crucial for ZAG's function. Despite evidence of ZAG binding to ligands, none have been identified from protein isolated from biological fluids. This could be due to the ligand's instability, variability, or loss during purification. Understanding how ZAG interacts with known natural and synthetic compounds will aid in finding its elusive ligand(s) and their role in ZAG signaling.

Recombinant human ZA2G, produced in HEK cells, is a single, glycosylated polypeptide chain consisting of 290 amino acids, encompassing residues 13 to 290. This recombinant protein is identical to the Swiss-Prot entry P25311 (amino acids 18-295), representing the mature form of Zinc-Alpha-2-Glycoprotein. An additional twelve amino acids have been added to the N-terminus.

White, lyophilized powder after filtration.

The product has been filtered through a 0.4 µm filter and lyophilized at a concentration of 0.5 mg/ml in a solution containing 0.1M Tris-HCl (pH 8.0) and 150mM NaCl.

To prepare a working solution, add deionized water to achieve a final concentration of approximately 0.5 mg/ml. Allow the lyophilized pellet to fully dissolve.

Lyophilized ZA2G remains stable for 3 weeks at room temperature. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, ZA2G should be stored at 4°C for 2-7 days. For prolonged storage, it is advisable to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing should be avoided.

Exceeds 90.0%, as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis and (b) SDS-PAGE analysis.

Human SGBS adipocytes, after differentiation, were treated with two different concentrations (5 and 20 µg/ml) of recombinant human ZA2G for 18 hours. Lipolysis was measured by quantifying glycerol release into the culture medium using a standard protocol. Isoproterenol (10 µM) and IBMX (100 µM) served as positive controls, while "Con" represents the negative control. Both ZA2G concentrations led to a 3-fold increase in glycerol release. The increase was statistically significant at both the 5 µg/ml dose of ZA2G (p<0.01) and in the positive controls.

Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, AZGP1, ZAG, Zinc-alpha-2-glycoprotein, ZNGP1, ZA2G.

293 Cell Line (Human Embryonic Kidney).

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