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Zinc-Alpha-2-Glycoprotein Human, Sheep Polyclonal Antibody

  • Regulatory status:RUO
  • Type:Polyclonal Antibody
  • Other names:ZA2G, ZAG, AZGP1, Zn-alpha-2-glycoprotein, Zn-alpha-2-GP, ZNGP1
  • Species:Human
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Cat. No. Size Price


RD184093100 0.1 mg
PubMed Product Details
Technical Data

Type

Polyclonal Antibody

Applications

Western blotting, ELISA, Immunohistochemistry

Antibodies Applications

Source of Antigen

293 cell line (Human embryonic kidney)

Hosts

Sheep

Preparation

The antibody was raised in sheep by immunization with the recombinant Human ZA2G.

Amino Acid Sequence

The immunization antigen is a protein containing 290 AA of recombinant Human ZA2G. The AA sequence (AA 13–290) is identical to Swiss-Prot-P25311 (AA 18–295, mature Zinc-Alpha-2– Glycoprotein). 12 extra AA were fused with the N-terminus (highlighted).

ASWSHPQFEKGSQENQDGRYSLTYIYTGLSKHVEDVPAFQALGSLNDLQFFRYNSKDRKSQPMGLWRQVEGMEDWKQDSQLQKAREDIFMETLKDIVEYYNDSNGSHVLQGRFGCEIENNRSSGAFWKYYYDGKDYIEFNKEIPAWVPFDPAAQITKQKWEAEPVYVQRAKAYLEEECPATLRKYLKYSKNILDRQDPPSVVVTSHQAPGEKKKLKCLAYDFYPGKIDVHWTRAGEVQEPELRGDVLHNGNGTYQSWVVVAVPPQDTAPYSCHVQHSSLAQPLVVPWEAS

Ala 1 to His 5 were confirmed by N-terminal sequencing

Species Reactivity

Human. Not yet tested in other species.

Purification Method

Immunoaffinity chromatography on a column with immobilized recombinant Human ZA2G.

Antibody Content

0.1 mg (determined by BCA method, BSA was used as a standard)

Formulation

The antibody is lyophilized in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2. AZIDE FREE.

Reconstitution

Add 0.1 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

The lyophilized antibody remains stable and fully active until the expiry date when stored at –20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles and store frozen at –80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show decline in activity after one week at 4°C.

Quality Control Test

Indirect ELISA – to determine titer of the antibody SDS PAGE – to determine purity of the antibody

Note

This product is for research use only.

Summary

Research topic

Energy metabolism and body weight regulation, Oncology

Summary

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.

References to Summary

References to Zinc-Alpha-2-Glycoprotein

  • Araki T, Gejyo F, Takagaki K, Haupt H, Schwick HG, Burgi W, Marti T, Schaller J, Rickli E, Brossmer R, et al. Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens. Proc Natl Acad Sci U S A. 1988 Feb;85 (3):679-83
  • Bao Y, Bing C, Hunter L, Jenkins JR, Wabitsch M, Trayhurn P. Zinc-alpha2-glycoprotein, a lipid mobilizing factor, is expressed and secreted by human (SGBS) adipocytes. FEBS Lett. 2005 Jan 3;579 (1):41-7
  • Bennett MJ, Lebron JA, Bjorkman PJ. Crystal structure of the hereditary haemochromatosis protein HFE complexed with transferrin receptor. Nature. 2000 Jan 6;403 (6765):46-53
  • Bing C, Bao Y, Jenkins J, Sanders P, Manieri M, Cinti S, Tisdale MJ, Trayhurn P. Zinc-alpha2-glycoprotein, a lipid mobilizing factor, is expressed in adipocytes and is up-regulated in mice with cancer cachexia. Proc Natl Acad Sci U S A. 2004 Feb 24;101 (8):2500-5
  • Brysk MM, Lei G, Adler-Storthz K, Chen Z, Brysk H, Tyring SK, Arany I. Zinc-alpha2-glycoprotein expression as a marker of differentiation in human oral tumors. Cancer Lett. 1999 Mar 22;137 (1):117-20
  • Brysk MM, Lei G, Selvanayagam P, Brysk H, Tyring SK, Arany I. Modulation by interferon-gamma of zinc-alpha 2-glycoprotein gene expression in human epithelial cell lines. Anticancer Res. 1997 Sep-Oct;17 (5A):3387-91
  • BURGI W, SCHMID K. Preparation and properties of Zn-alpha 2-glycoprotein of normal human plasma. J Biol Chem. 1961 Apr;236:1066-74
  • Burmeister WP, Gastinel LN, Simister NE, Blum ML, Bjorkman PJ. Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor. Nature. 1994 Nov 24;372 (6504):336-43
  • Diez-Itza I, Sanchez LM, Allende MT, Vizoso F, Ruibal A, Lopez-Otin C. Zn-alpha 2-glycoprotein levels in breast cancer cytosols and correlation with clinical, histological and biochemical parameters. Eur J Cancer. 1993;29A (9):1256-60
  • Freije JP, Fueyo A, Uria JA, Velasco G, Sanchez LM, Lopez-Boado YS, Lopez-Otin C. Human Zn-alpha 2-glycoprotein: complete genomic sequence, identification of a related pseudogene and relationship to class I major histocompatibility complex genes. Genomics. 1993 Dec;18 (3):575-87
  • Gohda T, Makita Y, Shike T, Tanimoto M, Funabiki K, Horikoshi S, Tomino Y. Identification of epistatic interaction involved in obesity using the KK/Ta mouse as a Type 2 diabetes model: is Zn-alpha2 glycoprotein-1 a candidate gene for obesity?. Diabetes. 2003 Aug;52 (8):2175-81
  • Hale LP. Zinc alpha-2-glycoprotein regulates melanin production by normal and malignant melanocytes. J Invest Dermatol. 2002 Aug;119 (2):464-70
  • Hale LP, Price DT, Sanchez LM, Demark-Wahnefried W, Madden JF. Zinc alpha-2-glycoprotein is expressed by malignant prostatic epithelium and may serve as a potential serum marker for prostate cancer. Clin Cancer Res. 2001 Apr;7 (4):846-53
  • Hansson SF, Puchades M, Blennow K, Sjogren M, Davidsson P. Validation of a prefractionation method followed by two-dimensional electrophoresis - Applied to cerebrospinal fluid proteins from frontotemporal dementia patients. Proteome Sci. 2004 Nov 18;2 (1):7
  • Hirai K, Hussey HJ, Barber MD, Price SA, Tisdale MJ. Biological evaluation of a lipid-mobilizing factor isolated from the urine of cancer patients. Cancer Res. 1998 Jun 1;58 (11):2359-65
  • Im JS, Yu KO, Illarionov PA, LeClair KP, Storey JR, Kennedy MW, Besra GS, Porcelli SA. Direct measurement of antigen binding properties of CD1 proteins using fluorescent lipid probes. J Biol Chem. 2004 Jan 2;279 (1):299-310
  • Jain S, Rajput A, Kumar Y, Uppuluri N, Arvind AS, Tatu U. Proteomic analysis of urinary protein markers for accurate prediction of diabetic kidney disorder. J Assoc Physicians India. 2005 Jun;53:513-20
  • Kamoshida S, Watanabe K, Suzuki M, Mizutani Y, Sakamoto K, Sugimoto Y, Oka T, Fukushima M, Tsutsumi Y. Expression of cancer cachexia-related factors in human cancer xenografts: an immunohistochemical analysis. Biomed Res. 2006 Dec;27 (6):275-81
  • Lopez-Boa
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