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Adiponectin (ADIPOQ) (N-Term) antibody

Details for Product No. ABIN115498, Supplier: Log in to see
Antigen
Epitope
N-Term
54
31
27
13
13
11
10
10
7
6
6
6
5
5
3
3
3
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human
449
144
96
30
15
4
4
2
1
Host
Rabbit
357
224
16
11
4
3
Clonality
Polyclonal
Conjugate
Un-conjugated
69
28
23
2
2
1
1
1
1
1
Application
Western Blotting (WB)
397
367
86
46
45
35
14
12
11
10
9
9
8
2
2
2
2
1
1
1
1
1
1
Supplier
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Immunogen The immunization antigen (26.4 kDa) is a protein containing 242 AA of recombinant Human Adiponectin. N-Terminal His-tag, 12 extra AA (highlighted).
Sequence MRGSHHHHHH GSGHDQETTT QGPGVLLPLP KGACTGWMAG IPGHPGHNGA PGRDGRDGTP GEKGEKGDPG LIGPKGDIGE TGVPGAEGPR GFPGIQGRKG EPGEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD TN Remarks: Source of Antigen: E.Coli
Specificity The antibody was raised in rabbits by immunization with the recombinant Adiponectin.
Cross-Reactivity (Details) Species reactivity (tested):Human.
Purification Immunoaffinity Chromatography.
Alternative Name Adiponectin
Background Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 aminoacid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells. The protein belongs to the soluble defence collagen superfamily, it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. Adiponectin forms homotrimers, which are the building blocks for higher order complexes found circulating in serum. Together, these complexes make up approximately 0.01 % of total serum protein. Adiponectin receptors AdipoR1 and AdipoR2 have been recently cloned, AdipoR1 is abundantly expressed in skeletal muscle, whereas AdipoR2 is predominantly expressed in the liver. Paradoxically, adipose tissue-expressed adiponectin levels are inversely related to the degree of adiposity. Adiponectin concentrations correlate negatively with glucose, insulin, triglyceride concentrations, liver fat content and body mass index and positively with high-density lipoproteincholesterol levels, hepatic insulin sensitivity and insulin-stimulated glucose disposal. Adiponectin has been shown to increase insulin sensitivity and decrease plasma glucose by increasing tissue fat oxidation. Of particular interest is that low adiponectin serum levels predict type 2 diabetes independent of other risk factors. Adiponectin also inhibits the inflammatory processes of atherosclerosis suppressing the expression of adhesion and cytokine molecules in vascular endothelial cells and macrophages, respectively. This adipokine plays a role as a scaffold of newly formed collagen in myocardial remodelling after ischaemic injury and also stimulates angiogenesis by promoting cross-talk between AMP-activated protein kinase and Akt signalling in endothelial cells. Low serum adiponectin levels are found in patients with coronary artery disease. Moreover, high circulating levels of adiponectin are associated with decreased risk of myocardial infarction, independent of other factors. Altogether, adiponectin has the potential to become a clinically relevant parameter to be measured routinely in subjects at risk for type 2 diabetes, atherosclerosis and the metabolic syndrome.Synonyms: 30 kDa adipocyte complement-related protein, ACDC, ACRP30, ADIPOQ, APM1, Adipocyte, Adipocyte complement-related 30 kDa protein, Adipose most abundant gene transcript 1 protein, C1q and collagen domain-containing protein, GBP28, Gelatin-binding protein
Gene ID 9370
NCBI Accession NP_001171271
UniProt Q15848
Research Area Cancer, Atherosclerosis, Metabolism, Hormones
Application Notes Western Blot.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Reconstitution Restore with 0.1 mL of deionized water and let 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.
Buffer 0.05 M phosphate buffer, 0.5 M NaCl, pH 7.2, None
Preservative Without preservative
Handling Advice Avoid repeated freezing and thawing.
Storage -20 °C
Storage Comment Prior to reconstitution store at -70 °C. Following reconstitution store the antibody (in aliquots) at -20 °C for 6 month.
Expiry Date 6 months
Product cited in: Badakhshi, Marnitz, Scherer, Budach, Haisch: "[Adenoid cystic carcinoma of the oropharynx. Brachytherapy for the treatment of local recurrences]" in: HNO, Vol. 56, Issue 3, pp. 328-31, 2008

Background publications Waki, Yamauchi, Kamon, Kita, Ito, Hada, Uchida, Tsuchida, Takekawa, Kadowaki: "Generation of globular fragment of adiponectin by leukocyte elastase secreted by monocytic cell line THP-1." in: Endocrinology, Vol. 146, Issue 2, pp. 790-6, 2005

Wang, Lam, Xu, Lu, Xu, Cooper, Xu: "Adiponectin inhibits cell proliferation by interacting with several growth factors in an oligomerization-dependent manner." in: The Journal of biological chemistry, Vol. 280, Issue 18, pp. 18341-7, 2005

Chen, Montagnani, Funahashi, Shimomura, Quon: "Adiponectin stimulates production of nitric oxide in vascular endothelial cells." in: The Journal of biological chemistry, Vol. 278, Issue 45, pp. 45021-6, 2003

Berg, Combs, Scherer: "ACRP30/adiponectin: an adipokine regulating glucose and lipid metabolism." in: Trends in endocrinology and metabolism: TEM, Vol. 13, Issue 2, pp. 84-9, 2002

Yamauchi, Kamon, Minokoshi, Ito, Waki, Uchida, Yamashita, Noda, Kita, Ueki, Eto, Akanuma, Froguel, Foufelle, Ferre, Carling, Kimura, Nagai, Kahn, Kadowaki: "Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase." in: Nature medicine, Vol. 8, Issue 11, pp. 1288-95, 2002

Okamoto, Kihara, Ouchi, Nishida, Arita, Kumada, Ohashi, Sakai, Shimomura, Kobayashi, Terasaka, Inaba, Funahashi, Matsuzawa: "Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice." in: Circulation, Vol. 106, Issue 22, pp. 2767-70, 2002

Wang, Xu, Knight, Xu, Cooper: "Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity." in: The Journal of biological chemistry, Vol. 277, Issue 22, pp. 19521-9, 2002