Acrp30 (adipocyte complement-related protein of 30kD), also known as AdipoQ, APM1, Adiponectin, Gelatin binding protein 28kD/GBP28 or adipocyte most abundant gene transcript) was identified as a novel adipocyte-specific synthesized and secreted protein with structural resemblance to complement factor C1q. Like adipsin, Acrp30 secretion is induced ~10-fold during adipocyte differentiation. Plasma levels are reduced in obese humans, and low levels are associated with insulin-resistance. Treatment of db/db mice with TZD increased Acrp30 levels. Acrp30 (mouse 247aa, rat human 244aa; chromosome 3q27) consists of a predicted NT-signal sequence aa91-14), followed by a 27-aa unique region, and then by 22 perfect Gly-X-Pro or Gly-X- X collagen like repeats, and a globular segment at the C-terminus. Structurally, but at the sequence level, Acrp30 resembles other collagen-like and globular domain proteins (lung surfactant protein and hepatocytesmannan-bindingproteins).Acrp30is proteolytically cleaved at 104aa to generate the globular Acrp30 (gAcrp30). Administration of gAcrp30 into mice fed a diet high in fat and sugar caused substantial weight loss. Full length Acrp30 was less potent than gAcrp30. In the circulation, adiponectin is predominantly present as several characteristic oligomeric complexes. The basic building block of the adiponectin complex is a trimer or low molecular weight (LMW) oligomer, which is formed via hydrophobic interactions within its globular domain. Two trimers self-associate to form a disulfide-linked hexamer or middle molecular weight (MMW) oligomer, which further assembles into a bouquet-like high molecular weight (HMW) multimeric complex that consists of 12-18 monomers. Several conserved lysine residues (K68, K71, K80, and K104) within the collagenous domain of adiponectin are modified by hydroxylation and glycosylation. These three oligomeric forms were differentially glycosylated, with the HMW oligomer having the highest carbohydrate content. Disruption of hydroxylation and glycosylation by substitution of the four conserved lysines with arginines selectively abrogated the intracellular assembly of the HMW oligomers in vitro as well as in vivo. Replacement of cysteine 39 with alanine (C39A) can only form trimer but not hexamer or HMW for. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions on its target tissues. Clinical studies have also demonstrated that T2DM and coronary heart disease are associated with selective reduction of the HMW oligomeric adiponectin. Interestingly, two rare missense mutations (G84R and G90S) identified in T2DM patients can form trimers and hexamers, but lack the capacity to form the HMW complex.
Source:Recombinant protein corresponding to the Trimeric form of mouse Adiponectin, expressed in HEK293 cells, stably transfected with pchAd-Fvector encoding FLAG epitope-tagged proteins.
Biological Activity:ED50=3-8.5g/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.
Applications:Suitable for use in In vitro, Ex vivo, In vivo Activity Analysis, Binding assay and ELISA. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:Lyophilized powder may be stored at -20°C. Reconstitute with sterile buffer. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 6 months at -20°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.
仕様
Size：10ug
Source Antigen：Recombinant, HEK293 cells
Grade：Highly Purified
Purity：Highly Purified (~95%)
Form：Supplied as a lyophilized powder in PBS, pH 7.4. No preservative added. Reconstitute with sterile PBS, 0.1% protease-free BSA.
