Adiponectin (Acrp30) Active Protein | ACRP30 active protein

Mouse Adiponectin (Acrp30)

Cat. Num. AAA691926

• Gene Names: Adipoq; APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• Purity: > 98% by SDS-PAGE gel and HPLC analyses.
• Synonyms: Adiponectin (Acrp30); Mouse Adiponectin (Acrp30); Adipoq; APN; Acdc; apM1; 30 kDa; GBP28; adipo; Acrp30; ACRP30 active protein

• Host: Insect Cells
• Purity/Purification: > 98% by SDS-PAGE gel and HPLC analyses.
• Form/Format: Lyophilized; 20 mM Tris, pH 8.5 + 75mM L-Arginine.
• Sequence: RGHHHHHHHHVTTTEELAPALVPPPKGTCAGWMAGIPGHPGHNGTPGRDG RDGTPGEKGEKGDAGLLGPKGETGDVGMTGAEGPRGFPGTPGRKGEPGEA AYVYRSAFSVGLETRVTVPNVPIRFTKIFYNQQNHYDGSTGKFYCNIPGL YYFSYHITVYMKDVKVSLFKKDKAVLFTYDQYQEKNVDQASGSVLLHLEV GDQVWLQVYGDGDHNGLYADNVNDSTFTGFLLYHDTN
• Sequence Length: 247

• Endotoxin Level: <0.1 ng/ug of protein (<1EU/ug).
• Reconstitution: Centrifuge before opening to ensure complete recovery of vial contents. Reconstitute in water to a concentration of 1.0 mg/m. Do Not Vortex. Allow the reconstitutes vial to sit at room temperature for 30 minutes before use. This solution can be stored for up 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
• Tag: His-Tag
• Length (aa): 236
• Preparation and Storage: The lyophilized is stable at room temperature for 1 month and at 4°C for 6 months. Reconstituted working aliquots are stable for 1 week at 2°C to 8°C and for 3 months at -20° to -80°C.

Related Product Information for ACRP30 active protein

Adiponectin is an adipose-derived secreted protein containing 236 amino acid residues.  It is relatively abundant in humans and rodents, accounting for about 0.01% of total plasma protein. The circulating levels of adiponectin are decreased under conditions of obesity, insulin resistance, and type II diabetes.  Disruption of adiponectin in mice causes insulin resistance and neointimal formation.  Conversely, administration of recombinant adiponectin suppresses hepatic glucose production, and reverses insulin resistance associated with both lipoatrophy and obesity.  The protective role of adiponectin is attributed to its anti-inflammatory properties (e.g. ability to suppress expression of TNF-beta and class A scavenger receptor in macrophages). Recombinant adiponectin is a multimeric glycoprotein containing amino acids Val-21 to Asn-247 of the adiponectin precursor protein fused to an N-terminal histidine tag.  Monomeric glycosylated adiponectin migrates at an apparent molecular weight of approximately 31-36 kDa by SDS PAGE analysis under reducing conditions.

Product Categories/Family for ACRP30 active protein

Cytokines & Growth Factors

NCBI and Uniprot Product Information

• NCBI GI #: 87252711
• NCBI GeneID: 11450
• NCBI Accession #: NP_033735.3
• NCBI GenBank Nucleotide #: NM_009605.4
• UniProt Accession #: Q60994; Q62400; Q6GTX4; Q9DC68
• Molecular Weight: 31-36 kDa
• NCBI Official Full Name: adiponectin
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: Adipoq
• NCBI Official Synonym Symbols: APN; Acdc; apM1; 30kDa; GBP28; adipo; Acrp30
• NCBI Protein Information: adiponectin; adipocyte-specific protein AdipoQ; adipocyte complement related protein; 30 kDa adipocyte complement-related protein; adipocyte complement-related 30 kDa protein; adipocyte, C1Q and collagen domain containing; adipocyte, C1q and collagen domain-containing protein
• UniProt Protein Name: Adiponectin
• UniProt Gene Name: Adipoq
• UniProt Synonym Gene Names: Acdc; Acrp30; Apm1; ACRP30
• UniProt Entry Name: ADIPO_MOUSE

Uniprot Description

Function: Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subunit structure: Homomultimer. Forms trimers, hexamers and 12- to 18-mers. The trimers (low molecular weight complexes / LMW) are assembled via non-covalent interactions of the collagen-like domains in a triple helix and hydrophobic interactions within the globular C1q domain. Several trimers can associate to form disulfide-linked hexamers (middle molecular weight complexes / MMW) and larger complexes (higher molecular weight / HMW). The HMW-complex assembly may rely additionally on lysine hydroxylation and glycosylation. LMW, MMW and HMW complexes bind to HBEGF, MMW and HMW complexes bind to PDGFB, and HMW complex binds to FGF2. Interacts with CTRP9 via the C1q domain (heterotrimeric complex). Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location: Secreted.

Tissue specificity: Synthesized exclusively by adipocytes and secreted into plasma.

Induction: During hormone-induced adipose differentiation and activated by insulin.

Post-translational modification: HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. Ref.9 Ref.10 Ref.18O-glycosylated. Not N-glycosylated

By similarity O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups

By similarity. O-linked glycosylation in the N-terminal is disialylated with the structure Neu5Acalpha2->8Neu5Acalpha2->3Gal. Sialylated by alpha 2,8-sialyltransferase III. Ref.9 Ref.10 Ref.18

Miscellaneous: HMW-complex blood contents are higher in females than in males, are increased in males by castration and decreased again upon subsequent testosterone treatment, which blocks HMW-complex secretion.

Sequence similarities: Contains 1 C1q domain.Contains 1 collagen-like domain.