Adiponectin Recombinant Protein | ADIPOQ recombinant protein

Recombinant human Adiponectin protein

Cat. Num. AAA717060

• Gene Names: ADIPOQ; ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• Applications: ELISA, Western Blot
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Adiponectin; Recombinant human Adiponectin protein; ADIPOQ recombinant protein

• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence: ETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN

• Applicable Applications for ADIPOQ recombinant protein: ELISA, Western Blot
• Preparation and Storage: Store working aliquots at 4 degree C for up to one week. For extended storage, conserve at -20 degree C or -80 degree C. Repeated freezing and thawing is not recommended.

Related Product Information for ADIPOQ recombinant protein

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.

References

[1] "Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: evidence for regulation of multimerization by alterations in posttranslational modifications." Richards A.A., Stephens T., Charlton H.K., Jones A., Macdonald G.A., Prins J.B., Whitehead J.P. Mol. Endocrinol. 20:1673-1687(2006)
[2] "Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome." Kondo H., Shimomura I., Matsukawa Y., Kumada M., Takahashi M., Matsuda M., Ouchi N., Kihara S., Kawamoto T., Sumitsuji S., Funahashi T., Matsuzawa Y. Diabetes 51:2325-2328(2002)

NCBI and Uniprot Product Information

• NCBI GI #: 295317371
• NCBI GeneID: 9370
• NCBI Accession #: NP_001171271.1
• NCBI GenBank Nucleotide #: NM_001177800.1
• UniProt Accession #: Q15848; Q58EX9
• Molecular Weight: 30 KD
• NCBI Official Full Name: Homo sapiens adiponectin, C1Q and collagen domain containing (ADIPOQ), transcript variant 1, mRNA
• NCBI Official Synonym Full Names: adiponectin, C1Q and collagen domain containing
• NCBI Official Symbol: ADIPOQ
• NCBI Official Synonym Symbols: ACDC; ADPN; APM1; APM-1; GBP28; ACRP30; ADIPQTL1
• NCBI Protein Information: adiponectin; OTTHUMP00000210047; OTTHUMP00000210048; gelatin-binding protein 28; adipose specific collagen-like factor; 30 kDa adipocyte complement-related protein; adipocyte complement-related 30 kDa protein; adipose most abundant gene transcript 1 protein
• UniProt Protein Name: Adiponectin
• Protein Family: Adiponectin
• UniProt Gene Name: ADIPOQ
• UniProt Synonym Gene Names: ACDC; ACRP30; APM1; GBP28
• UniProt Entry Name: ADIPO_HUMAN

NCBI Description

This gene is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes. Mutations in this gene are associated with adiponectin deficiency. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Apr 2010]

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.9Subunit 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 aditionally 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 CTRP9A via the C1q domain (heterotrimeric complex) By similarity. Ref.10 Ref.11 Ref.12Subcellular location: Secreted. Tissue specificity: Synthesized exclusively by adipocytes and secreted into plasma.Domain: The C1q domain is commonly called the globular domain.Post-translational modification: Hydroxylated Lys-33 was not identified in Ref.11, probably due to poor representation of the N-terminal peptide in mass fingerprinting.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 By similarity. Ref.11 Ref.12O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation. Ref.11 Ref.12Polymorphism: Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIM:612556].Involvement in disease: Defects in ADIPOQ are the cause of adiponectin deficiency (ADPND) [MIM:612556]. ADPND results in very low concentrations of plasma adiponectin. Ref.13Genetic variations in ADIPOQ are associated with non-insulin-dependent diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes mellitus type 2. NIDDM is characterized by an autosomal dominant mode of inheritance, onset during adulthood and insulin resistance.Pharmaceutical use: Adiponectin might be used in the treatment of diabetes type 2 and insulin resistance.Miscellaneous: Variants Arg-84 and Ser-90 show impaired formation of HMW complexes whereas variants Cys-112 and Thr-164 show impaired secretion of adiponectin in any form.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 By similarity. In type 2 diabetic patients, both the ratios of HMW to total adiponectin and the degree of adiponectin glycosylation are significantly decreased as compared with healthy controls.Sequence similarities: Contains 1 C1q domain.Contains 1 collagen-like domain.