Anti-Adiponectin antibody (AA26774)

$187.00


Alternative names Adiponectin, 30 kDa adipocyte complement-related protein, Adipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein, ADIPOQ, ACDC, APM1, GBP28, ADIPO_HUMAN, Q15848, 9370
Source 244
Species Reactivity Human, Mouse, Rat
Applications IHC, WB
Host Rabbit
Class Polyclonal
Conjugated Unconjugated


Description

Product name Anti-Adiponectin antibody (AA26774)
Catalog number AA26774
Brand family Ango
Product type Primary Antibody
Antibody Alternative Names Adiponectin antibody, 30 kDa adipocyte complement-related protein antibody, Adipocyte complement-related 30 kDa protein antibody, ACRP30 antibody, Adipocyte, C1q and collagen domain-containing protein antibody, Adipose most abundant gene transcript 1 protein antibody, apM-1 antibody, Gelatin-binding protein antibody, ADIPOQ antibody, ACDC antibody, APM1 antibody, GBP28 antibody, ADIPO_HUMAN antibody


Biological Information

Immunogen Recombinant protein of human ADIPOQ
Concentration 1 mg/ml
Isotype IgG
Application Notes WB 1:500 - 1:2000 IHC 1:50 - 1:200
Purification method Purified by affinity chromatography


Target

Target Name Adiponectin
SwissProt ID Link Q15848
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.
Subcellular Location Secreted.
Involvement in Disease Adiponectin deficiency: A condition that results in very low concentrations of plasma adiponectin. The disease is caused by mutations affecting the gene represented in this entry. Diabetes mellitus, non-insulin-dependent: A multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Disease susceptibility is associated with variations affecting the gene represented in this entry.
Post-Translational Modification Hydroxylated Lys-33 was not identified in PubMed:16497731, 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. O-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.
Tissue Specificity Synthesized exclusively by adipocytes and secreted into plasma.
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 CTRP9A via the C1q domain (heterotrimeric complex).
Sequence Similarities Contains 1 C1q domain. Contains 1 collagen-like domain.


Poduct Presentation

Form Liquid
Preservative 0.02% (w/v) sodium azide
Storage buffer PBS with 50% glycerol, pH 7.3


Storage and Shipping Information

Storage Store at -20 or -80 C. Avoid multiple freeze/thaw cycles.