ADIPOQ Antibody - #DF7000

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Product: ADIPOQ Antibody
Catalog: DF7000
Description: Rabbit polyclonal antibody to ADIPOQ
Application: WB IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 28kDa; 26kD(Calculated).
Uniprot: Q15848
RRID: AB_2838956

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 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

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Related Downloads
MS Report
HPLC Report
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(83%), Bovine(89%), Horse(94%), Sheep(83%), Rabbit(89%), Dog(94%), Chicken(83%)
Clonality:
Polyclonal
Specificity:
ADIPOQ Antibody detects endogenous levels of total ADIPOQ.
RRID:
AB_2838956
Cite Format: Affinity Biosciences Cat# DF7000, RRID:AB_2838956.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

30 kDa adipocyte complement related protein; 30 kDa adipocyte complement-related protein; ACDC; ACRP30; ADIPO_HUMAN; Adipocyte; Adipocyte C1q and collagen domain containing protein; Adipocyte complement related 30 kDa protein; Adipocyte complement related protein of 30 kDa; Adipocyte complement-related 30 kDa protein; adipocyte-specific secretory protein; Adiponectin; Adiponectin precursor; adiponectin, C1Q and collagen domain containing; Adipoq; Adipose most abundant gene transcript 1; Adipose most abundant gene transcript 1 protein; Adipose specific collagen like factor; ADIPQTL1; ADPN; APM 1; apM-1; APM1; C1q and collagen domain-containing protein; GBP28; Gelatin binding protein; Gelatin binding protein 28; Gelatin-binding protein;

Immunogens

Immunogen:
Uniprot:

Q15848(ADIPO_HUMAN) >>Visit HPA database.

Gene(ID):
ADIPOQ(9370)
Expression:
Q15848 ADIPO_HUMAN:

Synthesized exclusively by adipocytes and secreted into plasma.

Description:
Adiponectin, also termed AdipoQ, Acrp30, apM1 and GBP28, is an adipokine expressed exclusively in brown and white adipocytes (1). It is secreted into the blood and exists in three major forms: a low molecular weight trimer, a medium molecular weight hexamer and a high molecular weight multimer (1). Adiponectin levels are decreased in obese and insulin-resistant mice and humans (2), suggesting that this adipokine is critical to maintain insulin sensitivity. Adiponectin stimulates the phosphorylation of AMPKα at Thr172 and activates AMPK in skeletal muscle (3). It also stimulates glucose uptake in myocytes (3). The block of AMPK activation by a dominant-negative AMPKα2 isoform inhibits the effect of adiponectin on glucose uptake, indicating that adiponectin stimulates glucose uptake and increases insulin sensitivity through its action on AMPK (3). Adiponectin mutants that are not able to form oligomers larger than trimers have no effect on the AMPK pathway (4). Mutations that render adiponectin unable to form high molecular weight multimers are associated with human diabetes (4), indicating the importance of multimerization for adiponectin activity.
Sequence:
MLLLGAVLLLLALPGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGEKGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKDVKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGERNGLYADNDNDSTFTGFLLYHDTN

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Horse
94
Dog
94
Bovine
89
Rabbit
89
Pig
83
Sheep
83
Chicken
83
Xenopus
72
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q15848 As Substrate

Site PTM Type Enzyme
T21 O-Glycosylation
T22 O-Glycosylation
S174 Phosphorylation
T235 Phosphorylation

Research Backgrounds

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.

PTMs:

HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagen-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.

Succination of Cys-36 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits polymerization and secretion of adiponectin. Adiponectin is a major target for succination in both adipocytes and adipose tissue of diabetic mammals. It was proposed that succination of proteins is a biomarker of mitochondrial stress and accumulation of Krebs cycle intermediates in adipose tissue in diabetes and that succination of adiponectin may contribute to the decrease in plasma adiponectin in diabetes.

Subcellular Location:

Secreted.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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 is also modulated by the degree of 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).

Family&Domains:

The C1q domain is commonly called the globular domain.

Research Fields

· Environmental Information Processing > Signal transduction > AMPK signaling pathway.   (View pathway)

· Human Diseases > Endocrine and metabolic diseases > Type II diabetes mellitus.

· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).

· Organismal Systems > Endocrine system > PPAR signaling pathway.

· Organismal Systems > Aging > Longevity regulating pathway.   (View pathway)

· Organismal Systems > Endocrine system > Adipocytokine signaling pathway.

References

1). Single xenotransplant of rat brown adipose tissue prolonged the ovarian lifespan of aging mice by improving follicle survival. Aging Cell, 2019 (PubMed: 31389140) [IF=7.8]

Application: WB    Species: mouse    Sample: lung

FIGURE 1|Rat‐to‐mouse (RTM) xenotransplanted brown adipose tissue (BAT) was functional well and did not cause injurious histocompatibility in aging mice.(h) HLA‐A blot showed that HLA‐A level in BAT of RTM and MTM groups was significantly higher than aging or young group; HLA‐A level in the lung of young group is significantly low; HLA‐A levels in other main tissues (liver,spleen, brain, kidney, heart) are similar among all four groups.
2). Aerobic Exercise Prevents Arterial Stiffness and Attenuates Hyperexcitation of Sympathetic Nerves in Perivascular Adipose Tissue of Mice after Transverse Aortic Constriction. International Journal of Molecular Sciences, 2022 (PubMed: 36232489) [IF=5.6]

Application: WB    Species: Mouse    Sample:

Figure 5 Effects of exercise on the expressions of β3-AR and adiponectin in PVAT of mice after TAC. Representative Western blot assessment of β3-AR (A) and adiponectin (B) expressions in PVAT normalized to the expressions of GAPDH. Data were analyzed using one-way ANOVA; values are mean ± SD. * indicates p < 0.05. Abbreviations: β3-AR, β3-adrenergic receptor; SHAM, sham surgery; TAC-SE, transverse aortic constriction-sedentary; and TAC-EX, transverse aortic constriction-exercise.
3). Autologous decellularized extracellular matrix promotes adipogenic differentiation of adipose derived stem cells in low serum culture system by regulating the ERK1/2-PPARγ pathway. Adipocyte, 2021 (PubMed: 33825675) [IF=3.3]

Application: WB    Species: Human    Sample: ADSCs

Figure 7. Effects of d-ECM on the ERK1/2-PPARγ pathway and the expression of adipocyte secreting factors ADIPOQ and aP2 in the fully differentiated ADSCs. After 3-days treatments and 14-days adipogenic induction, ADSCs at the 5th passage were collected and used for Western blotting analysis (a). Protein levels of ERK1/2 (b), p-ERK1/2 (c), PPARγ (d), p-PPARγ (e), ADIPOQ (f) and aP2 (g) were examined. GAPDH demonstrated the equal loading of protein samples. N = 3. *, p < 0.05, vs. 10% FBS group; **, p < 0.01, vs. 10% FBS group; #, p < 0.05, vs. 2% FBS group; ##, p < 0.01, vs. 2% FBS group; $, p < 0.05, vs. 2% FBS + d-ECM group; $$, p < 0.01, vs. 2% FBS + d-ECM group. ADIPOQ, adiponectin; aP2, adipocyte fatty-acid binding protein

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