Technical Data
A0725-02A
Acrp30 (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28)
Description:
Adipose tissue is the largest reservoir of fuel, storing energy in the form of rapidly utilizable triglycerides. Adipocytes synthesize and store energy in periods of nutritional abundance and mobilize lipids during starvation and other times of need. In order to accomplish these complex tasks of energy balance, adipocytes express many genes, including Acrp30 which is involved in lipid metabolism and glucose homeostasis.

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. It is a 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. 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 91-14aa); followed by a 27aa unique region; followed by 22 perfect Gly-X-Pro or Gly-X-X collagen like repeats; a globular segment at the C-terminus. Structurally, at the sequence level, Acrp30 resembles other collagen-like and globular domain proteins (lung surfactant protein and hepatocytes mannan-binding proteins). Acrp30 is 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. A marked reduction in plasma triglycerides, glucose and free fatty acids was attributed due in part to increased fatty acid oxidation by muscle. Full length Acrp30 was less potent than gAcrp30. Therefore, gAcrp30 may open new avenues to control obesity.

Applications:
Suitable for use in ELISA, Western Blot. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000-1:5000 (ECL).
ELISA: 1:10,000-50,000. Coat plate with 10-100ng of control peptide/well.
Optimal dilutions to be determined by the researcher.

Control Peptide:
A0725-50: Acrp30, Human, Control Peptide (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28)
A0725-50A: Acrp30, Human, Western Blot Control (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28)

Molecular Weight:
Full length Acrp30: ~30kD.
Recombinant Acrp30: ~37kD
gAcrp30:~16kD.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. 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.

Related Products:
A0725: Acrp30 Pab Rb xMo (antiserum)
A0725-01: Acrp30 Pab Rb xMo (affiniity purified antibody)
A0725-02: Acrp30, Mouse (Control Peptide)
TypeIsotypeCloneGrade
PabIgGSerum
SizeStorageShippingSourceHost
100ul-20CBlue IceHumanRabbit
Concentration:
As reported
Immunogen:
Synthetic peptide 20aa sequence near the N-terminus of mature human Acrp30 (KLH coupled).
Purity:
Serum
Form
Supplied as a liquid, neat serum, 0.05% sodium azide, 40% glycerol.
Specificity:
Recognizes Adipocyte Complement-Related Protein of 30kD. Does not detect truncated, proteolytically cleaved gAcrp30. No significant sequence similarity with the related protein C1q. Species Sequence Homology: Does not crossreact with mouse or rat. Human sequence is not well conserved in mouse or rat Acrp30. Refer to cat# A0725, A0725-01, A0725-02 for mouse Acrp30 related products.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Scherer, P.E., et al. (1995) JBC 270: 26746. 2. Hu, E., et al. (1996) JBC 271: 10697. 3. Das, K., et al. (2001) BBRC 280: 1120. 4. Fruebis, J., et al. (2001) PNAS 98: 2005. 5. Maeda, K., et al. (1996) BBRC 221: 286. 6. Schaffler, A., et al. (1998) BBA 1399: 187. 7. Schaffler, A., et al. (1999) BBRC 260: 416.