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A0725-02 Acrp30, NT, Mouse, Control Peptide (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28) CAS:

Specifications
References
Grade
Highly Purified
Specificity
Synthetic peptide 15aa sequence near the N-terminus of mature mouse Acrp30. No significant sequence similarity with the related protein C1q. Does not detect truncated, proteolytically cleaved gAcrp30. Species Sequence Homology: No significant sequence homology with human and rat. Refer to Cat# A0725-02A, A0725-25, A0725-50 for human Acrp30.
Applications
E
EU Commodity Code
38220090
Shipping Temp
Blue Ice
Storage Temp
-20°C

Control Peptide for A0725 (antiserum) and A0725-01 (affinity purified antibody).

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; and 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, Antibody Blocking. Not suitable for use in Western Blot. Other applications not tested.
Recommended Dilution
ELISA: 1:10,000-1:50,000. Coat plates at 10-100ng of Control Peptide/well. Antibody Blocking: 5-10ug per 1ul A0725 (antiserum) or per 1ug A0725-01 (affinity purified antibody). Optimal dilutions to be determined by the researcher.
Control Peptide: A0725-02
MW
Full length Acrp30: ~30kD. Recombinant Acrp30: ~37kD gAcrp30: ~16kD.
Storage and Stability
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 6 months at -20°C. 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.
Human Acrp30
A0725-02A: Acrp30 (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28) Pab Rb xHu A0725-25: Acrp30 (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28) Pab Rb xHu A0725-50: Acrp30, Human, Control Peptide (Adipocyte Complement-related Protein of 30kD, Adiponectin, AdipoQ, apM1, Gelatin Binding Protein 28, GPB28)
Source
Mouse, synthetic peptide
Purity
Highly purified
Concentration
~1mg/ml
Form
Supplied as a liquid in PBS, pH 7, 0.05% sodium azide.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
References
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.
USBio References
No references available
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