Human globular ACRP-30 (AF)
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| Amount : | 100 µg |
| Purification : | Reducing and Non-Reducing SDS PAGE at >= 90% |
| Content : | Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM Tris, 0.75 mM DTT, pH 8.0 Sterile 5 mM Tris and 0.75 mM DTT, pH 8 at 0.1 mg/mL |
| Storage condition : | Store at -20°C |
| AA sequence : | Â MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN |
Source: Genetically modified E.coli.
Predicted MW: Monomer, 16.7 kDa (145 aa)
The globular subunit of adipocyte complement-related protein of 30 kDa (ACRP-30) is a naturally occurring cleavage product of adiponectin, a protein made exclusively by adipocytes. ACRP-30 is an abundant serum protein and plays an important role in hyperglycemia, insulin resistance, and fatty acid oxidation. ACRP-30 signals through adiponectin receptor 1 (AdipoR1) and adiponectin receptor 2 (AdipoR2).
Endotoxin: Less than 0.5 ng/µg (1 IEU/µg) as determined by LAL test.
Biological Activity was determined by Bioactive protein. Centrifuge vial before opening, Suspend the product by gently pipetting the above recommended solution down the sides of the vial. DO NOT VORTEX. Allow several minutes for complete reconstitution. For prolonged storage, dilute to working aliquots in a 0.1% BSA solution, store at -80°C and avoid repeat freeze thaws. Upon reconstitution, a small amount of visible precipitate can be expected. A 10% overfill has been added to the total material vialed to compensate for this loss.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Secreted |
| Post transnational modification: | 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. |
| BioGrid: | 114771. 22 interactions. |
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