Perilipin-2/ADFP Recombinant Protein Antigen Summary
Description |
A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human Perilipin-2/ADFP Source: E. coli
Amino Acid Sequence: ISQLHSTVHLIEFARKNVYSANQKIQDAQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLLSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNAASFKEVSDSLLTSSKGQ Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)
This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions. |
Source |
E. coli |
Protein/Peptide Type |
Recombinant Protein Antigen |
Gene |
PLIN2 |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Applications/Dilutions
Dilutions |
- Antibody Competition 10-100 molar excess
|
Application Notes |
This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP2-48532. It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml. For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com |
Theoretical MW |
32 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
Packaging, Storage & Formulations
Storage |
Store at -20C. Avoid freeze-thaw cycles. |
Buffer |
PBS and 1M Urea, pH 7.4. |
Preservative |
No Preservative |
Purity |
>80% by SDS-PAGE and Coomassie blue staining |
Alternate Names for Perilipin-2/ADFP Recombinant Protein Antigen
Background
Perilipin-2/Plin-2, also known as adipose differentiation-related protein (ADFP), ADRP, and adipophilin, is a member of the perilipin family of lipid droplet (LD) proteins that functions in lipid accumulation, lipid storage, and LD formation (1,2). Perilipin-2 is ubiquitously expressed and is the major LD protein of the liver (1-3). Human perilipin-2 is 437 amino acids (aa) in length with a theoretical molecular weight of 48 kDa (1,4). Human and mouse perilipin-2 share 81.8% sequence identity. One defining structural feature of perilipin-2 and other LD-related proteins is formation of amphipathic alpha helices (1,3,5). The perilipin-2 protein contains a PAT (perilipin A, ADRP, TIP47) domain, a 11-mer repeat motif, and a 4-helix bundle (1,5). The PAT domain has a role in triglyceride (TG) stabilization, the 11-mer repeat motif functions in cytoplasmic LD binding, and the 4-helix bundle facilitates membrane binding (5). Unlike LDs coated with other perilipin family members (e.g., perilipin-1 and perilipin-5), LDs coated with perilipin-2 are more permissive to lipolysis and protective of lipids and TGs (1-3). Studies have revealed that perilipin-2 knockout (KO) in mice is associated with resistance to fatty liver disease and diet-induced obesity (1). On the other hand, overexpression of perilipin-2 causes increased lipid and TG accumulation, which is a feature of many metabolic, cardiovascular, and age-related diseases (2). Additional research has found higher levels of perilipin-2 is associated with certain cancers such as colorectal cancer and renal carcinomas, and it may be a useful biomarker for detection (2). Though more research is needed, it is possible that inhibition or blocking of perilipin-2 may be a key strategy to combatting several pathologies (2).
References
1. Itabe H, Yamaguchi T, Nimura S, Sasabe N. Perilipins: a diversity of intracellular lipid droplet proteins. Lipids Health Dis. 2017;16(1):83. https://doi.org/10.1186/s12944-017-0473-y
2. Conte M, Franceschi C, Sandri M, Salvioli S. Perilipin 2 and Age-Related Metabolic Diseases: A New Perspective. Trends Endocrinol Metab. 2016;27(12):893-903. https://doi.org/10.1016/j.tem.2016.09.001
3. Sztalryd C, Brasaemle DL. The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis. Biochim Biophys Acta Mol Cell Biol Lipids. 2017;1862(10 Pt B):1221-1232. https://doi.org/10.1016/j.bbalip.2017.07.009
4. Uniprot (Q99541)
5. Chong BM, Reigan P, Mayle-Combs KD, Orlicky DJ, McManaman JL. Determinants of adipophilin function in milk lipid formation and secretion. Trends Endocrinol Metab. 2011;22(6):211-217. https://10.1016/j.tem.2011.04.003
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are
guaranteed for 3 months from date of receipt.
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