Human Recombinant ANGPTL4 protein, hFc Tag (V2LY-0526-LY2119)

Name: Human Recombinant ANGPTL4 protein, hFc Tag
SKU: V2LY-0526-LY2119
Rating: 5 (1 reviews)

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Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Human

Tag

hFc Tag

Protein Construction

This product is Human Recombinant ANGPTL4 protein, hFc Tag consist of Amino Acid: 166-406 and predicts a molecular mass of 55.5 kDa.

Molecule Mass

55.5 kDa

Sequence

Amino Acid: 166-406

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity

>92% as determined by SDS-PAGE

Endotoxin

Please contact us for more information.

Format

Lyophilized

Reconstitution

Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.

Buffer

Lyophilized from sterile Tris, NaCl, TCEP, Glycerol

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

angiopoietin-like 4

Function

Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17068295). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (PubMed:17068295). Depending on context, may modulate tumor-related angiogenesis (By similarity).
ANGPTL4 N-terminal chain: Mediates inactivation of the lipoprotein lipase LPL, and thereby plays an important role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). Has higher activity in LPL inactivation than the uncleaved protein (PubMed:19270337, PubMed:21398697).

Biological Process

Angiogenesis Source: UniProtKB-KW
Lipid metabolic process Source: UniProtKB-KW
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of endothelial cell apoptotic process Source: Ensembl
Negative regulation of lipoprotein lipase activity Source: BHF-UCL
Positive regulation of angiogenesis Source: UniProtKB
Protein unfolding Source: ARUK-UCL
Regulation of metabolic process Source: Reactome
Response to hypoxia Source: UniProtKB
Triglyceride homeostasis Source: BHF-UCL

Cellular Location

Secreted; Extracellular matrix. The unprocessed form interacts with the extracellular matrix (PubMed:17068295, PubMed:21398697). This may constitute a dynamic reservoir, a regulatory mechanism of the bioavailability of ANGPTL4 (Probable).

PTM

N-glycosylated.
ANGPTL4 N-terminal chain: Forms disulfide-linked dimers and tetramers.
Cleaved into a smaller N-terminal chain and a larger chain that contains the fibrinogen C-terminal domain; both cleaved and uncleaved forms are detected in the extracellular space. The cleaved form is not present within the cell.

Sodhi, A., Ma, T., Menon, D., Deshpande, M., Jee, K., Dinabandhu, A., ... & Montaner, S. (2019). Angiopoietin-like 4 binds neuropilins and cooperates with VEGF to induce diabetic macular edema. The Journal of clinical investigation, 129(11), 4593-4608.

Theofilatos, D., Fotakis, P., Valanti, E., Sanoudou, D., Zannis, V., & Kardassis, D. (2018). HDL-apoA-I induces the expression of angiopoietin like 4 (ANGPTL4) in endothelial cells via a PI3K/AKT/FOXO1 signaling pathway. Metabolism, 87, 36-47.

Dijk, W., Ruppert, P. M., Oost, L. J., & Kersten, S. (2018). Angiopoietin-like 4 promotes the intracellular cleavage of lipoprotein lipase by PCSK3/furin in adipocytes. Journal of Biological Chemistry, 293(36), 14134-14145.

Zhang, T., Kastrenopoulou, A., Larrouture, Q., Athanasou, N. A., & Knowles, H. J. (2018). Angiopoietin-like 4 promotes osteosarcoma cell proliferation and migration and stimulates osteoclastogenesis. BMC cancer, 18(1), 1-10.

Dijk, W., Schutte, S., Aarts, E. O., Janssen, I. M., Afman, L., & Kersten, S. (2018). Regulation of angiopoietin-like 4 and lipoprotein lipase in human adipose tissue. Journal of clinical lipidology, 12(3), 773-783.

Janssen, A. W., Katiraei, S., Bartosinska, B., Eberhard, D., van Dijk, K. W., & Kersten, S. (2018). Loss of angiopoietin-like 4 (ANGPTL4) in mice with diet-induced obesity uncouples visceral obesity from glucose intolerance partly via the gut microbiota. Diabetologia, 61(6), 1447-1458.

Yang, X., Cheng, Y., & Su, G. (2018). A review of the multifunctionality of angiopoietin-like 4 in eye disease. Bioscience reports, 38(5).

Cushing, E. M., Chi, X., Sylvers, K. L., Shetty, S. K., Potthoff, M. J., & Davies, B. S. (2017). Angiopoietin-like 4 directs uptake of dietary fat away from adipose during fasting. Molecular metabolism, 6(8), 809-818.

McQueen, A. E., Kanamaluru, D., Yan, K., Gray, N. E., Wu, L., Li, M. L., ... & Wang, J. C. (2017). The C-terminal fibrinogen-like domain of angiopoietin-like 4 stimulates adipose tissue lipolysis and promotes energy expenditure. Journal of Biological Chemistry, 292(39), 16122-16134.

Cara-Fuentes, G., Segarra, A., Silva-Sanchez, C., Wang, H., Lanaspa, M. A., Johnson, R. J., & Garin, E. H. (2017). Angiopoietin-like-4 and minimal change disease. PloS one, 12(4), e0176198.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

Alternative Versions

Human Recombinant ANGPTL4 protein, His Tag (CAT#: V2LY-0526-LY2120)

Mouse Recombinant ANGPTL4 protein, His Tag (CAT#: V2LY-0526-LY7811)

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Isotype control

For research use only. Not intended for any clinical use.

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