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Manufactured by BioVendor

Angiopoietin-Like Protein 3 Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:Angiopoietin-related protein 3, Angiopoietin-5, ANG-5, ANGPT5, UNQ153/PRO179, ANGPTL-3
  • Species:Human
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Cat. No. Size Price


RD172092050-HEK 0.05 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 450 AA. MW: 52.6 kDa (calculated). UniProtKB acc. No. Q9Y5C1 (Ser17-Glu460). C-terminal His-Tag (6 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

SRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFEHHHHHH

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

14 % SDS-PAGE separation of Human ANGPTL3 :
1. MW marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5 μg/lane
3. non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 0.1 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized in 0.5 mg/mL in 0.05 M phosphate buffer, 0.075 M NaCl, pH 7.4

Reconstitution

Add deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Filter your culture media/working solutions containing this product before using in cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Energy metabolism and body weight regulation, Oncology

Summary

Angiopoietin-like proteins ANGPTL3 and ANGPTL4 are secreted proteins mainly expressed in liver that have been demonstrated to regulate triglyceride metabolism by inhibiting the lipolysis of triglyceride-rich lipoproteins. ANGPTL3 is structurally similar to angiopoietins, which are vascular endothelial growth factors. The experimental results show that Angptl3 and Angptl4 function to regulate circulating triglyceride levels during different nutritional states and therefore play a role in lipid metabolism during feeding/fasting through differential inhibition of Lipoprotein lipase (LPL). Using deletion mutants of human ANGPTL3, it was demonstrated that the N-terminal domain containing fragment – (17–207) and not the C-terminal fibrinogen-like domain containing fragment – (207–460) increased the plasma triglyceride levels in mice. The fasting-induced adipose factor (FIAF, ANGPTL4, PGAR, HFARP) was identified as an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. At the protein level, in human and mouse blood plasma, FIAF was found to be present both as a native protein and in a truncated form. Differentiation of mouse 3T3-L1 adipocytes was associated with the production of truncated FIAF, whereas in human white adipose tissue and SGBS adipocytes, only the native FIAF could be detected. Interestingly, the truncated FIAF was produced by human liver. Experimental data suggest that FIAF is mainly presented in human blood plasma in a truncated form (FIAF-S2), whose level is increased by fenofibrate treatment. Levels of both truncated and native FIAF showed marked inter individual variation but were not associated with body mass index and were not influenced by prolonged semistarvation.

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