Review





Similar Products

full-length angptl3 produced in hek293 cells  (ProSpec)
90
ProSpec full-length angptl3 produced in hek293 cells
Full Length Angptl3 Produced In Hek293 Cells, supplied by ProSpec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full-length+angptl3/human+embryonic+kidney+cell+line++hek293/pmc05148603-281-4-9
Average 90 stars, based on 1 article reviews
full-length angptl3 produced in hek293 cells - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
full-length angptl3  (ProSpec)
90
ProSpec full-length angptl3
Panel A shows a sequence alignment of the first 55 residues of fully processed human <t>ANGPTL3,</t> ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012
Full Length Angptl3, supplied by ProSpec, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full-length+angptl3/human+embryonic+kidney+cell+line++hek293/pmc05148603-281-0-9
Average 90 stars, based on 1 article reviews
full-length angptl3 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
full-length angptl3  (Adipogen)
90
Adipogen full-length angptl3
Panel A shows a sequence alignment of the first 55 residues of fully processed human <t>ANGPTL3,</t> ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012
Full Length Angptl3, supplied by Adipogen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full-length+angptl3/angptl3+elisa+test+kit/pm25338813-55-0-7
Average 90 stars, based on 1 article reviews
full-length angptl3 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
full-length cdna sequences encoding angptl3  (Liuyang SANLI Medical Technology Development)
90
Liuyang SANLI Medical Technology Development full-length cdna sequences encoding angptl3
Panel A shows a sequence alignment of the first 55 residues of fully processed human <t>ANGPTL3,</t> ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012
Full Length Cdna Sequences Encoding Angptl3, supplied by Liuyang SANLI Medical Technology Development, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full-length+angptl3/full+length+cdna+sequences+encoding+angptl3/10__1016_slash_S2095___3119_ascii40_12_ascii41_60113___0-60-8-17
Average 90 stars, based on 1 article reviews
full-length cdna sequences encoding angptl3 - by Bioz Stars, 2026-11
90/100 stars
  Buy from Supplier
full length human angptl3 cdna  (TaKaRa)
86
TaKaRa full length human angptl3 cdna
Panel A shows a sequence alignment of the first 55 residues of fully processed human <t>ANGPTL3,</t> ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012
Full Length Human Angptl3 Cdna, supplied by TaKaRa, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/full-length+angptl3/10__1074_slash_jbc__m203215200-66-2-12
Average 86 stars, based on 1 article reviews
full length human angptl3 cdna - by Bioz Stars, 2026-11
86/100 stars
  Buy from Supplier

Image Search Results


Panel A shows a sequence alignment of the first 55 residues of fully processed human ANGPTL3, ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012

Journal: eLife

Article Title: The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

doi: 10.7554/eLife.20958

Figure Lengend Snippet: Panel A shows a sequence alignment of the first 55 residues of fully processed human ANGPTL3, ANGPTL4, and ANGPTL8. Identical sequences are highlighted by blue letters. The filled red box highlights the two-residue acidic motif at the start of the N-terminal α-helix, followed by a conserved α-helical region (open box). The two cysteine residues unique to ANGPTL4 are shown in yellow boxes. Panel B shows the time-dependent unfolding of 10 µM LPL by 1 µM ANGPTL3 ( green circles ) as defined by the appearance of bimodality in the isotope envelopes for peptide 131–165. For comparison the unfolding of LPL by 1 µM ANGPTL4 1–159 is shown as solid (wild-type) and hatched (E15K) gray lines. Spontaneous unfolding is shown by black triangles. Panel C shows the residual lipolytic activity of 10 µM LPL incubated for 10 min alone or in the presence of 1 µM ANGPTL3, 1 µM ANGPTL3 and 30 µM GPIHBP1, or 1 µM ANGPTL4 1–159 . DOI: http://dx.doi.org/10.7554/eLife.20958.012

Article Snippet: Full-length ANGPTL3 produced in HEK293 cells was purchased from ProSpec (Ness-Ziona, Israel).

Techniques: Sequencing, Residue, Comparison, Activity Assay, Incubation