ELISA with Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein 5206

Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein 5206

$525.00 – $1,750.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ser17-Lys219

SKU: 5206parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C‑terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake.
molecular weight	The protein has a predicted MW of 26.6 kDa. Due to glycosylation, the protein migrates to 30-38 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein 5206

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
ANGPTL3 is a secreted glycoprotein that is structurally related to the angiopoietins. Mature human ANGPTL3 contains an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development through adulthood. Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake.
Protein names Angiopoietin-related protein 3 (Angiopoietin-5) (ANG-5) (Angiopoietin-like protein 3) [Cleaved into: ANGPTL3(17-221); ANGPTL3(17-224)]
Gene names ANGPTL3,ANGPTL3 ANGPT5 UNQ153/PRO179
Mass 9606Da
Function Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity).; [ANGPTL3(17-221)]: In vitro inhibits LPL activity; not effective on GPIHBP1-stabilized LPL.; Involved in angiogenesis. Binds to endothelial cells via integrin alpha-V/beta-3 (ITGAV:ITGB3), activates FAK, MAPK and Akt signaling pathways and induces cell adhesion and cell migration (PubMed:11877390). Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling (PubMed:18535744). May increase the motility of podocytes. May induce actin filament rearrangements in podocytes implicating integrin alpha-V/beta-3 and Rac1 activation. Binds to hematopoietic stem cells (HSC) and is involved in the regulation of HSC activity probably implicating down-regulation of IKZF1/IKAROS (By similarity).
Subellular location Secreted. Cell projection, lamellipodium. Note=Colocalized with HSPG2 and activated ITGB3 on podocytes.
Tissues Expressed principally in liver. Weakly expressed in kidney. Binds to adipocytes. Increased expression and colocalization with activated ITGB3 in glomeruli of patients with nephrotic syndrome showing effaced podocyte foot processes (at protein level).
Structure Interacts with ANGPTL8. Interacts with ITGB3 (By similarity).
Post-translational modification O-glycosylated at Thr-226 by GALNT2; blocks processing and activation by proprotein convertases.; In part proteolytically cleaved by proprotein convertases; proposed to be involved in activation.
Domain Th
Target Relevance information above includes information from UniProt accession: Q9Y5C1
The UniProt Consortium

Data

ELISA with Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein

Immobilized Anti-ANGPTL3 Antibody, hFc Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human ANGPTL3, His Tag with the EC50 of 10.2ng/ml determined by ELISA.

HPLC of Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein

The purity of Biotinylated Human ANGPTL3 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Human ANGPTL3/Angiopoietin-like 3 Protein

Biotinylated Human ANGPTL3 on Tris-Bis PAGE under reduced conditions. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.