Recombinant Mouse Angiopoietin-Related Protein 3 (ANGPTL3) Protein (His)

Name: Recombinant Mouse Angiopoietin-Related Protein 3 (ANGPTL3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00132P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins, Recombinant proteins fall special offers - full-length proteins

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Product Overview

Description	Recombinant Mouse Angiopoietin-Related Protein 3 (ANGPTL3) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q9R182
Target Symbol	ANGPTL3
Synonyms	(Angiopoietin-like protein 3)(17-224)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SRVDPDLSSFDSAPSEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKTGIQEPSENSLSSKSRAPRTTPPLQLNETENTEQDDLPADCSAVYNRGEHTSGVYTIKPRNSQGFNVYCDTQSGSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLEKIYAIVQQSNYILRLELQDWKDSKHYVEYSFHLGSHETNYTLHVAEIAGNIPGALPEHTDLMFSTWNHRAKGQLYCPESYSGGWWWNDICGENNLNGKYNKPRTKSRPERRRGIYWRPQSRKLYAIKSSKMMLQPTT
Expression Range	17-455aa
Protein Length	Full Length of Mature Protein
Mol. Weight	54.8 kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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. Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity; the function seems to be specific for the feeding conditions. 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. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids; the cleaved N-terminal domain is more efficient than the uncleaved proprotein. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol. 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. 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.; 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. May increase the motility of podocytes. Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling. 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.
Subcellular Location	Secreted. Cell projection, lamellipodium.
Database References	KEGG: mmu:30924 STRING: 10090.ENSMUSP00000030280 UniGene: Mm.28341
Tissue Specificity	Predominantly expressed in liver, weakly expressed in kidney and lung. Expressed in podocytes (at protein level). Expressed in hypothalamic neurons (at protein level). Expressed in bone marrow sinusoidal endothelial cells (at protein level).

Gene Functions References

The role of ANGPLT3 in controlling lipoprotein metabolism and risk of cardiovascular diseases is reviewed here. PMID: 29334984
ANGPTL8 has a functional LPL inhibitory motif, but only inhibits LPL and increases plasma TG levels in mice in the presence of ANGPTL3 PMID: 28413163
The data suggests that ANGPTL3 is part of the machinery causing dyslipidemia majorily via LPL inhibition in mastitis mice. PMID: 29104012
Using in vitro ketosis model by glucose starvation, studied inhibition of ketosis by momilactone B. Found momilactone B could regulate the angiopoietin-like-3 (ANGPTL3)-lipoprotein lipase (LPL)pathway, and suppressed the expression of HMGCS2 through the increased expression of STAT5b. PMID: 27874312
This model suggests a general mechanism by which TAG trafficking is coordinated by lipasin, Angptl3 and Angptl4 at different nutritional statuses. PMID: 26687026
Inactivation of ANGPTL3 reduces hepatic VLDL-triglyceride secretion PMID: 25954050
The deletion of ANGPTL3 tremendously attenuates proteinuria and protects podocytes from injury in a mouse model of adriamycin-induced nephropathy. PMID: 25710887
ANGPTL3 has a role in regulating white adipose tissue energy homeostasis but not in liver PMID: 26305978
Data indicate that expression of Angptl3 in hematopoietic stem cell (HSC) through lentiviral transduction promoted HSC expansion. PMID: 25170927
Angptl3 could induce actin filament rearrangement, mainly in lamellipodia formation, and that this process was mediated by integrin alpha(V)beta-mediated FAK and PI3K phosphorylation and Rac1 activation. PMID: 24294595
Furin has a role as the primary in vivo convertase of ANGPTL3 and endothelial lipase in hepatocytes PMID: 23918928
ANGPTL8, a paralog of ANGPTL3 that arose through duplication of an ancestral DOCK gene, regulates postprandial TAG and fatty acid metabolism by controlling activation of its progenitor, and perhaps other ANGPTLs PMID: 23150577
Angptl3, as an extrinsic factor, thus supports the stemness of hematopoietic stem cells in the bone marrow niche. PMID: 20959605
ANGPTL3 expression is upregulated in puromycin-induced podocyte damage and is associated with the reduction of perlecan and agrin expression PMID: 20424482
a molecular connection between ANGPTL3, lipoprotein lipase, and proprotein convertases PMID: 20581395
ANGPTL3 to be capable of regulating the motility and permeability of podocytes and that the mechanism of ANGPTL3's regulation could be associated with the altered expression of nephrin. PMID: 20633534
Like ANGPTL4, ANGPTL3 inhibited nonstabilized LPL but not GPIHBP1-stabilized LPL PMID: 19542565
ANGPTL3 stimulates endothelial cell adhesion and migration via integrin alpha vbeta 3 and induces blood vessel formation in vivo PMID: 11877390
affects VLDL triglyceride clearance by interfering with LPL activity PMID: 12097324
hepatic Angptl3 has a role in hypertriglyceridemia associated with the treatment of LXR ligand PMID: 12672813
the cleavage of ANGPTL3 at two sites is important for the activation of ANGPTL3 in vivo PMID: 12909640
Expression of ANGPTL3 was enhanced in both insulin-deficient and -resistant diabetic states; results strongly suggest ANGPTL3 to play an important role in hyperlipidemia in diabetes. PMID: 15094378
Elevated ANGPTL3 by leptin- or insulin-resistance is attributed to increased plasma triglycerides and free fatty acid levels in obesity. PMID: 15336575
Differential regulation of Angptl3 and Angptl4 by sites of expression, nutritional status, and ligands of nuclear receptors may confer unique roles of each in lipoprotein metabolism. Angptl3 is a target gene of liver X receptor PMID: 15863837
Angptl3-deficiecy displayed hypotriglyceridemia with elevated postheparin plasma lipoprotein lipase, with greater effect in fed state. Deficiecy in both Angptl proteins had additive effect on plasma triglycerides with survival not past 2 months of age. PMID: 16081640
Angptl3 acts as an inhibitor of EL and may be involved in the regulation of plasma HDL cholesterol and HDL-PL levels in humans and rodents. PMID: 17110602
SE1 region of ANGPTL3 and ANGPTL4 functions as a domain important for binding LPL and inhibiting its activity in vitro and in vivo. PMID: 19318355

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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