Recombinant Mouse Angiopoietin-Like Protein 8 (ANGPTL8) Protein (His)

Name: Recombinant Mouse Angiopoietin-Like Protein 8 (ANGPTL8) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00383P
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-Like Protein 8 (ANGPTL8) 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.
Uniprotkb	Q8R1L8
Target Symbol	ANGPTL8
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	VRPAPVAPLGGPEPAQYEELTLLFAGALALGAALNGVYRATEARLTEAGHSLGLYDRALEFLGTEVRQGQDATQELRTSLSEIQVEEDALHLRAEATARSLGEVARAQQALRDTVRRLQVQLRGAWLGQAHQEFETLKARADKQSHLLWALTGHVQRQQREMAEQQQWLRQIQQRLHTAALPA
Expression Range	16-198aa(H40A,Q44A,Q47A)
Protein Length	Full Length of Mature Protein
Mol. Weight	21.3 kDa
Research Area	Others
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	Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels. May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state. According to a report, may act by promoting ANGPTL3 cleavage. According to another study, not required for cleavage of ANGPTL3.
Subcellular Location	Secreted.
Protein Families	ANGPTL8 family
Database References	KEGG: mmu:624219 STRING: 10090.ENSMUSP00000058951 UniGene: Mm.440264
Tissue Specificity	Expressed in liver and fat. Enriched in white and brown adipose tissues.

Gene Functions References

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
knock-down of Angptl8 in adipocytes suggests that the protein acts to inhibit intracellular lipolysis, analogous to its activity in the circulation. Depletion of Angptl8 results in an altered cellular phospholipid composition. The findings identify Angptl8 as a central insulin-regulated controller of adipocyte lipid metabolism. PMID: 28528274
The high levels of ANGPTL8 found in fetal life together with its relationship with newborn adiposity and brown adipose tissue point to ANGPTL8 as a potential new player in the modulation of the thermogenic machinery during the fetal-neonatal transition. PMID: 27469268
Obesity is associated with increased betatrophin suppression after an oral glucose load; this response appears to be driven by hyperglycemia. Data suggest that insulin or low glucose (as in hypoglycemia) increases betatrophin expression/secretion in adipocytes (3T3-L1 cells here); elevation of glucose levels blunts this effect. PMID: 27459526
circulating betatrophin is increased in mice and humans with NAFLD and its expression was induced by endoplasmic reticulum stress in hepatocytes PMID: 27045862
The expression of betatrophin is upregulated in the liver, white adipose tissue (WAT) and brown adipose tissue in obese hyperinsulinemic type 2 diabetes but decreased in WAT in hypoinsulinemic type 1 diabetes, suggesting its positive correlation with body weight and plasma insulin but not blood glucose. PMID: 27097546
This model suggests a general mechanism by which TAG trafficking is coordinated by lipasin, Angptl3 and Angptl4 at different nutritional statuses. PMID: 26687026
ANGPTL8 is a stress-response protein that down-regulates expression of ATGL. PMID: 26569053
no substantial change in beta cell replication, mass or glucose homeostasis was observed following ANGPTL8 overexpression PMID: 25917759
A monoclonal antibody against Angptl8, a feeding-induced hepatokine, lowers serum triglyceride levels when injected into mice. Angptl8 inhibits the activity of lipoprotein lipase in cardiac and skeletal muscle, but not in white adipose tissue. Therefore, Angptl8 acts, at least in part, in an endocrine manner, and its inhibition has therapeutical potential in treating hypertriglyceridemia. PMID: 26687026
ANGPTL8 is not required for beta cell function or the compensatory beta cell growth response to insulin resistance, overexpression of ANGPTL8 does not increase beta cell area nor improve glycemic control, and ANGPTL8 regulates plasma triglyceride levels. PMID: 25417115
Mice lacking ANGPTL8 (Betatrophin) manifest disrupted triglyceride metabolism without impaired glucose homeostasis. PMID: 24043787
These results suggest Lipasin and some ANGPTLs play distinct physiological roles in mediating thermogenesis and energy homeostasis. PMID: 23261442
Lipasin is a novel but atypical member of the angiopoietin-like protein family. PMID: 23261442
Lipasin is thus a novel nutritionally-regulated liver-enriched factor that plays a role in lipid metabolism. PMID: 22809513
RIFL is an important new regulator of lipid metabolism. PMID: 22569073

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.