Recombinant Mouse Apolipoprotein C-Iii (APOC3) Protein (His-SUMO)

Name: Recombinant Mouse Apolipoprotein C-Iii (APOC3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03122P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Apolipoprotein C-Iii (APOC3) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P33622
Target Symbol	APOC3
Synonyms	Apoc3Apolipoprotein C-III; Apo-CIII; ApoC-III; Apolipoprotein C3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	EEVEGSLLLGSVQGYMEQASKTVQDALSSVQESDIAVVARGWMDNHFRFLKGYWSKFTDKFTGFWDSNPEDQPTPAIES
Expression Range	21-99aa
Protein Length	Full Length of Mature Protein
Mol. Weight	24.9kDa
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	Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. Plays a multifaceted role in triglyceride homeostasis. Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors. Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners.
Subcellular Location	Secreted.
Protein Families	Apolipoprotein C3 family
Database References	KEGG: mmu:11814 STRING: 10090.ENSMUSP00000034586 UniGene: Mm.390161

Gene Functions References

Both triglyceride-rich lipoproteins (TRLs) and ApoCIII contribute to the progression of atherosclerosis, and the modulation of TRLs and ApoCIII may represent a novel therapeutic approach against hypertriglyceridemia induced atherosclerosis. PMID: 30223835
C3(QK) variant is a gain-of-function mutation that can stimulate VLDL1 production, through enhanced DNL PMID: 28887372
intestinal apoC-III overexpression results in the secretion of smaller, less dense chylomicron particles along with reduced triacylglycerol secretion from the intestine PMID: 28159868
ApoC-III inhibits turnover of TG-rich lipoproteins primarily through a hepatic clearance mechanism mediated by the LDLR/LRP1 axis PMID: 27400128
These data strongly suggest that intestinal apoC-III is not a FoxO1 target and support the idea that apoC-III is not regulated coordinately with hepatic apoC-III, and establishes another key aspect of apoC-III that is unique in the intestine from the liver. PMID: 28739253
APOC3, whose dysregulation is liable for hypertriglyceridemia, is not a predisposing factor for linking overnutrition to NAFLD in obesity PMID: 28115523
Severe hypertriglyceridaemia resulting from ApoCIII overexpression promotes restenosis and atherosclerosis PMID: 26160324
Under conditions of islet insulin resistance, locally produced apoCIII is an important diabetogenic factor involved in impairment of beta-cell function. PMID: 25941406
decreased ApoAI synthesis might be accounted for the lower plasma HDL level in ApoCIII transgenic mice PMID: 25969427
ApoCIII hyperactivates beta cell CaV1 channels through SR-BI/beta1 integrin-dependent coactivation of PKA and Src. PMID: 23949443
Increased plasma APOC3 concentrations predispose mice to diet-induced nonalcoholic fatty liver and hepatic insulin resistance. PMID: 21793029
Glucose induces apoCIII transcription, which may represent a mechanism linking hyperglycemia, hypertriglyceridemia, and cardiovascular disease in type 2 diabetes. PMID: 21183731
PGC-1beta regulates plasma triglyceride metabolism through stimulating apolipoprotein C3 (APOC3) expression and elevating APOC3 levels in circulation PMID: 20889132
The apoC-III metabolism may contribute to dyslipidemia in CKD, and this requires further investigation. PMID: 19542564
Association between SstI polymorphism of the gene, glucose intolerance and cardiovascular risk in renal transplant recipients PMID: 11959336
ApoB lipoproteins that contain apoCIII increase THP-1 cell adhesion to ECs via PKCalpha and RhoA-mediated beta1-integrin activation. PMID: 16461842
oxidized fatty acids may act through an APOA5/APOClll mechanism that contributes to lowering of TG levels other than PPAR* induction PMID: 18243209
the apoCIII enhancer contributes to the maintenance of an active chromatin subdomain of the apoAI/CIII/AIV genes, but not apoAV PMID: 18678879
These results suggest that apoC-III may play a specific role in lipid storage and mobilization in adipocytes, non-lipoprotein-secreting cells, and indicate the functional role of RXRalpha during adipocyte differentiation. PMID: 19121312

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.