Recombinant Mouse Adropin (ENHO) Protein (His-KSI)

Name: Recombinant Mouse Adropin (ENHO) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-07085P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Mouse Adropin (ENHO) Protein (His-KSI) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8K1D8
Target Symbol	ENHO
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	CHSRSADVDSLSESSPNSSPGPCPEKAPPPQKPSHEGSYLLQP
Expression Range	34-76aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.8 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	Involved in the regulation of glucose homeostasis and lipid metabolism.
Subcellular Location	Secreted.
Database References	KEGG: mmu:69638 UniGene: Mm.372459
Tissue Specificity	Expressed in liver and brain. Expressed in regions of the brain involved in metabolic regulation.

Gene Functions References

Adropin prevents atherosclerosis development by suppressing monocyte-endothelial cell adhesion and smooth muscle cell proliferation. PMID: 29701665
An inverse correlation between serum adropin levels and mouse age that was attenuated by calorie restriction. PMID: 28922017
our data suggest that adropin is a membrane-bound protein that interacts with the brain-specific Notch1 ligand NB3. PMID: 25074942
these results suggest a role for adropin in regulating muscle substrate preference under various nutritional states. PMID: 24848071
Release of adropin in the fed condition regulates fuel selection in skeletal muscle, promoting glucose oxidation over fat oxidation. The molecular mechanisms of adropin's effects involve acetylation (suggesting inhibition) of the transcriptional co-activator PGC1alpha, reducing PDK4 and CPT1B activity. Increased PGC1alpha acetylation by adropin may be mediated by inhibiting Sirtuin-1 (SIRT1), a PGC1alpha deacetylase. PMID: 24848071
a potential endothelial protective role of adropin that is likely mediated via upregulation of endothelial NO synthase expression through the VEGFR2-phosphatidylinositol 3-kinase-Akt and VEGFR2-extracellular signal regulated kinase 1/2 pathways. PMID: 20837912
Adropin has an endothelial protective function mediated via upregulation of eNOS expression through the VEGFR2-PI3K-Akt and VEGFR2-ERK1/2 pathways. Adropin therapy may thus be useful for limiting diseases characterized by endothelial dysfunction. PMID: 20837912
Adropin regulated expression of hepatic lipogenic genes and adipose tissue peroxisome proliferator-activated receptor gamma, a major regulator of lipogenesis. PMID: 19041763
Adropin is the name given to the secreted peptide encoded by human C9orf165. In mice, it is abundant in liver where it is regulated by dietary macronutrients. Adropin regulates expression of genes involved in lipogenesis and adipogenesis. PMID: 19041763

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.