Recombinant Human ANGPTL7/CDT6 Protein

Name: Recombinant Human ANGPTL7/CDT6 Protein
Brand: Beta LifeScience
SKU: BLK-00491P-100UG
Availability: InStock

Human ANGPTL7 on Tris-Bis PAGE under reduced condition. The purity is greater than 90%.

Collections: High-quality recombinant proteins, Other recombinant proteins

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.

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Product Overview

Description	Recombinant Human ANGPTL7/CDT6 Protein is expressed from HEK293 with His and Avi tag at the C-Terminus.It contains GIn27-Pro346.
Purity	> 90% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
Accession	O43827
Target Symbol	ANGPTL7
Synonyms	angiopoietin-like 7; Angiopoietin-like factor; ANGPTL7; AngX; CDT6; dJ647M16.1; RP4-647M16.2
Species	Human
Expression System	HEK293
Tag	C-His-Avi
Expression Range	GIn27-Pro346
Mol. Weight	The protein has a predicted MW of 40.2 kDa. Due to glycosylation, the protein migrates to 35-40 kDa based on Tris-Bis PAGE result.
Form	Lyophilized
Formulation	Lyophilized from 0.22um filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Endotoxin	Less than 1EU per ug by the LAL method.
Storage	Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Shipping	Shipped at ambient temperature.
Gene Background	Angiopoietin-like 7 (ANGPTL7), also known as Corneal-Derived Transcript 6 (CDT6), is a secreted glycoprotein that is structurally related to the angiopoietins. Members of this protein family contain an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Its production is up‑regulated in trabecular meshwork cells by glucocorticoids and TGF-beta and in cartilage by TNF-alpha.

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.