Recombinant Human BST1 Protein, Active

Name: Recombinant Human BST1 Protein, Active
Brand: Beta LifeScience
SKU: BLK-02630P-100UG
Availability: InStock

Human BST1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Collections: Other recombinant proteins, 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 BST1 Protein is expressed from HEK293 with His tag at the C-Terminus.It contains Gly29-Ala293.
Purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
Accession	Q10588
Target Symbol	BST1
Synonyms	Antigen BP3; BST-1; Bp-3; Bp3; Ly65; Bst1; BST1; CD157
Species	Human
Expression System	HEK293
Tag	C-His
Expression Range	Gly29-Ala293
Mol. Weight	The protein has a predicted MW of 31.2 kDa. Due to glycosylation, the protein migrates to 38-48 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.
Activity	Immobilized Human BST1, His Tag at 1ug/ml (100ul/Well) on the plate. Dose response curve for Anti-BST1 Antibody, hFc Tag with the EC50 of 2.5ng/ml determined by ELISA. Contact us for detailed testing images.
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	BST1 overexpression conferred resistance to sphingosine in yeast. BST1 deletion produced sensitivity to exogenous D-erythro-sphingosine and phytosphingosine and intracellular accumulation of sphingosine 1-phosphate upon exposure to exogenous sphingosine. sphingoid base metabolism is similar in all eukaryotes and suggests that yeast genetics may be useful in the isolation and identification of other genes involved in sphingolipid signaling and metabolism.

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.