Recombinant Human CD9 Protein

Name: Recombinant Human CD9 Protein
Brand: Beta LifeScience
SKU: BL-0122PS
Availability: InStock

Collections: Cluster of differentiation (cd) proteins, Featured cd protein molecules, 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

Tag	N/A
Host Species	Human
Synonym	CD9 antigen, 5H9 antigen, Cell growth-inhibiting gene 2 protein, Leukocyte antigen MIC3, Motility-related protein, CD9, MRP-1, Tetraspanin-29, Tspan-29, p24, MIC3, TSPAN29, GIG2, BTCC-1, DRAP-27, TSPAN-29.
Background	CD9 which is found on the surface of exosomes is a cell surface glycoprotein which is interacts with integrins and various transmembrane superfamily proteins. CD9 is involved in platelet activation and aggregation and also regulates paranodal junction formation. CD9 takes part in cell adhesion and migration and also promotes muscle cell fusion. CD9 is necessary for the egg-sperm fusion during mammalian fertilization.
Description	CD9 Human Recombinant expressed in E. coli is a single polypeptide chain containing 107a.a. (112-195) and having a molecular weight of 12kDa.CD9 is fused to a 23a.a. His-tag at N-terminus and purified by unique purification methods.
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MGSSHKDEVI KEVQEFYKDT YNKLKTKDEP QRETLKAIHY ALNCCGLAGG VEQFISDICP KKDVLETFTV KSCPDAIKEV FDNKFHI.
Purity	>85.0% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Formulation	The CD9 solution (0.25mg/1ml) contains Phosphate buffer saline (pH 7.4), 20% glycerol and 1mM DTT.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

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.