Recombinant Human CD27 Protein (His Tag)

Name: Recombinant Human CD27 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-0840
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cluster of differentiation (cd) proteins, Co-stimulatory receptors, Featured cd protein molecules, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P26842
Synonym	S152, S152. LPFS2, S152.LPFS2, T14, TNFRSF7, Tp55
Background	CD27, also known as TNFRSF7, is a member of the TNF-receptor superfamily limited to cells of the lymphoid lineage, and exists as both a dimeric glycoprotein on the cell surface and as a soluble protein in serum. As a type I transmembrane glycoprotein of about 55 kDa existing as disulfide-linked homodimer, CD27 has been shown to play roles in lymphoid proliferation, differentiation, and apoptosis.It has important role in generation of T cell immunity, and is an apparently robust marker for normal memory B cells. It is a T and B cell co-stimulatory molecule, the activity of CD27 is governed by its TNF-like ligand CD7 on lymphocytes and dendritic cells. The CD27-CD7 interaction is required for Th1 generation responses to differentiation signals and long-term maintenance of T cell immunity, and meanwhile, plays a key role in regulating B-cell differentiation, activation and immunoglobulin synthesis.Immune CheckpointImmune Checkpoint Detection: AntibodiesImmune Checkpoint Detection: ELISA AntibodiesImmune Checkpoint Detection: IHC AntibodiesImmune Checkpoint Detection: ICC AntibodiesImmune Checkpoint Detection: FCM AntibodiesImmune Checkpoint ProteinsImmune Checkpoint TargetsCo-stimulatory Immune Checkpoint Targets ImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the human CD27(P26842) ( Met 1-Ile192) was expressed with a C-terminal His tag.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Ala 20
AA Sequence	Met 1-Ile192
Molecular Weight	The secreted recombinant human CD27 consists of 183 a.a. and predicts a molecular mass of 20.7 KDa. The apparent molecular mass of the protein is approximately 27 KDa in SDS-PAGE under reducing conditions due to glycosylation.
Purity	>85% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured by its binding ability in a functional ELISA.Immobilized human CD27-his at 10 ug/mL (100 ul/well) can bind biotinylated human CD70-Fc, The EC50 of biotinylated human CD70-Fc is 57-85 ng/mL.
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated 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.