Recombinant Human CD30 Protein (His & Fc Tag)

Name: Recombinant Human CD30 Protein (His & Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-0866
Availability: InStock

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

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Product Overview

Tag	His&Fc
Host Species	Human
Accession	NP_001234.2
Synonym	CD30, D1S166E, Ki-1
Background	CD3, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD3 protein is expressed by activated, but not resting, T and B cells. CD3 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD3 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD3 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD3 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the human TNFRSF8 (NP_001234.2) extracellular domain (Met 1-Lys 379) was fused with the C-terminal His-tagged Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Phe 19
AA Sequence	Met 1-Lys 379
Molecular Weight	The recombinant human TNFRSF8/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer consists of 609 a.a. and has a predicted molecular mass of 66.5 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhTNFRSF8/Fc monomer is approximately 130 kDa due to glycosylation.
Purity	>90% 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 recombinant human CD30L at 20 ug/ml (100 ul/well) can bind biotinylated human CD30 with a linear range of 0.31-20 ng/ml.
Formulation	Lyophilized from sterile PBS, 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.