Recombinant Human TNFRSF1A Protein (His & Fc Tag)

Name: Recombinant Human TNFRSF1A Protein (His & Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-4597
Availability: InStock

Collections: Cytokines and growth factors, Recombinant proteins, Tumor necrosis factors and receptors (tnfs)

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Product Overview

Tag	His&Fc
Host Species	Human
Accession	NP_001056.1
Synonym	CD120a, FPF, MS5, p55, p55-R, p60, TBP1, TNF-R, TNF-R-I, TNF-R55, TNFAR, TNFR1, TNFR1-d2, TNFR55, TNFR60
Background	The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 32 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD12a (cluste of differentiation 12a), also known as TNFR1 / TNFRSF1A, is a member of CD family, tumor necrosis factor receptor superfamily. CD12a is one of the most primary receptors for the tumor necrosis factor-alpha. It has been shown to be localized to both plasma membrane lipid rafts and the trans golgi complex with the help of the death domain (DD). CD12a can activate the transcription factor NF-κB, mediate apoptosis, and regulate inflammation processes.
Description	A DNA sequence encoding the human TNFRI (NP_001056.1) extracellular domain (Met 1-Thr 211) was fused with the C-terminal His-tagged Fc region of human IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Ile 22
AA Sequence	Met 1-Thr 211
Molecular Weight	The recombinant human TNFRI/Fc is a disulfide-linked homodimer. The reduced monomer consists of 438 a.a. and has a predicted molecular mass of 49.3 kDa. As a result of glycosylation, rh TNFRI/Fc monomer migrates with an apparent molecular mass of 60-65 kDa in SDS-PAGE under reducing conditions.
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 ability to inhibit TNF-alpha-mediated cytotoxicity in L-929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is typically 2-12ng/mL in the presence of 1 ng/mL recombinant human TNF-alpha.
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.