Human TNFRSF14 (Tumor Necrosis Factor Receptor Superfamily Member 14) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-05003P
SDS-PAGE analysis of Human TNFRSF14 (Tumor Necrosis Factor Receptor Superfamily Member 14) - Recombinant Protein, CAT
SDS-PAGE analysis of Human TNFRSF14 (Tumor Necrosis Factor Receptor Superfamily Member 14) - Recombinant Protein, CAT# BLT-05003P, showing >95% purity under 15% SDS-PAGE (Reduced)

Human TNFRSF14 (Tumor Necrosis Factor Receptor Superfamily Member 14) - Recombinant Protein

Beta LifeScience SKU/CAT #: BLT-05003P
Regular price $595.00 Sale price $475.00Save $120
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Pack Size Price (USD)
500 µg $1,100 (Summer Promotion)
1 mg $1,990 (Summer Promotion)

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Product Overview

Product Name Recombinant Human TNFSF14 / LIGHT / CD258 (TNFRSF14) Protein
Product Overview This recombinant human TNFSF14 / LIGHT / CD258 (TNFRSF14) protein includes amino acids 74-240aa of the MAPT gene is expressed in HEK293 Cells.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization.
Target Uniprot Id Q92956
Recommended Name Tumor necrosis factor receptor superfamily member 14
Gene Name TNFRSF14
Synonyms CD258;HVEML;LIGHT;LTg;TR2
Species Human
Predicted Molecular Mass 20.4 kDa
Expression System Mammalian Cell
Expression Range 74-240aa
Tag N-His
Purity >95%
Formulation Lyophilized
Buffer Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose
Storage Condition 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Reconstitution Instruction Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Applications Positive Control; Immunogen; SDS-PAGE; WB
Research Area Cancer
Target Function Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network. Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation. Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions. Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response. In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and proinflammatory cytokines. Upon binding to CD160 on activated CD4+ T cells, downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response. May interact in cis (on the same cell) or in trans (on other cells) with BTLA. In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells.; (Microbial infection) Acts as a receptor for Herpes simplex virus 1/HHV-1.; (Microbial infection) Acts as a receptor for Herpes simplex virus 2/HHV-2.
Subcellular Location Cell membrane; Single-pass type I membrane protein.
Tissue Specificity Widely expressed, with the highest expression in lung, spleen and thymus. Expressed in a subpopulation of B cells and monocytes. Expressed in naive T cells.

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.

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