Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 8 (TNFSF8) Protein (His), Active

Name: Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 8 (TNFSF8) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05823P
Price: 299.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Activity Measured by its binding ability in a functional ELISA. Immobilized CD30 at 5 μg/ml can bind human CD30L, the EC 50 is 9.531-12.49 ng/ml. Biological Activity Assay

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Price Save $108

Size

100ug

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Product Overview

Description	Recombinant Human Tumor Necrosis Factor Ligand Superfamily Member 8 (TNFSF8) Protein (His), Active is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/ug as determined by LAL method.
Activity	Measured by its binding ability in a functional ELISA. Immobilized CD30 at 5 μg/ml can bind human CD30L, the EC 50 is 9.531-12.49 ng/ml.
Uniprotkb	P32971
Target Symbol	TNFSF8
Synonyms	TNFSF8; CD30L; CD30LG; Tumor necrosis factor ligand superfamily member 8; CD30 ligand; CD30-L; CD antigen CD153
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	N-6His
Target Protein Sequence	QRTDSIPNSPDNVPLKGGNCSEDLLCILKRAPFKKSWAYLQVAKHLNKTKLSWNKDGILHGVRYQDGNLVIQFPGLYFIICQLQFLVQCPNNSVDLKLELLINKHIKKQALVTVCESGMQTKHVYQNLSQFLLDYLQVNTTISVNVDTFQYIDTSTFPLENVLSIFLYSNSD
Expression Range	63-234aa
Protein Length	Partial
Mol. Weight	21.8 kDa
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 20 mM Tris-HCl, 0.5 M NaCl, 6% Trehalose, pH 8.0
Reconstitution	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%.
Storage	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.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Cytokine that binds to TNFRSF8/CD30. Induces proliferation of T-cells.
Subcellular Location	Membrane; Single-pass type II membrane protein.
Protein Families	Tumor necrosis factor family
Database References	HGNC: 11938 OMIM: 603875 KEGG: hsa:944 STRING: 9606.ENSP00000223795 UniGene: Hs.494901

Gene Functions References

circulant sCD30L is functionally active and that it may favor persistence of active inflammation by inducing apoptosis of CD30(+)T cells, known to down-modulate inflammation in rheumatoid synovitis. PMID: 24447865
TNFSF8 is an important leprosy T1R susceptibility gene. PMID: 25320285
The heritability of IgA levels is moderate and can partly be attributable to common variation in the CD30L locus. PMID: 24676358
The TNFSF8 polymorphisms rs927374 and rs2295800 were associated with neutrophil count. This finding suggests that post-MI inflammatory response is genetically modulated. PMID: 22033252
Positional candidate gene screening in the SPA2 locus allowed us to identify and replicate an association between a rare SNP located in TNFSF8 and spondylarthritis. PMID: 21480186
a possible role of novel TNFSF8 variants in susceptibility to lung cancer. PMID: 21292647
capability to up-regulate expression of CD30, release of soluble CD30 and production of IL-4 in pre-activated T cells upon co-culture PMID: 11728464
Mast cells were found to be the predominant CD30 ligand-positive (CD30L-positive) cell in the chronic inflammatory skin diseases psoriasis and atopic dermatitis. PMID: 16964309
CD153 antigen was expressed by synovial mast cells, and correlated with serum levels, in Rheumatoid Arthritis patients PMID: 19208589
Single nucleotide polymorphism in TNFSF8 gene is associated with bone disease in myeloma. PMID: 19657367

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.