Recombinant Sheep TNF alpha Protein

Beta LifeScience SKU/CAT #: BLA-1071P

Recombinant Sheep TNF alpha Protein

Beta LifeScience SKU/CAT #: BLA-1071P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Host Species Sheep
Accession P23383
Synonym APC1 APC1 protein Cachectin DIF Differentiation inducing factor Macrophage cytotoxic factor Tnf TNF superfamily member 2 TNF superfamily, member 2 TNF, macrophage derived TNF, monocyte derived TNF-a TNF-alpha TNFA TNFA_HUMAN TNFSF2 Tumor necrosis factor Tumor necrosis factor (TNF superfamily member 2) Tumor necrosis factor alpha Tumor necrosis factor ligand superfamily member 2 Tumor Necrosis Factor, Membrane Form Tumor necrosis factor, soluble form
Description Recombinant Sheep TNF alpha Protein was expressed in Yeast. It is a Full length protein
Source Yeast
AA Sequence LRSSSQASNN KPVAHVVANI SAPGQLRWGD SYANALMANG VELKDNQLVV PTDGLYLIYS QVLFRGHGCP STPLFLTHTI SRIAVSYQTK VNILSAIKSP CHRETLEGAE AKPWYEPIYQ GGVFQLEKGD RLSAEINLPE YLDYAESGQV YFGIIAL
Molecular Weight 17 kDa
Purity Greater than 95% SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon reconsitution add a carrier protein (0.1% BSA). Store at -20°C. Avoid freeze / thaw cycle.

Target Details

Target Function Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance. Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6.; The TNF intracellular domain (ICD) form induces IL12 production in dendritic cells.
Subcellular Location Cell membrane; Single-pass type II membrane protein.; [Tumor necrosis factor, membrane form]: Membrane; Single-pass type II membrane protein.; [Tumor necrosis factor, soluble form]: Secreted.; [C-domain 1]: Secreted.; [C-domain 2]: Secreted.
Protein Families Tumor necrosis factor family
Database References

KEGG: oas:443540

UniGene: Oar.455

Gene Functions References

  1. The aim of the study was to assess the prognostic significance of Tumor Necrosis Factor-alpha, Interleukin-12(p40), Interleukin-6 and Interleukin 10 levels in cerebrospinal fluid (CSF) in sheep with encephalitic listeriosis. PMID: 25817420
  2. The p38 MAPK inhibitor decreased (P < 0.01) gene expression of TNFa but its effect was not observed at the level of TNFa protein synthesis PMID: 24995301
  3. TNF-alpha gene expression in multifidus was greater on both sides in the disc lesion animals than in the muscle of control animals. PMID: 24718080
  4. Injection of peptidoglycan-polysaccharide resulted in fever, increased concentrations of TNF-alpha on the day of and the day after challenge, and decreased concentrations of progesterone on days 14 and 21. PMID: 20603027
  5. These data are consistent with the effects of LPS on GH secretion originating through peripheral cytokine presentation to the pituitary, as well as a potential to act directly on selective populations of pituitary cells via CD14. PMID: 15899940
  6. plasma IL-1 beta, TNF-alpha and MCP-1 may potentially serve as markers to monitor prognosis of pregnancy toxaemia in ewes PMID: 17221363

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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