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Gibco™ Human TNF-alpha Recombinant Protein

Catalog No. PHC3015L
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PHC3015L 10 μg
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Recombinant Protein

Carrier-Free Storage: Store the liquid human TNF-alpha at ≤-20°C. Upon thawing, apportion into working aliquots and store at ≤-20°C. Avoid repeated freeze-thaw cycles.

TNF alpha is a multifunctional proinflammatory cytokine that belongs to the tumor necrosis factor (TNF) superfamily. This cytokine is mainly secreted by macrophage and bind to its receptors, TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. TNF alpha is involved in the regulation of immune cells, cell proliferation, differentiation, apoptosis, lipid metabolism, and coagulation. TNF alpha exists as a multimer of two, three, or five noncovalently linked units, but shows a single 17 kDa band following SDS-PAGE under non-reducing conditions. Knockout studies in mice also suggested the neuroprotective function of TNF alpha, and has been observed to causes tumor necrosis when injected into tumor-bearing mice. Other functions of TNF-alpha include its role in the immune response to bacterial, viral, parasitic and certain fungal infections, as well as its role in the necrosis of specific tumors. TNF alpha causes cytolysis or cytostasis of certain transformed cells, being synergistic with interferon-gamma in its cytotoxicity. This cytokine has been implicated in a variety of diseases, including autoimmune diseases, insulin resistance, and cancer.
TRUSTED_SUSTAINABILITY

Specifications

Accession Number P01375
For Use With (Application) Bioactivity
Formulation 40mM tris with no preservative; pH 8
Gene ID (Entrez) 7124
Molecular Weight (g/mol) 17.5 kDa
Name Human TNF-alpha
pH Range 8
Purification Method Purified
Quantity 10 μg
Storage Requirements -20°C
Regulatory Status RUO
Endotoxin Concentration <0.1 ng/μg
Gene Alias APC1 protein; Cachectin; C-domain 1; C-domain 2; cTNF; DADB-70P7.1; DIF; ICD1; ICD2; Intracellular domain 1; Intracellular domain 2; N-terminal fragment; NTF; RATTNF; Tnf; TNF alpha; TNF superfamily; TNF α; TNF, macrophage-derived; TNF, monocyte-derived; TNFA; TNF-a; TNFalpha; TNF-alpha; Tnfsf1a; TNFSF2; TNFα; TNLG1F; Tumor necrosis factor; tumor necrosis factor (TNF superfamily, member 2); tumor necrosis factor alpha; tumor necrosis factor alpha (cachetin); tumor necrosis factor alpha precursor; tumor necrosis factor ligand 1F; tumor necrosis factor ligand superfamily member 2; Tumor necrosis factor, membrane form; Tumor necrosis factor, soluble form; tumor necrosis factor-alpha; tumor necrosis factor-alpha precursor; tumor-necrosis factor; tumour necrosis factor
Common Name TNF alpha
Gene Symbol Tnf
Biological Activity ED50 = 0.02 - 0.05 ng/mL; determined by the dose-dependent cytotoxcity on L929 cells in the presence of actinomycin D.
Product Type Protein
Conjugate Unconjugated
Species Human
Recombinant Recombinant
Content And Storage -20°C
Activity ED50 = 0.02 - 0.05 ng/mL; determined by the dose-dependent cytotoxcity on L929 cells in the presence of actinomycin D.
Endotoxin Level <0.1 ng/μg
Shipping Condition Dry Ice
Expression System E. coli
Protein Family Cytokines & Receptors
Protein Form Recombinant, Ligand
Form Liquid
Protein Subtype TNF (Tumor Necrosis Factor)
Research Category Immunology, Signal Transduction, Stem Cell Research, Inflammation, Oncology
Product Line Gibco
Purity or Quality Grade >95% by SDS-PAGE
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It looks like the recombinant protein vial I received from you is empty. Is this normal?

Gibco recombinant proteins are frequently formulated without carrier proteins or additives (e.g., BSA, HSA, sucrose, etc.) and no Gibco PeproTech recombinant protein contains a carrier protein. As a result, during lyophilization, the protein product may be deposited on the vial as a thin, and sometimes invisible, film instead of a pellet. The size of the pellet, if any, is not directly related to the quantity of the recombinant protein in the vial. Our quality control procedures assure that each vial contains the correct amount of product.

To ensure complete recovery of protein product, before opening a vial of lyophilized recombinant protein, we recommend centrifuging it in a microcentrifuge for 20-30 seconds to drive any protein that may be lodged in the cap or on the side to the bottom of the vial. After reconstitution, you can confirm the presence of product protein by running a small amount on SDS-PAGE. In general, a protein band with expected size should be visible with as little as 10 ng of protein loaded on an acrylamide gel.

Why does my recombinant protein not show activity in my own experiment?

Assay time is critical. Each assay needs to beoptimized and performed at the peak response time. Different cells may respond differently to a growth factor or cytokine. We suggest repeating our QC assay using same indicator cells as suggested in the manual to see if you can obtain a similar response. In addition, serum may be masking the response. Serum starvation might be needed for certain types of assays.

How should I store the reconstituted recombinant proteins?

Protein solutions are generally not very stable when frozen at low concentration. Upon freeze and thaw, some proteins in the solution may stick to the wall of the container, which results in significant reduction of protein concentration if the starting concentration was low. Therefore, carrier proteins are used to reduce such loss. The most commonly used carrier proteins include bovine serum albumin (BSA), human serum albumin (HSA), or fetal bovine serum (FBS). These carrier proteins are generally used at 0.1% concentration. As a rule of thumb, if the concentration of the recombinant protein is less than 0.5 mg/mL, it is a good idea to add some carrier protein

How do I store my lyophilized recombinant protein?

Lyophilized proteins can typically be stored at 2 to 8 degrees C for several weeks, or stored dessicated at -20 degrees C for long-term storage.

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