Recombinant Human Tumor Necrosis Factor-alpha,His (rHuTNF-α-His)

Catalogue Numbers: PR1126-10, PR1126-50, PR1126-1000

Sizes: 10µg, 50µg, 1.0mg (Contact us for the 1.0mg option)

Source: Escherichia coli

Molecular Weight:Approximately 17.5 kDa. a single, non-glycosylated, polypeptide chain containing 157 amino acids fragment (77-233) and having a molecular mass of 21.85 kDa with an amino-terminal hexahistidine tag.

Purity: >95% by SDS-PAGE and HPLC analyses.

Biological Activity: Fully biologically active when compared to standard. The Specific Activity is ≥2.0 × 107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation: Lyophilized from a 0.2mm filtered concentrated solution in PBS, pH 7.0.

AA Sequence: MHHHHHHVRS SSRTPSDKPV AHVVANPQAE GQLQWLNRRA NALLANGVEL
RDNQLVVPSE GLYLIYSQVL FKGQGCPSTH VLLTHTISRI AVSYQTKVNL
LSAIKSPCQR ETPEGAEAKP WYEPIYLGGV FQLEKGDRLS AEINRPDYLD
FAESGQVYFG IIAL

Endotoxin: Less than 1EU/mg of rHuTNF-α-his as determined by LAL method.

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.

Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

Usage: This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE. Made in China

Tumor necrosis factor alpha (TNF-α), also called cachectin, is produced by neutrophils, activated lymphocytes, macrophages, NK cells, LAK cells, astrocytes endothelial cells, smooth muscle cells and some transformed cells. TNF-α occurs as a secreted, soluble form and as a membrane-anchored form, both of which are biologically active. The naturally-occurring form of TNF-α is glycosylated, but non-glycosylated recombinant TNF-α has comparable biological activity. The biologically active native form of TNF-α is reportedly a trimer. Human and murine TNF-α show approximately 79% homology at the amino acid level and crossreactivity between the two species. Two types of receptors for TNF-α have been described and virtually all cell types studied show the presence of one or both of these receptor types.