Rat TNFRSF1A / TNFR1 Protein

Sino Biological Inc. liefert Rat TNFRSF1A / TNFR1 Protein mit höherer Qualität und günstiger Kosten im Vergleich mit anderen globalen Lieferanten.

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Produkt-Information von TNFRSF1A / TNFR1 Protein

QC Testing von TNFRSF1A / TNFR1 Protein

Purity	> 90% as determined by SDS-PAGE	SDS-PAGE: TNFR1 protein
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Stability	Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal	Ile 22
Molecular Mass	The recombinant rat TNFRSF1A/Fc is a disulfide-linked homodimer. The reduced monomer comprises 431 amino acids and has a predicted molecular mass of 47.9 kDa. The apparent molecular mass of the protein is approximately 59 kDa in SDS-PAGE under reducing conditions.
Formulation	Lyophilized from sterile PBS, pH7.4. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.

Usage Guide von TNFRSF1A / TNFR1 Protein

Verwandte Produkte & Themen von TNFRSF1A / TNFR1 Protein

Cancer>>Angiogenesis>>Cytokines/Chemokines in Angiogenesis>>TNFR1/CD120a

Immunology>>Cytokine & Receptor>>TNF Superfamily>>TNFR1/CD120a

Immunology>>Cluster of Differentiation>>T Cell CD Antigen>>Helper T Cells>>TNFR1/CD120a

Beschreibung von TNFRSF1A / TNFR1 Protein

Tumor necrosis factor receptor superfamily, member 1A (TNFRSF1A), also known as TNFRI, TNF R-p55/p60, and CD120a, is a type I transmembrane protein widely expressed and is present on the cell surface as a trimer of 55 kDa subunits. Human TNFRSF1A/TNFRI is a 455 aa protein that contains a 21 aa signal sequence, a 190 aa ECD with a PLAD domain which mediates constitutive trimer formation followed by four TNF-α trimer-binding cysteine-rich domains (CRDs), a 23 aa transmembrane domain, and a 221 aa cytoplasmic sequence that contains a neutral sphingomyelinase activation domain and a death domain. TNFRSF1A/TNFRI serves as a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor, and the resulting death-inducing signaling complex (DISC) initiates the subsequent cascade of caspases mediating apoptosis. TNFRSF1A/TNFRI can also activate the transcription factor NF-kB, and functions as a regulator of inflammation. Germline mutations of the extracellular domains of TNF RI are found to be associated with the human genetic disorder called periodic fever syndrome.

References

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