TNFRSF1A Protein, Mouse, Recombinant (His Tag)

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TNFRSF1A Protein, Mouse, Recombinant (His Tag): Product Information

Purity
> 96 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its binding ability in a functional ELISA.
2. Immobilized human TNFa at 10 μg/mL (100 μl/well) can bind  biotinylated mouse TNFRSF1A-his. The EC50 of biotinylated mouse TNFRSF1A-his is 0.28 μg/mL.
3. Immobilized mouse TNFa at 10 μg/mL (100 μl/well) can bind  biotinylated mouse TNFRSF1A-his. The EC50 of biotinylated mouse TNFRSF1A-his is 0.13 μg/mL.
Protein Construction
A DNA sequence encoding the mouse TNFRSF1A (NP_ 035739.2) extracellular domain (Met 1-Ala 212) was expressed, with a polyhistidine tag at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Mouse
Predicted N Terminal
Leu 30
Molecule Mass
The secreted recombinant mouse TNFRSF1A consists of 194 amino acids and has a predicted molecular mass of 21.8 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm TNFRSF1A is approximately 35 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

TNFRSF1A Protein, Mouse, Recombinant (His Tag): Images

TNFRSF1A Protein, Mouse, Recombinant (His Tag): Alternative Names

CD120a Protein, Mouse; FPF Protein, Mouse; p55 Protein, Mouse; p55-R Protein, Mouse; TNF-alphaR1 Protein, Mouse; TNF-R Protein, Mouse; TNF-R-I Protein, Mouse; TNF-R1 Protein, Mouse; TNF-R55 Protein, Mouse; TNFalpha-R1 Protein, Mouse; TNFAR Protein, Mouse; Tnfr-2 Protein, Mouse; Tnfr1 Protein, Mouse; TNFR60 Protein, Mouse; TNFRI Protein, Mouse; TNFRp55 Protein, Mouse

TNFRSF1A Background Information

The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 32 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. CD12a (cluste of differentiation 12a), also known as TNFR1 / TNFRSF1A, is a member of CD family, tumor necrosis factor receptor superfamily. CD12a is one of the most primary receptors for the tumor necrosis factor-alpha. It has been shown to be localized to both plasma membrane lipid rafts and the trans golgi complex with the help of the death domain (DD). CD12a can activate the transcription factor NF-κB, mediate apoptosis, and regulate inflammation processes.
Full Name
tumor necrosis factor receptor superfamily member 1A
Research Areas
References
  • Zola H, et al. (2007) CD molecules 2006-human cell differentiation molecules. J Immunol Methods. 318 (1-2): 1-5.
  • Ho IC, et al. (2009) GATA3 and the T-cell lineage: essential functions before and after T-helper-2-cell differentiation. Nat Rev Immunol. 9 (2): 125-35.
  • Matesanz-Isabel J, et al. (2011) New B-cell CD molecules. Immunology Letters.134 (2): 104-12.
  • Cottin V, et al. (2002) Restricted localization of the TNF receptor CD120a to lipid rafts: a novel role for the death domain. The journal of immunology. 168: 4095-102.
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