Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | Q9D777 |
express system | HEK293 |
product tag | N-His-Flag |
purity | > 90% as determined by Tris-Bis PAGE;> 90% as determined by HPLC |
background | The APRIL (a proliferation-inducing ligand), also known as TNFSF13, TALL2, TRDL1, and CD256, is a member of the TNF ligand superfamily.Both APRIL and its close relative BAFF bind and signal through the TNF superfamily receptors TACI and BCMA, while BAFF additionally functions through BAFF R. |
molecular weight | The protein has a predicted MW of 18.53 kDa. Due to glycosylation, the protein migrates to 24-30 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Mouse APRIL/TNFSF13 Protein 2483
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Ala96-Leu241
Mouse APRIL/TNFSF13 Protein 2483
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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The APRIL (a proliferation-inducing ligand), also known as TNFSF13, TALL2, TRDL1, and CD256, is a member of the TNF ligand superfamily.Both APRIL and its close relative BAFF bind and signal through the TNF superfamily receptors TACI and BCMA, while BAFF additionally functions through BAFF R. |
Protein names Tumor necrosis factor ligand superfamily member 13 (A proliferation-inducing ligand) (APRIL) (CD antigen CD256) |
Gene names Tnfsf13,Tnfsf13 April |
Protein family Tumor necrosis factor family |
Mass 10090Da |
Function Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes. |
Subellular location Secreted . |
Structure Homotrimer. |
Post-translational modification The soluble form derives from the membrane form by proteolytic processing. |
Target Relevance information above includes information from UniProt accession: Q9D777 |
The UniProt Consortium |
Publications
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We haven't added any publications to our database yet. |
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