Recombinant Human CD40 Ligand/TNFSF5 Avi-tag His-tag, CF

Catalog # Availability Size / Price Qty
AVI11596-050
Biotinylated Recombinant Human CD40 Ligand/TNFSF5 Avi-tag His-tag Protein Binding Activity.
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Recombinant Human CD40 Ligand/TNFSF5 Avi-tag His-tag, CF Summary

Product Specifications

Accession #
N-terminal Sequence
Analysis
Gly of Avi-tag
Structure / Form
Biotinylated via Avi-tag
Predicted Molecular Mass
19 kDa
SDS-PAGE
18 - 25 kDa, under reducing conditions

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AVI11596

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

AVI11596

Formulation Lyophilized from a 0.2 μm filtered solution in PBS and EDTA with Trehalose.
Reconstitution Reconstitute at 250 μg/mL in sterile water.
Stability & Storage: Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.

Scientific Data

Binding Activity View Larger

Biotinylated Recombinant Human CD40 Ligand/TNFSF5 Avi-tag His-tag Protein (Catalog # AVI11596) binds Recombinant Human CD40/TNFRSF5 Fc Chimera (1493-CDB) with an ED50 of 2.50-30.0 ng/mL.

SDS-PAGE View Larger

2 μg/lane of Biotinylated Recombinant Human CD40 Ligand/TNFSF5 Avi-tag His-tag Protein (Catalog # AVI11596) was resolved with SDS-PAGE under reducing (R) condition and visualized by Coomassie® Blue staining, showing bands at 18-25 kDa.

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Background: CD40 Ligand/TNFSF5

CD40 Ligand, also known as TNFSF, CD154, TRAP, and gp39, is a 34-39 kDa type II transmembrane glycoprotein that belongs to the TNF superfamily (1-3). Mature human CD40 Ligand consists of a 22 amino acid (aa) cytoplasmic domain, a transmembrane segment, and an 215 aa extracellular region (4, 5). The extracellular domain of human CD40 Ligand shares 74% and 76% aa sequence identity with mouse and rat CD40 Ligand, respectively. Similar to other TNF superfamily members, CD40 Ligand forms a bioactive homotrimer, both as membrane bound and soluble forms (6-9). The 18 kDa soluble form (aa 113-261) arises from proteolytic processing. Mutation and alternative splicing generate additional forms of CD40 Ligand that are often truncated or non-trimerizable (8). CD40 Ligand is expressed on platelets, as well as on activated T cells and B cells, basophils, eosinophils, fibroblasts, mast cells, monocytes, natural killer cells, vascular endothelial cells, and smooth muscle cells. CD40 Ligand binds to CD40, which is expressed on the surface of B cells, dendritic cells, macrophages, monocytes, platelets, endothelial, and epithelial cells (10). The interaction of CD40 Ligand with CD40 initiates signaling in both CD40 and CD40 Ligand expressing cells (11).  CD40 ligation by CD40 Ligand promotes B cell activation and T cell-dependent humoral responses (12, 13). CD40 Ligand dysregulation on T cells and antigen presenting cells contributes to the immune deficiency associated with HIV infection and AIDS (14, 15). It is also implicated in the pathology of multiple cardiovascular diseases including atherosclerosis, atherothrombosis, and restenosis (16, 17). Our Avi-tag Biotinylated human CD40 Ligand features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

References
  1. Zhang, G. (2004) Curr. Opin. Struct. Biol. 14:154.
  2. Hehlgans, T. and K. Pfeffer (2005) Immunology 115:1.
  3. Quezada, S.A. et al. (2004) Annu. Rev. Immunol. 22:307.
  4. Graf, D. et al. (1992) Eur. J. Immunol. 22:3191.
  5. Hollenbaugh, D. et al. (1992) EMBO J. 11:4313.
  6. Khandekar, S.S. et al. (2001) Protein Expr. Purif. 23:301.
  7. Pietravalle, F. et al. (1996) J. Biol. Chem. 271:5965.
  8. Garber, E. et al. (1999) J. Biol. Chem. 274:33545.
  9. Vakkalanka, R.K. et al. (1999) Arthritis Rheum. 42:871.
  10. van Kooten, C. and J. Banchereau (1997) Curr. Opin. Immunol. 9:330.
  11. Eissner, G. et al. (2004) Cytokine Growth Factor. Rev. 15:353.
  12. Rickert, R.C. et al. (2011) Immunol. Rev. 244:115.
  13. Elgueta, R. et al. (2009) Immunol. Rev. 229:152.
  14. Kornbluth, R.S. (2000) J. Leukoc. Biol. 68:373.
  15. Chougnet, C. (2003) J. Leukoc. Biol. 74:702.
  16. Pamukcu, B. et al. (2011) Ann. Med. 43:331.
  17. Hassan, G.S. et al. (2012) Immunobiology 217:521.
Entrez Gene IDs
959 (Human); 21947 (Mouse); 84349 (Rat)
Alternate Names
CD154 antigen; CD154; CD40 antigen ligand; CD40 Ligand; CD40L; CD40-L; CD40LG; CD40LIGM; gp39; hCD40L; HIGM1; T-B cell-activating molecule; T-BAM; T-cell antigen Gp39; TNF-related activation protein; TNFSF5; TNFSF5IMD3; TRAP; TRAPtumor necrosis factor (ligand) superfamily, member 5 (hyper-IgM syndrome); tumor necrosis factor (ligand) superfamily member 5; Tumor necrosis factor ligand superfamily member 5

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