Recombinant Mouse Pro-EMAP-II Protein, CF Summary
Product Specifications
Ala2-Lys310, with an N-terminal Met and 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
2026-EM
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: EMAP-II
EMAP-II (endothelial monocyte-activating polypeptide II; also AIMP1 and SCYE1) is a 23 kDa polypeptide originally identified in the supernatant of TNF-alpha treated Meth-A fibrosarcoma cells (1, 2). In addition to EMAP-I/S100C and EMAP-III/VEGF, EMAP-II was one of three molecules presumed to enhance TNF-alpha -induced tissue factor expression on endothelial cells. Pro-EMAP-II, otherwise known as p43, is the 310 amino acid (aa) precursor to EMAP-II (3). It is considered to have widespread, if not ubiquitous expression, and is found both intra- and extracellularly (1, 4, 5). Pro-EMAP-II contains no canonical signal sequence. It does possess a 144 aa N-terminus that is characterized by the presence of two coiled-coil regions (aa 6 - 77) and two heparin-binding motifs (aa 71 - 73 and 120 - 122) (6, 7, 8). The C-terminal 166 aa are synonymous with EMAP‑II. This region binds t-RNA (5, 8). Although Pro‑EMAP‑II is 34 kDa in size, it can run anomalously in SDS-page at 43 - 44 kDa (1, 5, 9, 10). When secreted, Pro-EMAP-II circulates as either a dimer or higher-order oligomer, likely due to its coiled-coil region (5). Mouse Pro-EMAP-II shares 89% and 86% aa identity with rat and human Pro-EMAP-II, respectively, and is known to be active on human cells (3, 11). Within the cell, Pro-EMAP-II is one of eleven subunits that constitute the mammalian multisynthetase complex. This is essential for ribosomal protein synthesis (12). When cells are stressed, they dissociate Pro-EMAP-II from this complex and release it (1, 10, 13). Although the particulars are unclear, it would appear that secreted Pro-EMAP-II binds to cell surface ATP synthase alpha -subunits (14). Here, it presumably either acts as a cytokine, or undergoes proteolytic cleavage, first by MMPs at Pro108 (based on human), and later by cathepsin L at Ser145 (10, 15). The cleavage products are monomers and likely not active cytokines (5, 10, 14). In theory, Pro-EMAP-II acts as a mediator of tissue restructuring. Upon cell stress (and subsequent apoptosis), Pro-EMAP-II is released and establishes an environment where phagocytic cells can migrate to, and actively remove, dying cells and cellular debris (1, 5, 10, 13, 16).
- Van Horssen, R. et al. (2006) Cytokine Growth Factor Rev. 17:339.
- Kao, J. et al. (1994) J. Biol. Chem. 267:20239.
- Kao, J. et al. (1994) J. Biol. Chem. 269:25106.
- Murray, J.C. et al. (2000) Am. J. Pathol. 157:2045.
- Shalak, V. et al. (2001) J. Biol. Chem. 276:23769.
- Kim, Y. et al. (2000) J. Biol. Chem. 275:27062.
- Ahn, H-C. et al. (2003) FEBS Lett. 542:119.
- Chang, S-Y. et al. (2005) Mol. Pharmacol. 67:1534.
- Knies, U.E. et al. (1998) Proc. Natl. Acad. Sci. USA 95:12322.
- Shalak, V. et al. (2007) J. Biol. Chem. 282:10935.
- Kao, J. et al. (1994) J. Biol. Chem. 269:9774.
- Robinson J-C. et al. (2000) J. Mol. Biol. 304:983.
- Ko, Y-G. et al. (2001) J. Biol. Chem. 276:23028.
- Chang, S.Y. et al. (2002) J. Biol. Chem. 277:8388.
- Liu, J. and M.A. Schwarz (2006) Exp. Cell Res. 312:2231.
- Barnett, G. et al. (2000) Cancer Res. 60:2850.
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