Product Specifications for Recombinant Human Galectin-3BP/MAC-2BP Protein, CF
Mouse myeloma cell line, NS0-derived human Galectin-3BP/MAC-2BP protein Val19-Asp585, with a C-terminal 10-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
26-30 kDa, 60-69 kDa and 81-94 kDa, reducing conditions
Measured by its binding ability in a functional ELISA. When Recombinant Human Galectin-3BP/MAC-2BP is immobilizedat 0.5 µg/mL,100 μL/well, It can bind Recombinant Human Galectin‑3 (Catalog # 1154-GA) with an ED50 of 0.2-1 μg/mL.
Scientific Data Examples for Recombinant Human Galectin-3BP/MAC-2BP Protein, CF
Recombinant Human Galectin-3BP/MAC-2BP Protein Bioactivity
When Recombinant Human Galectin-3BP/MAC-2BP (Catalog # 2226-GBA) is immobilized at 0.5 µg/mL, 100 µL/well, It binds Recombinant Human Galectin-3 (Catalog # 1154-GA) with an ED50 of 0.2-1 µg/mL.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
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
Lyophilized from a 0.2 μm filtered solution in PBS and DTT with Trehalose.
Reconstitute at 500 μg/mL in PBS.
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.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Galectin-3 binding protein (Galectin-3BP), also known as MAC-2 binding protein (MAC-2BP or M2BP), and the 90 kDa tumor associated antigen (TAA90K or 90K), is a secreted glycoprotein of the scavenger receptor cysteine-rich (SRCR) superfamily (1, 2). Galectin-3BP binds Galectin-3 (formerly MAC-2) with high affinity, but also binds Galectins -1 and -7, several collagen types, fibronectin, beta 1 integrins and nidogen (3, 6, 7). It is widely expressed in all extracellular fluids and in pericellular areas of cell‑rich tissues (1‑3). The 585 amino acid (aa) human Galectin‑3BP contains an 18 aa signal sequence and four definitive domains (4‑6). Domain 1 is a group A scavenger receptor domain (4), domain 2 is a BTB/POZ domain that strongly mediates dimerization (5), and domain 3 is an IVR domain, that is also found following the POZ domain in Drosophila kelch protein. Although little is known about domain 4, recombinant domains 3 and 4 reproduce the solid‑phase adhesion profile of full‑length Galectin‑3BP (5, 6). Glycosylation at seven N‑linked sites, generates a molecular size of 85‑97 kDa (1, 2, 6). Galectin‑3BP dimers form linear and ring‑shaped oligomers, most commonly decamers and dodecamers (3, 5). In vitro, Galectin‑3BP has been shown to stimulate natural killer cells and lymphokine‑activated killer cell activity (2). High Galectin‑3BP expression has been correlated with tumor aggressiveness in several, but not all, study systems (7). Mature human Galectin‑3BP shares 69% aa identity with mouse cyclophilin C‑associated protein (CyCAP), which does not appear to bind Galectin‑3 (8). Human Galectin‑3BP also shares 73%, 67% and 68% aa identity with relatively uncharacterized orthologs in dog, rat and cow, respectively. A human N‑terminally truncated sequence that begins within the BTB/POZ domain (aa 196) has been reported (9).
Koths, K. et al. (1993) J. Biol. Chem. 268:14245.
Ullrich, A. et al. (1994) J. Biol. Chem. 269:18401.
Sasaki, T. et al. (1998) EMBO J. 17:1606.
Hohenester, E. et al. (1999) Nat. Struct. Biol. 6:228.
Muller, S. A. et al. (1999) J. Mol. Biol. 291:801.
Hellstern, S. et al. (2002) J. Biol. Chem. 277:15690.
Grassadonia, A. et al. (2004) Glycoconj. J. 19:551.
Jalkanen, K. et al. (2001) Eur. J. Immunol. 31:3075.
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