>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
40 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in HCl.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile 4 mM HCl.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Tsukushi/TSK Protein, CF
E2IG4
E2IG4E2-induced gene 4 protein
leucine rich repeat containing 54
Leucine-rich repeat-containing protein 54
LRRC54
TSK
TSKtsukushi homolog
TSKU
tsukushi small leucine rich proteoglycan homolog (Xenopus laevis)
Tsukushi
tsukushi, small leucine rich proteoglycan
tsukushin
Background
TSK, also known as Tsukushi, is an atypical member of the small leucine-rich proteoglycan (SLRP) family of extracellular matrix proteins (1, 2). All contain leucine-rich repeats (LRR) flanked by conserved cysteines, but the C-terminus of TSK resembles the structure of nyctalopin and chondroadherin rather than class I - III SLRPs (1). The human TSK cDNA encodes a 16 amino acid (aa) signal sequence and a 337 aa secreted (presumably glycosylated) protein that contains nine LRR (2). Proteoglycan modification of TSK has not been shown. SLRP-like activity or expression of TSK has been identified in several contexts. TSK mRNA is upregulated by estrogen treatment in breast cancer cell lines, and so is proposed to be involved in hormonally regulated extracellular matrix remodeling (2). TSK is upregulated along with bone markers in Vitamin K2-treated osteosarcoma cell lines, mediated by the pregnane X receptor, PXR (3). TSK was also shown to contribute to vitamin K2-mediated enhancement of collagen accumulation. Other SLRPs have been shown to form a protective coat around collagen fibrils, shielding them from proteolysis (4). In rats, expression of TSK in liver, intestines and islets of Langerhans resembles the pattern of Glut2 (5). TSK transcription is upregulated by both estrogen and insulin in hepatocytes. In Xenopus and chick embryos, TSK is expressed in the middle primitive streak, where it binds and antagonizes BMP-4 and promotes dorsalization and formation of the neural crest and the primitive organizer (6, 7). Xenopus TSK also binds the extracellular region of delta-1, modulating Notch activity (7). Human TSK shows 87%, 86%, 86%, 85%, 52% and 50% aa identity with canine, mouse, rat, bovine, chick, and Xenopus TSK, respectively, with the highest identity in the first four LRR.
McEwan, P.A. et al. (2006) J. Struct. Biol. 155:294.
Charpentier, A.H. et al. (2000) Cancer Res. 60:5977.
Ichikawa, T. et al. 2006, J. Biol. Chem. 281:16927.
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