Bioactivity: Fully biologically active when compared to standard. The ED₅₀ as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/ml, corresponding to a specific activity of > 100 IU/mg.
Endotoxin Concentration: <1.0 EU/μg
Item Number
rp152656
Grouped product items
SKU
Size
Availability
Price
Qty
rp152656-10μg
10μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$87.90
rp152656-50μg
50μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$327.90
rp152656-100μg
100μg
Available within 4-8 weeks(?)
Items will be manufactured post-order and can take 4-8 weeks. Thank you for your patience!
$597.90
rp152656-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
Fully biologically active when compared to standard. The ED₅₀ as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/ml, corresponding to a specific activity of > 100 IU/mg.
Recombinant Human Trefoil Factor 3 Protein (rp152656)-Protein Bioactivity Fully biologically active when compared to standard. The ED₅₀ as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10 μg/mL, corresponding to a specific activity of > 100 IU/mg.
Recombinant Human Trefoil Factor 3 Protein (rp152656)-SDS-PAGE Recombinant Human Trefoil Factor 3 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining. Showing a single band at 14.5 kDa under reducing conditions and 29 kDa under non-reducing conditions.
Product Specifications
Form
Lyophilized
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportio
Storage Temp
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And 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 reconst
Certificates
Certificate of Analysis(COA)
Enter Lot Number to search for COA:
Find and download the COA for your product by matching the lot number on the packaging.
1.Hauser, F F and 6 more authors.. (1993) hP1.B, a human P-domain peptide homologous with rat intestinal trefoil factor, is expressed also in the ulcer-associated cell lineage and the uterus.. Proceedings of the National Academy of Sciences of the United States of America, (1):[PMID:8346203]
2.Podolsky, D K DK and 7 more authors.. (1993) Identification of human intestinal trefoil factor. Goblet cell-specific expression of a peptide targeted for apical secretion.. The Journal of biological chemistry, (25):[PMID:8454642]
3.Seib, T T and 8 more authors.. (1997) The three human trefoil genes TFF1, TFF2, and TFF3 are located within a region of 55 kb on chromosome 21q22.3.. Genomics, (15):[PMID:9070946]
4.Hattori, M M and 64 more authors.. (2000) The DNA sequence of human chromosome 21.. Nature, (18):[PMID:10830953]
5.Berry, A A and 16 more authors.. (2000) Refined localization of autosomal recessive nonsyndromic deafness DFNB10 locus using 34 novel microsatellite markers, genomic structure, and exclusion of six known genes in the region.. Genomics, (15):[PMID:10950923]
6.Oertel, M M and 5 more authors.. (2001) Trefoil factor family-peptides promote migration of human bronchial epithelial cells: synergistic effect with epidermal growth factor.. American journal of respiratory cell and molecular biology, [PMID:11694446]
7.Casadei, Raffaella R and 10 more authors.. (2003) mRNA 5' region sequence incompleteness: a potential source of systematic errors in translation initiation codon assignment in human mRNAs.. Gene, (4):[PMID:14637006]
8.Muskett, Frederick W FW, May, Felicity E B FE, Westley, Bruce R BR and Feeney, James J.. (2003) Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins.. Biochemistry, (30):[PMID:14690424]
9.Zhang, Zemin Z and Henzel, William J WJ.. (2004) Signal peptide prediction based on analysis of experimentally verified cleavage sites.. Protein science : a publication of the Protein Society, [PMID:15340161]
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