FK506 Binding Protein-12 (FKBP12, FKBP1A), human recombinant

FK506 binding protein, is a family of proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not in amino acid sequence. FKBPs have been identified in many eukaryotes from yeast to humans and function as protein folding chaperones for proteins containing proline residues. Along with cyclophilin, FKBPs belong to the immunophilin family.

FKBP12 is notable in humans for binding the immunosuppressant molecule tacrolimus (originally designated FK506), which is used in treating patients after organ transplant and patients suffering from autoimmune disorders. Tacrolimus has been found to reduce episodes of organ rejection over a related treatment, the drug ciclosporin, which binds cyclophilin

This highly pure protein is suitable for the study of protein crystallization, enzyme kinetics, inhibitor screening, inhibitor design and selectivity profiling.

 

Bulk pricing is available for large quantities upon request. Ask us for a quote.

Catalog Number Product Size AVAILABILITY Price Qty
FCA007
FK506 Binding Protein-12 (FKBP12, FKBP1A, mTOR), human recombinant
25ug (15.4mg/mL) In stock
Price: $209.00
Specifications
Product Type: Protein
Source: E. coli
Molecular Weight: 12.24 kDa
Purity: > 95% (densitometry)
Buffer: 50 mM HEPES-pH 7.5, 0.5 mM DTT, 0.5 mM EDTA, and 2.5 % glycerol.
Concentration: 15.4mg/mL
Storage: Stable > 12 months -80C
Shipped: Dry ice
Comments

SDS-Page:

Binding Characteristics:  Assay conditions: 50 mM HEPES, pH 7.8, +50 nM FKBP12, plus titrated FK506 (titration range 200-3.125 nM) incubated at 24C for 30 min. Add 200 ?M substrate (suc-Ala-Phe-Pro-Phe-pNA) followed by addition of chymotrypsin (50 ?g/ml) in a final volume of 100 ?l. Absorbance (A390) was then measured every 4 sec at 24oC for 2 min. Inhibition values were calculated by comparing the rates of FKBP12-specific substrate cleavage in the presence and absence of FK506. FK506 IC50 = 37 nM.
Crystallography: apo FKBP12 crystals (right) diffract to 1.6 Å resolution using in-house X-ray source.
References

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