rHuFlt-3 Ligand GMP

Escherichia coli

> 98% by SDS-PAGE and HPLC analyses.

Approximately 17.6 kDa, a single non-glycosylated polypeptide chain containing 155 amino acids.

TQDCSFQHSP ISSDFAVKIR ELSDYLLQDY PVTVASNLQD EELCGGLWRL VLAQRWMERL KTVAGSKMQG LLERVNTEIH FVTKCAFQPP PSCLRFVQTN ISRLLQETSE QLVALKPWIT RQNFSRCLEL QCQPDSSTLP PPWSPRPLEA TAPTA

> 1.0 × 10⁶ U/mg

Sterile filtered white lyophilized (freeze-dried) powder.

Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.0.

Store at -15℃ to -20℃

The product is shipped with polar packs.

Less than 0.01 EU/μg

Less than 0.05%

Less than 20 ng/mg

Prior to opening, it is recommended to centrifuge the vial briefly to bring the contents down the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. If animal-origin-free condition is expected in your product, then sterile distilled water is recommended. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

For research or further manufacturing use only, not for direct human use.

Conforms

Negative

Negative

Flt-3 ligand (FL) is a recently identified hematopoietic cytokine whose activities are mediated by binding to the transmembrane glycoprotein Flt-3. Flt-3 was first discovered as a member of the class III subfamily of receptor tyrosine kinases (RTK) whose expression among hematopoietic cells was found to be restricted to highly enriched stem/progenitor cell populations. Additionally, class III RTKs include the receptors from SCF, M-CSF and PDGF. Not surprisingly, Flt-3 ligand is also structurally related to M-CSF and SCF. All three cytokines have been shown to exist both as type I transmembrane proteins and as soluble proteins. The predominant human FL isoform is a transmembrane protein that can undergo proteolytic cleavage to generate a soluble form of the protein. An alternatively-spliced FL mRNA, encoding a soluble form of the human FL, has also been identified. FL is widely expressed in various human and mouse tissues. At the amino acid sequence level, human and mouse FL are approximately 72% identical and the two proteins exhibit cross-species activity. FL has been shown to synergize with a wide variety of hematopoietic cytokines to stimulate the growth and differentiation of early hematopoietic progenitors.