Mouse SerpinF1 Protein (His Tag)

serine (or cysteine) peptidase inhibitor, clade F, member 1 Protein Datasheet

PEDF / SerpinF1 Protein Price Information

50ug:  Inquiring Price;200ug:  Inquiring Price; ≥1mg Bulk:  Inquiring Price

PEDF / SerpinF1 Protein Product Information

• PEDF Synonym: Serpinf1,RP23-384C18.1, AI195227, EPC-1, Pedf, Pedfl, Sdf3
• Protein Construction: A DNA sequence encoding the extracellular domain (Met 1-Thr 417) of mouse SerpinF1(NP_035470.3) precursor was expressed with a C-terminal polyhistidine tag.
• Source: Mouse
• Expression Host: Human Cells

PEDF / SerpinF1 Protein QC Testing

• Purity: > 95%, as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per 1μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Gln 20
• Molecular Mass: The secreted recombinant mouse SerpinF1consists of 409 amino acids and has a calculated molecular mass of 45.8 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 60-65 kDa protein in SDS-PAGE under reducing conditions.
• Formulation: Lyophilized from sterile PBS , pH 7.4
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE:

PEDF / SerpinF1 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted and be used as soon as possible. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

PEDF / SerpinF1 Protein Description

Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit chymotrypsin-like serine proteases (serine protease inhibitors). As the largest and most diverse family of protease inhibitors, serpins are expressed in a cell-specific manner and over 1000 serpins have been identified in human, plants, fungi, bacteria, archaea and certain viruses. The superfamily of serine proteinase inhibitors are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression. SerpinF1, also known as Pigment epithelium-derived factor (PEDF), is a 50 kDa secreted glycoprotein exhibiting no serine protease inhibitory activity, as it does not undergo the S to R conformational transition characteristic of active serpins. Mouse SerpinF1 is highly expressed in the liver, gastric glandular mucosa and renal tubules. SerpinF1 has been described as a natural and potent angiogenesis inhibitor with neurotrophic and immune-modulation properties. SerpinF1 exerts actions via multiple high affinity ligands and cell receptors, and thus balances angiogenesis in the eye and blocks tumor progression.

References

1. Irving, J. A. et al., 2000, Genome Res. 10: 1845–1864.
2. Irving, J. et al., 2002, Mol Biol Evol. 19 (11): 1881–1890.
3. van Gent, D. et al., 2003, Int J Biochem Cell Biol. 35 (11):1536-1547.
4. Rawlings, N.D. et al., 2004, Biochem J. 378: 705–716.
5. Filleur, S. et al., 2009, J Cell Biochem 106 (5):769-775.