0 products, total $0.+86-400-890-9989      Login |  Register 中文한국어

Browse By Molecule:

Your Position: Home > Recombinant Protein > Human Cell Expressed > SerpinF2 / SERPINF2 Protein (His Tag)

SerpinF2 / SERPINF2 Protein (His Tag) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
10297-H08H
  YES          

Alpha-2-antiplasmin ( SerpinF2 / SERPINF2 / AAP ) Protein

 

SerpinF2 / SERPINF2 / AAP Protein Price Inquiry ( Available Sizes )

SerpinF2 / SERPINF2 / AAP Protein Product Information

Synonym : SerpinF2,   AAP,   API,   PLI,   α-2 AP,   ALPHA-2-PI
Protein Construction:

A DNA sequence encoding the human SerpinF2 ( NP_000925.2 ) ( Met 1 - Lys 491 ) was expressed, with a C-terminal polyhistidine tag

Source: Human
Expression Host: Human Cells

SerpinF2 / SERPINF2 / AAP Protein QC Testing

Purity: > 97 % as determined by SDS-PAGE SDS-PAGE:
Serpin F2 protein

Serpin F2 protein

Bio-activity:

Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate,Mca-RPKPVE-Nval-WRK(Dnp)-NH2 (Anaspec, Catalog#27114)
The IC50 value is < 0.5 nM

Endotoxin: < 1.0 EU per μg 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: Met 28
Molecular Mass:

The recombinant human SerpinF2 consists of 475 amino acids after removal of the signal peptide and predicts a molecular mass of 53.2 kDa. By SDS-PAGE under reducing conditions, the apparent molecular mass of rhSerpinF2 is approximately 70 kDa due to glycosylation

Formulation: Lyophilized from sterile 25mM Tris, 150mM  NaCl, pH 7.5
  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.

SerpinF2 / SERPINF2 / AAP Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. 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.

SerpinF2 / SERPINF2 / AAP Protein Related Products & Topics

Related Areas:

Enzyme>>Protease & Regulator>>Serine Protease & Regulator>>Serpin Superfamily>>SerpinF2

Immunology>>Innate Immunity>>Coagulation>>SerpinF2

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
SerpinF2 Human SerpinF2 Protein, Recombinant 10297-H08H
SerpinF2 Mouse SerpinF2 Protein, Recombinant 50167-M08H

Antibodies:

Molecule Application Description //For Detailed Info. and Price------CLICK! Cat. No
Human
SerpinF2
WB, ELISA SerpinF2 Antibody, Mouse MAb 10297-MM05
Human
SerpinF2
WB, ELISA SerpinF2 Antibody, Rabbit PAb 10297-RP01
Human
SerpinF2
WB, ELISA SerpinF2 Antibody, Rabbit PAb (Antigen Affinity Purified) 10297-RP02
Mouse
SerpinF2
WB, ELISA Rabbit Monoclonal Antibody 50167-R128
Mouse
SerpinF2
WB, ELISA Rabbit Polyclonal Antibody 50167-RP01
Mouse
SerpinF2
WB, ELISA Rabbit Polyclonal Antibody (Antigen Affinity Purified) 50167-RP02

SerpinF2 / SERPINF2 / AAP Protein Description

SerpinF2, also known as alpha-2 antiplasmin (alpha-2 AP), is a member of the Serpin superfamily. SerpinF2 is the principal physiological inhibitor of serine protease plasmin, and as well as, an efficient inhibitor of trypsin and chymotrypsin. This protease is produced mainly by liver and kidney, and also expressed at moderate level in other tissues such as muscle, intestine, central nervous system and placenta. Alpha-2 AP is an unusual serpin in that it contains extensive N- and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. Alpha-2 AP plays the dominant role in inhibiting both plasma clot lysis and thrombus lysis, and accordingly, the deficiency of Alpha-2 antiplasmin in humans results in uncontrolled fibrinolysis and a bleeding disorder.

References

  1. Potempa, J. et al., 1988, Science. 241: 699-700.
  2. Menoud, P.A. et al., 1996, J. Clin. Invest. 97: 2478-2484.
  3. Mutch, NJ. et al., 2007, J. Thromb. Haemost. 5: 812-817.
  4. Victoria, J. et al., 2007, Blood, 109: 5286-5292.