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Z-VDVAD-FMK, CAS 210344-95-9
Z-VDVAD-FMK, CAS 210344-95-9
Artikelnummer
BPS27668-1
Verpackungseinheit
5 mg
Hersteller
BPS Bioscience
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Amino Acid Sequence: Z-Val-Asp(OMe)-Val-Ala-Asp(OMe)-CH2F
Background: VDVAD has been shown to be a preferred cleavage site for caspase-2. Caspase 2 is a very versatile caspase with multiple functions. It is a member of the family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase 2 is part of the Ich-1 subfamily. Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5, and caspase 9. It is produced as a zymogen with a long pro-domain. Pro-caspase-2 contains two subunits, p19 and p12. Caspase 2 associates with several proteins involved in apoptosis via its CARD domain, including RAIDD, ARC, and DEFCAP. Together with RAIDD and PIDD/LRDD, caspase 2 has been shown to form the PIDDosome, which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD. Caspase 2 may also form a complex with the DNA-PKcs and PIDD/LRDD, which is involved in DNA repair after DNA damage.
Biological Activity: We recommend using 2-10 µM for inhibiting caspase activity in cell culture. The optimal dose may vary for different cells and culture conditions.
CAS Number: 210344-95-9
Description: Z-VDVAD-FMK is a synthetic peptide that irreversibly inhibits the activity of caspase-2. It attenuates oxyhemoglobin-induced cleavage of PARP and apoptosis in endothelial cells. Z-VDVAD-FMK can be used for both in vitro and in vivo studies--see note for using this product in vitro.
Purity: ≥90% by HPLC
Solubility: Soluble in DMSO
Storage Stability: Store at or below -20°C. Solid form is stable at least 12 months from date of receipt, when stored as directed. Do not store aqueous solutions for more than one day.
Target: Caspase 2
Biosafety Level: Not applicable (BSL-1)
Amino Acid Sequence: Z-Val-Asp(OMe)-Val-Ala-Asp(OMe)-CH2F
Background: VDVAD has been shown to be a preferred cleavage site for caspase-2. Caspase 2 is a very versatile caspase with multiple functions. It is a member of the family of cysteine proteases called caspases that cleave proteins only at an amino acid following an aspartic acid residue. Within this family, caspase 2 is part of the Ich-1 subfamily. Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5, and caspase 9. It is produced as a zymogen with a long pro-domain. Pro-caspase-2 contains two subunits, p19 and p12. Caspase 2 associates with several proteins involved in apoptosis via its CARD domain, including RAIDD, ARC, and DEFCAP. Together with RAIDD and PIDD/LRDD, caspase 2 has been shown to form the PIDDosome, which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD. Caspase 2 may also form a complex with the DNA-PKcs and PIDD/LRDD, which is involved in DNA repair after DNA damage.
Biological Activity: We recommend using 2-10 µM for inhibiting caspase activity in cell culture. The optimal dose may vary for different cells and culture conditions.
CAS Number: 210344-95-9
Description: Z-VDVAD-FMK is a synthetic peptide that irreversibly inhibits the activity of caspase-2. It attenuates oxyhemoglobin-induced cleavage of PARP and apoptosis in endothelial cells. Z-VDVAD-FMK can be used for both in vitro and in vivo studies--see note for using this product in vitro.
Purity: ≥90% by HPLC
Solubility: Soluble in DMSO
Storage Stability: Store at or below -20°C. Solid form is stable at least 12 months from date of receipt, when stored as directed. Do not store aqueous solutions for more than one day.
Target: Caspase 2
Biosafety Level: Not applicable (BSL-1)
| Artikelnummer | BPS27668-1 |
|---|---|
| Hersteller | BPS Bioscience |
| Hersteller Artikelnummer | 27668-1 |
| Green Labware | Nein |
| Verpackungseinheit | 5 mg |
| Mengeneinheit | STK |
| Produktinformation (PDF) |
|
| MSDS (PDF) |
|
Immer für Sie da
Gernot Ensinger, M.Sc.
Laurent Haze
