产品名称
Hexokinase II VDAC Binding Domain Peptide, Cell-Permeable, A cell-permeable peptide analog of Hexokinase II VDAC binding domain peptide.
assay
≥95% (HPLC)
form
lyophilized solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated (hygroscopic)
protect from light
color
white
solubility
water: 1 mg/mL
shipped in
wet ice
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
Cell permeable: yes
Primary Target
Detach and translocate HXK2 from mitochondria to the cytosol
Detach and translocate HXK2 from mitochondria to the cytosol
Product does not compete with ATP.
Reversible: no
Disclaimer
Toxicity: Standard Handling (A)
General description
A cell-permeable peptide analog of Hexokinase II VDAC binding domain peptide (Cat. No. 376815). The internalization domain of the Antennapedia homeoprotein is fused to the methionine amino terminal. Shown to completely detach and translocate HXK2 from mitochondria to the cytosol in HeLa cells at 100 µM. Does not induce Bax translocation or cytochrome c release when used alone. However, it markedly sensitizes cells to cytochrome c release and to the induction of apoptosis when used in combination with a Bax-dependent apoptosis inducer, Indomethacin (Cat. No. 405268).
Other Notes
H-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-Met-Ile-Ala-Ser-His-Leu-Leu-Ala-Tyr-Phe-Phe-Thr-Glu-Leu-Asn-NH₂
Pastorino, J.G., et al. 2002. J. Biol. Chem.277, 7610.
Holinger, E.P., et al. 1999. J. Biol. Chem.274, 13298.
Sui, D., and Wilson, J.E. 1997. Arch. Biochem. Biophys.345, 111.
Holinger, E.P., et al. 1999. J. Biol. Chem.274, 13298.
Sui, D., and Wilson, J.E. 1997. Arch. Biochem. Biophys.345, 111.
Packaging
Packaged under inert gas
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Jia Sun et al.
Redox biology, 39, 101811-101811 (2020-12-29)
Vascular complications of diabetes are a serious challenge in clinical practice, and effective treatments are an unmet clinical need. Acidic fibroblast growth factor (aFGF) has potent anti-oxidative properties and therefore has become a research focus for the treatment of diabetic
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