Suc-Leu-Leu-Val-Tyr-AMC | Cytiva思拓凡-Whatman滤纸滤膜滤器

Suc-Leu-Leu-Val-Tyr-AMC; 纯度: 98.87%

Suc-Leu-Leu-Val-Tyr-AMC 是一种荧光底物。

Suc-Leu-Leu-Val-Tyr-AMC Chemical Structure

CAS No. : 94367-21-2

规格	价格	是否有货	数量
1 mg	￥660	In-stock
5 mg	￥1300	In-stock
10 mg	;	询价	;
50 mg	;	询价	;

* Please select Quantity before adding items.

Suc-Leu-Leu-Val-Tyr-AMC 相关产品

bull;相关化合物库:

Bioactive Compound Library Plus
Peptide Library

生物活性

Suc-Leu-Leu-Val-Tyr-AMC is a fluorogenic substrate.

体外研究
(In Vitro)

Suc-Leu-Leu-Val-Tyr-AMC (Suc-LLVY) is a membrane-permeable calpain-specific fluorogenic substrate, pteolytic hydrolysis of the peptidyl-7-amino bond liberates the highly fluorescent 7-amino-4-methylcoumarin (AMC) moiety^[1]. The effect of TGF-β on hydrolysis of these substrates (e.g Suc-Leu-Leu-Val-Tyr-AMC) are assessed. Biliary epithelial H69 cells are incubated with 10, 1, 0.1, or 0 ng/mL TGF-β for 24 h. Substrate hydrolysis is then fluorometrically assessed in cytosolic extracts. Basal activity is 1.12, 8.33, and 14.52 nmol AMC/mg protein/min for suc-LLVY-AMC, z-LLE-AMC, and z-LLL-AMC hydrolysis, respectively^[2].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

分子量

763.88

Formula

C₄₀H₅₃N₅O₁₀

CAS 号

94367-21-2

Sequence

Suc-Leu-Leu-Val-Tyr

Sequence Shortening

Suc-LLVY

运输条件

Room temperature in continental US; may vary elsewhere.

储存方式

Protect from light, stored under nitrogen

Powder	-80deg;C	2 years
	-20deg;C	1 year

*In solvent : -80deg;C, 6 months; -20deg;C, 1 month (protect from light, stored under nitrogen)

溶解性数据

In Vitro:;

DMSO : ≥ 20 mg/mL (26.18 mM)

* “≥” means soluble, but saturation unknown.

配制储备液

浓度溶剂体积质量	1 mg	5 mg	10 mg

1 mM	1.3091 mL	6.5455 mL	13.0911 mL
5 mM	0.2618 mL	1.3091 mL	2.6182 mL
10 mM	0.1309 mL	0.6546 mL	1.3091 mL

请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。
储备液的保存方式和期限：-80°C, 6 months; -20°C, 1 month (protect from light, stored under nitrogen)。-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。

参考文献

[1]. Roberta L. Debiasi, et al. Reovirus-Induced Apoptosis Is Preceded by Increased Cellular Calpain Activity and Is Blocked by Calpain Inhibitors. J Virol. 1999 Jan; 73(1): 695–701.

[2]. Tadlock L, et al. Transforming growth factor-beta inhibition of proteasomal activity: a potential mechanism of growth arrest. Am J Physiol Cell Physiol. 2003 Aug;285(2):C277-85. Epub 2003 Mar 19.

[3]. Gardner RC, et al. Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells. Biochem J. 2000 Mar, 2:447-54.

Kinase Assay ^[3]	Immunoprecipitation is carried out for the two sets of samples, using the same amount of protein. The 20 S and 26 S proteasome immunoprecipitates are washed with 50 mM Hepes/KOH (pH 7.5), and 50 mM Hepes/KOH (pH 7.5) containing 2 mMATP, respectively, prior to the determination of peptidase activity using 50 μM suc-Leu- Leu-Val-Tyr-AMC as substrate in these buffers^[3]. MCE has not independently confirmed the accuracy of these methods. They are for reference only.
参考文献	[1]. Roberta L. Debiasi, et al. Reovirus-Induced Apoptosis Is Preceded by Increased Cellular Calpain Activity and Is Blocked by Calpain Inhibitors. J Virol. 1999 Jan; 73(1): 695–701. [2]. Tadlock L, et al. Transforming growth factor-beta inhibition of proteasomal activity: a potential mechanism of growth arrest. Am J Physiol Cell Physiol. 2003 Aug;285(2):C277-85. Epub 2003 Mar 19. [3]. Gardner RC, et al. Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells. Biochem J. 2000 Mar, 2:447-54.

Kinase Assay
^[3]

Immunoprecipitation is carried out for the two sets of samples, using the same amount of protein. The 20 S and 26 S proteasome immunoprecipitates are washed with 50 mM Hepes/KOH (pH 7.5), and 50 mM Hepes/KOH (pH 7.5) containing 2 mMATP, respectively, prior to the determination of peptidase activity using 50 μM suc-Leu- Leu-Val-Tyr-AMC as substrate in these buffers^[3].

MCE has not independently confirmed the accuracy of these methods. They are for reference only.

参考文献

[1]. Roberta L. Debiasi, et al. Reovirus-Induced Apoptosis Is Preceded by Increased Cellular Calpain Activity and Is Blocked by Calpain Inhibitors. J Virol. 1999 Jan; 73(1): 695–701.

[2]. Tadlock L, et al. Transforming growth factor-beta inhibition of proteasomal activity: a potential mechanism of growth arrest. Am J Physiol Cell Physiol. 2003 Aug;285(2):C277-85. Epub 2003 Mar 19.

[3]. Gardner RC, et al. Characterization of peptidyl boronic acid inhibitors of mammalian 20 S and 26 S proteasomes and their inhibition of proteasomes in cultured cells. Biochem J. 2000 Mar, 2:447-54.