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TPP1 Protein, Mouse, Recombinant (His)

TPP1 Protein, Mouse, Recombinant (His)

产品编号 TMPY-05215
别名: TPP-1, TPP-I, tripeptidyl peptidase I, LPIC, Cln2

Tripeptidyl-peptidase 1 (TPP1 / CLN2) is a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. TPP1 / CLN2 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.

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TPP1 Protein, Mouse, Recombinant (His)
规格 价格/CNY 货期 数量
50 μg ¥ 3,820 5日内发货
千万补贴 助力科研
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产品目录号及名称: TPP1 Protein, Mouse, Recombinant (His) (TMPY-05215)
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生物活性 Testing in progress
产品描述 Tripeptidyl-peptidase 1 (TPP1 / CLN2) is a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. TPP1 / CLN2 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.
种属 Mouse
表达系统 Baculovirus-Insect Cells
标签 His
蛋白编号 O89023
别名 TPP-1, TPP-I, tripeptidyl peptidase I, LPIC, Cln2
蛋白构建 A DNA sequence encoding the mouse TPP1 (NP_034036.1) (Met1-Pro562) was expressed with a polyhistidine tag at the C-terminus.
蛋白纯度 > 95 % as determined by SDS-PAGE.
分子量 Approxiamtely 60.9 kDa
内毒素 < 1.0 EU per μg protein as determined by the LAL method.
缓冲液 Lyophilized from sterile 20 mM Tris, 150 mM NaCl, pH 7.5, 10 % glycerol. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
复溶方法 A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
存储

Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

运输方式

In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.

研究背景 Tripeptidyl-peptidase 1 (TPP1 / CLN2) is a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. TPP1 / CLN2 may act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Defects in TPP1 / CLN2 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2), a form of neuronal ceroid lipofuscinosis which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy.

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Keywords

TPP1 Protein, Mouse, Recombinant (His) TPP-1 TPP-I tripeptidyl peptidase I LPIC TPP1 Cln2 TPP 1 recombinant recombinant-proteins proteins protein

 

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