Analytical Data
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基因名
TULP1
- Application
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别名
TULP1；TUBL1；Tubby-related Protein 1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O00294
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表达区间
290-542aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE
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分子量
31 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
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.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
TULP1 (tubby-like protein 1) is a member of the Tubby gene family, primarily associated with neuronal function and the development of photoreceptor cells in the retina. Mutations in TULP1 have been linked to inherited retinal disorders, such as retinal degeneration and retinitis pigmentosa, which lead to progressive vision loss. Understanding TULP1 and its functional mechanisms is critical for unraveling the pathogenesis of these conditions. Research has focused on the reconstitution of TULP1 protein to elucidate its structure, interaction with other cellular components, and its role in the phototransduction pathway. Advances in recombinant protein technology have facilitated the production of TULP1 in various expression systems, enabling detailed biochemical studies and the exploration of its signaling pathways. Moreover, TULP1's involvement in the trafficking of photoreceptor proteins within the cell provides insights into potential therapeutic targets. Consequently, the investigation of TULP1 not only enhances our knowledge of retinal biology but also holds promise for the development of gene therapies aimed at mitigating the effects of related vision disorders.
