Analytical Data
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基因名
TULP3
- Application
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别名
MGC45295; Tubby like Protein 3; Tubby related Protein 3; Tubby-like Protein 3; Tubby-related Protein 3; TUBL 3; TUBL3; TULP 3; TULP3; TULP3_HUMAN
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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
O75386
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表达区间
1-442 aa
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氨基酸序列
MEASRCRLSP SGDSVFHEEM MKMRQAKLDY QRLLLEKRQR KKRLEPFMVQ PNPEARLRRA KPRASDEQTP LVNCHTPHSN VILHGIDGPA AVLKPDEVHA PSVSSSVVEE DAENTVDTAS KPGLQERLQK HDISESVNFD EETDGISQSA CLERPNSASS QNSTDTGTSG SATAAQPADN LLGDIDDLED FVYSPAPQGV TVRCRIIRDK RGMDRGLFPT YYMYLEKEEN QKIFLLAARK RKKSKTANYL ISIDPVDLSR EGESYVGKLR SNLMGTKFTV YDRGICPMKG RGLVGAAHTR QELAAISYET NVLGFKGPRK MSVIIPGMTL NHKQIPYQPQ NNHDSLLSRW QNRTMENLVE LHNKAPVWNS DTQSYVLNFR GRVTQASVKN FQIVHKNDPD YIVMQFGRVA DDVFTLDYNY PLCAVQAFGI GLSSFDSKLA CE
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分子量
49.6 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
TULP3, a member of the TULP family of proteins, is crucial in the signaling pathways of photoreceptor cells in the retina. Understanding TULP3's role is essential because its dysfunction has been linked to retinal degenerative disorders, such as retinitis pigmentosa. Structural studies of TULP3, particularly its ability to bind to phosphoinositides, are crucial for elucidating its function in membrane trafficking and signaling. This research aims to explore the biochemical properties and structural features of TULP3 to better understand how it interacts with cellular membranes and signaling molecules. By characterizing the recombinant TULP3 protein, researchers strive to uncover the molecular mechanisms behind photoreceptor cell maintenance and survival. Ultimately, insights gleaned from TULP3 studies may pave the way for therapeutic strategies to combat retinal diseases, highlighting the protein's significance beyond basic biology to potential clinical applications.
