Analytical Data
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基因名
SH3GL1
- Application
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别名
SH3GL1；CNSA1；SH3D2B；Endophilin-A2
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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
Q99961
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表达区间
1-368aa
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氨基酸序列
MSVAGLKKQFYKASQLVSEKVGGAEGTKLDDDFKEMEKKVDVTSKAVTEVLARTIEYLQPNPASRAKLTMLNTVSKIRGQVKNPGYPQSEGLLGECMIRHGKELGGESNFGDALLDAGESMKRLAEVKDSLDIEVKQNFIDPLQNLCEKDLKEIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFEESKEVAETSMHNLLETDIEQVSQLSALVDAQLDYHRQAVQILDELAEKLKRRMREASSRPKREYKPKPREPFDLGEPEQSNGGFPCTTAPKIAASSSFRSSDKPIRTPSRSMPPLDQPSCKALYDFEPENDGELGFHEGDVITLTNQIDENWYEGMLDGQSGFFPLSYVEVLVPLPQ
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分子量
45.0 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
SH3GL1, or SH3-domain-containing protein 3 GTPase-activating protein, has garnered significant attention in cellular biology due to its pivotal role in membrane trafficking and cytoskeletal dynamics. This protein is primarily involved in clathrin-mediated endocytosis, where it facilitates the budding and scission of vesicles from the plasma membrane, thereby influencing nutrient uptake and signal transduction. Research has increasingly linked SH3GL1 to various pathological conditions, including cancer and neurodegenerative diseases, suggesting that dysregulation of its activity may disrupt normal cellular functions. Furthermore, studies have highlighted the importance of its SH3 and BAR (Bin/Amphiphysin/Rvs) domains, which are essential for its interactions with other proteins and membrane curvature generation. Understanding the structure and function of SH3GL1 through recombinant protein studies could reveal new insights into its mechanistic roles and regulatory pathways. Such insights may ultimately lead to the development of targeted therapeutic strategies aimed at correcting the aberrant cellular processes associated with SH3GL1 dysfunction, providing a promising avenue for future biomedical research.
