Analytical Data
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基因名
FNBP1
- Application
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别名
FNBP1；FBP17；KIAA0554；Formin-binding 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
Q96RU3
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表达区间
1-617aa
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氨基酸序列
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV DLARYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRH QMAEDSKADY SSILQKFNHE QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ VIPIIGKCLD GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP SAVPNGPQSP KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE DFSNLPPEQR RKKLQQKVDE LNKEIQKEMD QRDAITKMKD VYLKNPQMGD PASLDHKLAE VSQNIEKLRV ETQKFEAWLA EVEGRLPARS EQARRQSGLY DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD DEFDDEEPLP AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY VPTSYVEVCL DKNAKDS
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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
FNBP1 (F-BAR domain containing protein 1) is a vital protein involved in various cellular processes, including membrane dynamics, endocytosis, and cytoskeletal organization. Its F-BAR domain plays a crucial role in sensing and inducing membrane curvature, thereby facilitating the formation of membrane protrusions. Dysregulation of FNBP1 has been linked to several diseases, including cancer and neurodegenerative disorders, making it a significant target for research. Investigating FNBP1 through the development of recombinant proteins has become essential for understanding its structure-function relationships and interactions with other cellular components. Recombinant FNBP1 proteins can be used in various biochemical assays and structural studies to elucidate the mechanisms underlying its cellular roles. By studying FNBP1, researchers hope to uncover novel therapeutic strategies to target its dysregulation in disease contexts. This research is particularly relevant in the fields of cell biology and medicine, as knowledge about FNBP1 can further our understanding of fundamental cellular processes and their implications in health and disease.
