Analytical Data
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基因名
CAPN5
- Application
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别名
CAPN5；NCL3；Calpain-5
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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
O15484
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表达区间
1-640aa
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氨基酸序列
MFSCVKPYED QNYSALRRDC RRRKVLFEDP LFPATDDSLY YKGTPGPAVR WKRPKGICED PRLFVDGISS HDLHQGQVGN CWFVAACSSL ASRESLWQKV IPDWKEQEWD PEKPNAYAGI FHFHFWRFGE WVDVVIDDRL PTVNNQLIYC HSNSRNEFWC ALVEKAYAKL AGCYQALDGG NTADALVDFT GGVSEPIDLT EGDFANDETK RNQLFERMLK VHSRGGLISA SIKAVTAADM EARLACGLVK GHAYAVTDVR KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WNGPWSDTSE EWQKVSKSER EKMGVTVQDD GEFWMTFEDV CRYFTDIIKC RVINTSHLSI HKTWEEARLH GAWTLHEDPR QNRGGGCINH KDTFFQNPQY IFEVKKPEDE VLICIQQRPK RSTRREGKGE NLAIGFDIYK VEENRQYRMH SLQHKAASSI YINSRSVFLR TDQPEGRYVI IPTTFEPGHT GEFLLRVFTD VPSNCRELRL DEPPHTCWSS LCGYPQLVTQ VHVLGAAGLK DSPTGANSYV IIKCEGDKVR SAVQKGTSTP EYNVKGIFYR KKLSQPITVQ VWNHRVLKDE FLGQVHLKAD PDNLQALHTL HLRDRNSRQP SNLPGTVAVH ILSSTSLMAV
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分子量
73.1 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
Related Products
Protein Description
CAPN5, a member of the calpain family of cysteine proteases, has garnered significant attention in recent years due to its potential roles in various biological processes and diseases. This enzyme is primarily expressed in the retina and has been implicated in the regulation of cell survival, apoptosis, and inflammatory responses. Research has shown that CAPN5 may play a crucial role in retinal diseases, making it a target for therapeutic interventions. The study of recombinant CAPN5 protein allows for a better understanding of its functional properties and interactions with other cellular components. Investigating its structure and enzymatic activity can provide insights into its mechanism of action and its involvement in pathological conditions. Furthermore, the recombinant expression of CAPN5 facilitates the development of specific inhibitors or modulators, which could serve as potential treatments for diseases linked to its dysregulation. With advancements in recombinant DNA technology, scientists can produce CAPN5 in various systems, enabling detailed studies on its enzymatic functionalities and interactions within the cellular environment, thereby advancing our knowledge of its biological significance and therapeutic potential.
