关键信息
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基因名
NJMU-R1
- 应用
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别名
C17orf75Protein Njmu-R1
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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
Q9HAS0
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表达区间
1-396 aa
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氨基酸序列
MLPSLQESMD GDEKELESSE EGGSAEERRL EPPSSSHYCL YSYRGSRLAQ QRGDSEDGSP SGTNAETPSG DDFSLSLADT NLPSEVEPEL RSFIAKRLSR GAVFEGLGNV ASVELKIPGY RVGCYYCLFQ NEKLLPETVT IDSERNPSEY VVCFLGGSEK GLELFRLELD KYIQGLKNNM NCEARGLESH IKSYLSSWFE DVVCPIQRVV LLFQEKLTFL LHAALSYTPV EVKESDEKTK RDINRFLSVA SLQGLIHEGT MTSLCMAMTE EQHKSVVIDC SSSQPQFCNA GSNRFCEDWM QAFLNGAKGG NPFLFRQVLE NFKLKAIQDT NNLKRFIRQA EMNHYALFKC YMFLKNCGSG DILLKIVKVE HEEMPEAKNV IAVLEEFMKE ALDQSF
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分子量
44.6 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.
质检流程
相关产品
背景信息
The NJMU-R1 recombinant protein has garnered significant interest in the field of biomedical research due to its potential applications in therapeutic interventions and vaccine development. Research surrounding NJMU-R1 is rooted in understanding its role as an immunogenic protein derived from the pathogen NJMU, which is linked to various infectious diseases. Enhanced knowledge of NJMU-R1 is critical in elucidating the mechanisms of immune responses, as it can stimulate both humoral and cellular immunity in host organisms. The recombinant expression of NJMU-R1 facilitates the production of this protein in a controlled environment, allowing for detailed biochemical characterization and assessment of its immunogenic properties. Furthermore, studies leveraging NJMU-R1 are fundamental in exploring its efficacy as a candidate for vaccine formulations, with the aim of inducing protective immunity against NJMU-associated diseases. The strategic development and manipulation of NJMU-R1 not only contribute to our understanding of host-pathogen interactions but also hold promise for innovative therapeutic avenues in combating infectious diseases. Overall, this research paves the way for advancements in vaccine technology and opens new doors for immunological studies.
