Analytical Data
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基因名
GP
- Application
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别名
GP；Pancreatic secretory granule membrane major glycoProtein GP2
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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
P55259
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表达区间
1-537aa
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氨基酸序列
MPHLMERMVGSGLLWLALVSCILTQASAVQRGYGNPIEASSYGLDLDCGAPGTPEAHVCFDPCQNYTLLDEPFRSTENSAGSQGCDKNMSGWYRFVGEGGVRMSETCVQVHRCQTDAPMWLNGTHPALGDGITNHTACAHWSGNCCFWKTEVLVKACPGGYHVYRLEGTPWCNLRYCTVPRDPSTVEDKCEKACRPEEECLALNSTWGCFCRQDLNSSDVHSLQPQLDCGPREIKVKVDKCLLGGLGLGEEVIAYLRDPNCSSILQTEERNWVSVTSPVQASACRNILERNQTHAIYKNTLSLVNDFIIRDTILNINFQCAYPLDMKVSLQAALQPIVSSLNVSVDGNGEFIVRMALFQDQNYTNPYEGDAVELSVESVLYVGAILEQGDTSRFNLVLRNCYATPTEDKADLVKYFIIRNSCSNQRDSTIHVEENGQSSESRFSVQMFMFAGHYDLVFLHCEIHLCDSLNEQCQPSCSRSQVRSEVPAIDLARVLDLGPITRRGAQSPGVMNGTPSTAGFLVAWPMVLLTVLLAWLF
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分子量
59.4 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
GP recombinants, or glycoprotein recombinants, have garnered significant attention in biomedical research due to their pivotal role in various physiological and pathological processes. The research background of GP recombinant proteins is rooted in their relevance to infectious diseases, vaccine development, and therapeutic interventions. Glycoproteins, characterized by the presence of carbohydrate moieties, are crucial for the attachment and entry of viruses into host cells, making them prime candidates for targeting in vaccine design. Advances in genetic engineering have enabled the production of these proteins in heterologous systems, facilitating large-scale generation and purification. This capability is instrumental in understanding viral mechanisms, eliciting immune responses, and developing novel vaccines against diseases such as HIV, influenza, and emerging viral infections. Moreover, GP recombinants serve as essential tools in studying protein structure-function relationships and developing therapeutic antibodies. As the field continues to evolve, ongoing research aims to refine expression systems and enhance the immunogenicity of GP-based vaccines, offering promising strategies to combat infectious diseases and improve public health outcomes.
