Analytical Data
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基因名
LMLN
- Application
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别名
LMLN; Leishmanolysin-like peptidase; EC 3.4.24.-; Invadolysin
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q96KR4
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表达区间
1-655aa
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氨基酸序列
MVTTLGPKMAAEWGGGVGYSGSGPGRSRWRWSGSVWVRSVLLLLGGLRASATSTPVSLGSSPPCRHHVPSDTEVINKVHLKANHVVKRDVDEHLRIKTVYDKSVEELLPEKKNLVKNKLFPQAISYLEKTFQVRRPAGTILLSRQCATNQYLRKENDPHRYCTGECAAHTKCGPVIVPEEHLQQCRVYRGGKWPHGAVGVPDQEGISDADFVLYVGALATERCSHENIISYAAYCQQEANMDRPIAGYANLCPNMISTQPQEFVGMLSTVKHEVIHALGFSAGLFAFYHDKDGNPLTSRFADGLPPFNYSLGLYQWSDKVVRKVERLWDVRDNKIVRHTVYLLVTPRVVEEARKHFDCPVLEGMELENQGGVGTELNHWEKRLLENEAMTGSHTQNRVLSRITLALMEDTGRQMLSPYCDTLRSNPLQLTCRQDQRAVAVCNLQKFPKPLPQEYQYFDELSGIPAEDLPYYGGSVEIADYCPFSQEFSWHLSGEYQRSSDCRILENQPEIFKNYGAEKYGPHSVCLIQKSAFVMEKCERKLSYPDWGSGCYQVSCSPQGLKVWVQDTSYLCSRAGQVLPVSIQMNGWIHDGNLLCPSCWDFCELCPPETDPPATNLTRALPLDLCSCSSSLVVTLWLLLGNLFPLLAGFLLCIWH
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分子量
99 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
LMLN, or Lactic Acid Bacteria Mannan-Like Protein, is a recombinant protein that has garnered attention in biomedical research due to its potential applications in various fields, including immunology, nutrition, and biotechnology. The study of LMLN is rooted in the significance of protein engineering and recombinant DNA technology, enabling scientists to manipulate genetic sequences for the production of proteins with specific desired characteristics. Lactic acid bacteria, known for their probiotic properties, provide a natural source of such proteins, which can be harnessed for enhancing immune responses, improving gut health, and developing novel therapeutic strategies. Researchers are investigating the functional properties of LMLN, focusing on its interactions with the immune system and its ability to modulate inflammatory responses. Given the increasing interest in sustainable and health-promoting food ingredients, the exploration of LMLN's biochemical properties and mechanisms of action is paving the way for innovative applications in functional foods and supplements. Furthermore, as the demand for effective delivery systems for vaccines and therapeutics grows, understanding the potential of LMLN as an adjuvant or carrier protein offers promising pathways for improving vaccine efficacy and developing targeted drug delivery methods. Overall, the research surrounding LMLN represents a confluence of microbiology, molecular biology, and biotechnology, aimed at translating scientific insights into practical health benefits and contributing to the advancement of personalized medicine and nutrition.
