Analytical Data
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基因名
LBH
- Application
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别名
LBH;Protein LBH
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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
Q53QV2
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表达区间
1-105aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSMSIYFPI HCPDYLRSAK MTEVMMNTQP MEEIGLSPRK DGLSYQIFPD PSDFDRCCKL KDRLPSIVVE PTEGEVESGE LRWPPEEFLV QEDEQDNCEE TAKENKEQ
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分子量
15 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
The study of LBH (Limb-Bud-Heart) recombinant proteins has gained significant attention due to their crucial role in embryonic development and organogenesis. LBH is a nuclear protein that has been implicated in various cellular processes, including cell proliferation, differentiation, and signaling pathways critical for the formation of limbs and the heart. Disruptions in LBH expression or function have been associated with congenital heart defects and limb malformations, making it a focus of developmental biology and medical research. Researchers have been particularly interested in producing recombinant LBH proteins to analyze their structure-function relationships and interactions with other regulatory factors. The availability of purified LBH proteins enables detailed biochemical and biophysical studies that can elucidate its role in developmental processes and its potential involvement in pathologies. Furthermore, understanding the signaling mechanisms mediated by LBH can provide insights into therapeutic targets for genetic disorders. Overall, the exploration of LBH recombinant proteins not only enhances our comprehension of developmental biology but also holds promise for innovative strategies in regenerative medicine and interventions for congenital anomalies.
