Analytical Data
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基因名
ATP6V1B2
- Application
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别名
V-ATPase subunit B 2;Endomembrane proton pump 58 kDa subunit;HO57;Vacuolar proton pump subunit B 2
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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
P21281
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表达区间
1-511aa
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氨基酸序列
MALRAMRGIVNGAAPELPVPTGGPAVGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH
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分子量
61.5 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
ATP6V1B2, a subunit of the vacuolar ATPase (V-ATPase) complex, plays a crucial role in cellular acidification and membrane traffic regulation. This enzyme is responsible for transporting protons across cellular membranes, thereby maintaining pH balance and contributing to various cellular processes, including nutrient uptake, protein degradation, and ion homeostasis. Aberrant expression or mutations in ATP6V1B2 have been linked to several diseases, including renal tubular acidosis and cancer, highlighting its significance in cellular physiology and pathology. Research into recombinant ATP6V1B2 proteins is essential for elucidating its structural and functional properties, facilitating studies on V-ATPase assembly and its interaction with other cellular components. Moreover, understanding the dynamics of ATP6V1B2 can provide insights into therapeutic targets for diseases characterized by V-ATPase dysregulation. Overall, the study of ATP6V1B2 recombinant proteins represents a vital step in comprehensively understanding the role of V-ATPase in health and disease.
