Analytical Data
-
基因名
ATP6V1F
- Application
-
别名
ATP6V1F；ATP6S14；VATF；V-type proton ATPase subunit F
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q16864
-
表达区间
1-119aa
-
氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSMAGRGKL IAVIGDEDTV TGFLLGGIGE LNKNRHPNFL VVEKDTTINE IEDTFRQFLN RDDIGIILIN QYIAEMVRHA LDAHQQSIPA VLEIPSKEHP YDAAKDSILR RARGMFTAED LR
-
分子量
16 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
ATP6V1F is a vital component of the V-ATPase (vacuum-type ATPase) enzyme complex, which plays a critical role in cellular pH regulation, protein sorting, and nutrient transport across cellular membranes. This enzyme is pivotal in various physiological processes, including bone resorption, neurotransmitter release, and the maintenance of acid-base balance. Disruptions in V-ATPase activity have been linked to several diseases, such as osteopetrosis, renal tubular acidosis, and cancer, highlighting the importance of understanding its function and regulation. Recent advancements in recombinant protein technology have enabled the production of ATP6V1F in host systems, facilitating detailed structural and functional studies. Research into the recombinant form of ATP6V1F aims to elucidate its biochemical properties, interaction with other subunits of the V-ATPase complex, and its role in pathological conditions. Such studies are essential for developing potential therapeutic strategies that target V-ATPase activity, offering new avenues for treating diseases associated with its dysregulation.
