Analytical Data
-
基因名
ADAM5P
- Application
-
别名
ADAM5; ADAM5P; TMDC2; Putative disintegrin and metalloProteinase domain-containing Protein 5
-
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
Q6NVV9
-
表达区间
1-412aa
-
氨基酸序列
MQTSILIKSS CRPQFQRRFH HRMQKQIQNI ISILSSASVI NSYDENDIRH SKPLLVQMDC NYNGYVAGIP NSLVTLSVCS GLRGTMQLKN ISYGIEPMEA VSGFIHKIYE EKYADTNILL EENDTYTWFN SEYQVRKSSE KTDFIKLFPR YIEMHIVVDK NLFKPANMIC RKSVGKECDF TEYCNGDLPY CLPDTYVRDG EYCDSGGAFC FQGKCRTFDK QCDDLIGRGS RGAPVFCYDE INTRGDNFGN CGTAHCLFQH ILCGKLVCTW EHRDLISRPN LSVIYAHVRD QTCVSTYLPR RTPPPVNSPI SITSYYSAED RDETFVQDGS MCGPDMYCFE MHCKHVRFLM NLKLCDASNH CDRHGVCNNF NHCHCEKGYN PPYCQPKQGA FGSIDDGHLV PPTERSYMEE GR
-
分子量
47.1 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
ADAM5P, a member of the ADAM (A Disintegrin and Metalloproteinase) family, is a protein that plays a crucial role in various biological processes, including cell adhesion, migration, and proteolytic activity. Recent studies have suggested that ADAM5P may be involved in the modulation of inflammatory responses and the progression of certain diseases, such as cancer and neurodegenerative disorders. Its unique structure, characterized by a disintegrin-like domain and a metalloproteinase domain, enables it to interact with various substrates and signaling molecules, thereby influencing cellular behavior. Research has focused on the functional characterization of ADAM5P and its potential as a therapeutic target. The development of recombinant ADAM5P protein has opened avenues for detailed biochemical and biophysical studies, allowing scientists to investigate its enzymatic functions and interactions with other proteins. Understanding the role of ADAM5P in biological systems can provide insights into its potential implications in disease mechanisms and may facilitate the development of novel therapeutic strategies. Overall, the study of ADAM5P as a recombinant protein represents a significant step towards unraveling the complexities of its functions and its contributions to health and disease.












