Analytical Data
-
基因名
COLM
- Application
-
别名
GLDN; COLM; UNQ9339/PRO34011Gliomedin
-
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
Q6ZMI3
-
表达区间
1-551aa
-
氨基酸序列
MARGAEGGRGDAGWGLRGALAAVALLSALNAAGTVFALCQWRGLSSALRALEAQRGREQREDSALRSFLAELSRAPRGASAPPQDPASSARNKRSHSGEPAPHIRAESHDMLMMMTYSMVPIRVMVDLCNSTKGICLTGPSGPPGPPGAGGLPGHNGLDGQPGPQGPKGEKGANGKRGKMGIPGAAGNPGERGEKGDHGELGLQGNEGPPGQKGEKGDKGDVSNDVLLAGAKGDQGPPGPPGPPGPPGPPGPPGSRRAKGPRQPSMFNGQCPGETCAIPNDDTLVGKADEKASEHHSPQAESMITSIGNPVQVLKVTETFGTWIRESANKSDDRIWVTEHFSGIMVKEFKDQPSLLNGSYTFIHLPYYFHGCGHVVYNNSLYYHKGGSNTLVRFEFGQETSQTLKLENALYFDRKYLFANSKTYFNLAVDEKGLWIIYASSVDGSSILVAQLDERTFSVVQHVNTTYPKSKAGNAFIARGILYVTDTKDMRVTFAFDLLGGKQINANFDLRTSQSVLAMLAYNMRDQHLYSWEDGHLMLYPVQFLSTTLNQ
-
分子量
58.9 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
COLM, short for collagen-like molecule, has garnered increasing attention in the realm of biomaterials and tissue engineering due to its unique structural and biochemical properties. Collagen, being the most abundant protein in mammals, plays a crucial role in maintaining the structural integrity of tissues. COLM, as a recombinant protein, is engineered to mimic the triple-helix structure of natural collagen, providing versatility in various applications such as wound healing, drug delivery, and scaffolding for tissue regeneration. The ability to produce COLM in controlled environments allows for the customization of molecular properties, enhancing its biocompatibility and functionality. Additionally, studies have shown that COLM promotes cell adhesion and proliferation, making it a promising candidate for regenerative medicine. This synthetic approach not only addresses the limitations of sourcing and purifying collagen from animal tissues but also offers a sustainable alternative for developing advanced biomaterials. Ongoing research aims to optimize COLM's mechanical properties and explore its potential in delivering therapeutic agents, with the ultimate goal of improving patient outcomes in clinical settings.
