Mouse Pro-COL1A1 Protein, His Tag, low endotoxin (MALS verified)

分子別名（Synonym）

Pro-COL1A1

表達(dá)區(qū)間及表達(dá)系統(tǒng)（Source）

Mouse Pro-COL1A1 Protein, His Tag (PC1-M5243) is expressed from human 293 cells (HEK293). It contains AA Gln 23 - Ser 151 (Accession # P11087).

蛋白結(jié)構(gòu)（Molecular Characterization）

This protein carries a polyhistidine tag at the N-terminus.

The protein has a calculated MW of 15.9 kDa. The protein migrates as 25-27 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

內(nèi)毒素（Endotoxin）

Less than 0.01 EU per μg by the LAL method.

純度（Purity）

>90% as determined by SDS-PAGE.

制劑（Formulation）

Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 150 mM NaCl, pH7.5 with trehalose as protectant.

Contact us for customized product form or formulation.

重構(gòu)方法（Reconstitution）

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存儲(chǔ)（Storage）

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

-20°C to -70°C for 12 months in lyophilized state;

-70°C for 3 months under sterile conditions after reconstitution.

背景（Background）

Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a procollagen molecule which is characterized by a 300 nm triple helical domain flanked by globular N- and C-terminal propeptides. The triple helical domain contains Gly-Xaa-Yaa triplets where Xaa and Yaa are frequently proline and hydroxyproline, respectively. The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues. Type I collagen is a heterotrimer that consists of two alpha 1(I) chains and one alpha 2(I) chain, although homotrimers consisting of three identical alpha 1(I) chains have also been described .