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

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CO1-M5243-100ug
$360.00
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CO1-M5243-1mg
$2,380.00
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CO1-M5243
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

COL1A1

Source

Mouse COL1A1 Protein, His Tag (CO1-M5243) is expressed from human 293 cells (HEK293). It contains AA Leu 1218 - Val 1453 (Accession # P11087).

Predicted N-terminus: His

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

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

The protein has a calculated MW of 28.8 kDa. The protein migrates as 33-37 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

The protein is designed as a trimer.

Endotoxin

Less than 0.01 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

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.

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.

Shipping and Storage

This product is shipped at ambient temperature.

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.
ACRO Quality Management System

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 .