Recombinant Human Pro-Collagen I alpha 1/COL1A1 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 6220-CL

R&D Systems, part of Bio-Techne
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6220-CL-020
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Key Product Details

Source

CHO

Accession #

P02452

Conjugate

Unconjugated

Applications

Enzyme Activity

View all Collagen I alpha 1 Proteins and Enzymes »

Product Specifications

Source

Chinese Hamster Ovary cell line, CHO-derived human Collagen I alpha 1 protein
Gln23-Lys277 + Gly1094-Leu1464, with an N-terminal 6-His tag.

Purity

>80%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

His & Asp1219

Predicted Molecular Mass

65 kDa (full-length), 40 kDa, 28 kDa

SDS-PAGE

79-83 kDa, 54-56 kDa, 35-36 kDa, reducing conditions

Activity

Measured by the cleavage of its C-terminal propeptide by Recombinant Human BMP-1/PCP (Catalog # 1927-ZN).
>50% of full-length Pro-Collagen I alpha1 is cleaved by Recombinant Human BMP‑1/PCP (Catalog # 1927-ZN) , as measured under the described conditions.

Formulation, Preparation and Storage

6220-CL
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: Collagen I alpha 1

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 (1). 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 (1). Type I collagen is a heterotrimer that consists of two alpha1(I) chains and one alpha2(I) chain, although homotrimers consisting of three identical alpha1(I) chains have also been described (2). This recombinant mini pro-alpha 1(I) collagen consists of a shortened alpha1(I) chain with following domain structure from N- to C-terminus: N-propeptide, N‑telopeptide, the 33 most N-terminal Gly-Xaa-Yaa repeats, the 33 most C-terminal Gly-Xaa-Yaa repeats, C-telopeptide and C-propeptide. The preparation contains a mixture of the full-length molecule, pN collagen I( alpha1) and the C-terminal propeptide. This truncated pro-alpha 1(I) collagen is a substrate for procollagen N-proteinase and procollagen C-proteinase.

References

  1. Canty, E.G. et al. (2005) J. Cell Sci. 118:1341.
  2. Han, S. et al. (2008) J. Mol. Biol. 383:122.

Alternate Names

COL1A1, OI4

Entrez Gene IDs

1277 (Human)

Gene Symbol

COL1A1

UniProt

P02452

Additional Collagen I alpha 1 Products

Product Documents for Recombinant Human Pro-Collagen I alpha 1/COL1A1 Protein, CF

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Product Specific Notices for Recombinant Human Pro-Collagen I alpha 1/COL1A1 Protein, CF

For research use only

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