COL1A1 Protein (AA 1021-1109) (GST tag)
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- Target See all COL1A1 Proteins
- COL1A1 (Collagen, Type I, alpha 1 (COL1A1))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 1021-1109
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Origin
- Human
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This COL1A1 protein is labelled with GST tag.
- Sequence
- Glu 1021-Gly 1109
- Characteristics
- A DNA sequence encoding the Human COL1A1 protein (P02452) (Glu1021-Gly1109) was expressed with a N terminal GST tag.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Top Product
- Discover our top product COL1A1 Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Buffer
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Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization. - Storage
- 4 °C,-20 °C,-80 °C
- Storage Comment
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
- Expiry Date
- 12 months
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- Target
- COL1A1 (Collagen, Type I, alpha 1 (COL1A1))
- Alternative Name
- Collagen alpha-1 chain (COL1A1 Products)
- Background
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Abbreviation: Collagen alpha-1 chain,COL1A1
Target Synonym: Collagen alpha-1(I) chain,Alpha-1 type I collagen,COL1A1,COL1A1
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. This recombinant mini pro-alpha 1(I) collagen consists of a shortened alpha 1(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( alpha 1) and the C-terminal propeptide. This truncated pro-alpha 1(I) collagen is a substrate for procollagen N-proteinase and procollagen C-proteinase.
- Molecular Weight
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Calculated MW: 34.68 kDa
Observed MW: 35 kDa
- UniProt
- P02452
- Pathways
- Sensory Perception of Sound, Autophagy, Growth Factor Binding
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