• Species Reactivity

  Human

• Specificity

  Detects human Collagen I alpha 1 in direct ELISAs.    
   

• Source

  Monoclonal Mouse IgG    _2B Clone # 816161

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Chinese hamster ovary cell line CHO-derived recombinant human Collagen I alpha 1    
  Gln23-Lys277, Gly1094-Leu1464    
  Accession # P02452

• Formulation

  Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Immunocytochemistry

  8-25 µg/mL

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Reconstitution

  Reconstitute at 0.5 mg/mL in sterile PBS.

• Shipping

  The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & Storage

  Use a manual defrost freezer and avoid repeated freeze-thaw cycles.    

• 12 months from date of receipt, -20 to -70 °C as supplied.

• 1 month, 2 to 8 °C under sterile conditions after reconstitution.

• 6 months, -20 to -70 °C under sterile conditions after reconstitution.

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 alpha 1(I) chains and one alpha 2(I) chain, although homotrimers consisting of three identical alpha 1(I) chains have also been described (2). 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.

• References:

1. Canty, E.G. et al. (2005) J. Cell Sci. 118:1341.

2. Han, S. et al. (2008) J. Mol. Biol. 383:122.

• Entrez Gene IDs:

  1277 (Human)

• Alternate Names:

  Alpha-1 type I collagen; COL1A1; Collagen 1 alpha 1; Collagen 1; collagen alpha 1 chain type I; collagen alpha-1(I) chain; Collagen I alpha 1; collagen of skin, tendon and bone, alpha-1 chain; collagen, type I, alpha 1; Collagen1; Collagen-1; OI4; pro-alpha-1 collagen type 1