Anti-Collagen Alpha-1(I) Chain Carboxy-Propeptide [LF-42] Antibody

This rabbit IgG polyclonal antibody was raised against peptide and recognizes human and other species type 1 collagen alpha-1 carboxy propeptide.

Highlights:

  • Recognizes human and other species type 1 collagen alpha-1 carboxy propetide - Epitope - amino acid sequence PLDVGAPDQEFGFDVGPVCFL
  • Suitable for Immunohistochemistry and Western Blot applications

Collagen is a protein that supports many tissues in the body, including cartilage, bone, tendon, skin and the white part of the eye (sclera). Specifically collagen type 1 alpha 1 encodes the major component of type I collagen, the fibrillar collagen found in most connective tissues, including cartilage. Mutations in the gene can cause ostegensis imperfecta and ehlers-danlos syndrome.

From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.

Catalog Number Product DataSheet Size AVAILABILITY Price Qty
ENH017-FP
Anti-Collagen Alpha-1(I) Chain Carboxy-Propeptide [LF-42] Antibody
100uL In stock
Regular Price:$355.00
On Sale:

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Specifications

Product Type: Antibody
Antigen: Type I collagen alpha-1 carboxy-propeptide
Accession ID: P02452
Molecular Weight: 136514 Da
Isotype: IgG
Clonality: Polyclonal
Clone Name: LF-42
Reactivity: Human and most other species
Immunogen: Peptide
Species Immunized: Rabbit
Epitope: PLDVGAPDQEFGFDVGPVCFL
Buffer: Whole serum
Tested Applications: WB (1:2000), IHC (1:400)
Storage: -80C
Shipped: Cold Packs (Domestic, Overnight); Dry Ice (International)

Provider
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.
References
  1. Fisher LW, Stubbs JT 3rd, Young MF. Antisera and cDNA probes to human and certain animal model bone matrix noncollagenous proteins. Acta Orthop Scand Suppl. 1995 Oct;266:61-5.
  2. Bonfanti L, Mironov AA Jr, Martínez-Menárguez JA, Martella O, Fusella A, Baldassarre M, Buccione R, Geuze HJ, Mironov AA, Luini A. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: evidence for cisternal maturation. Cell. 1998 Dec 23;95(7):993-1003.
  3. Martínez-Glez V, Valencia M, Caparrós-Martín JA, Aglan M, Temtamy S, Tenorio J, Pulido V, Lindert U, Rohrbach M, Eyre D, Giunta C, Lapunzina P, Ruiz-Perez VL. Identification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta. Hum Mutat. 2012 Feb;33(2):343-50. doi: 10.1002/humu.21647.
  4. Tian C, Huang Y, Clauser KR, Rickelt S, Lau AN, Carr SA, Vander Heiden MG, Hynes RO. Suppression of pancreatic ductal adenocarcinoma growth and metastasis by fibrillar collagens produced selectively by tumor cells. Nat Commun. 2021 Apr 20;12(1):2328. View article 

If you publish research with this product, please let us know so we can cite your paper.

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