Anti-Collagen Alpha-1(III) Carboxy-Propeptide [LF-69] Antibody
![Anti-Collagen Alpha-1(III) Carboxy-Propeptide [LF-69] Antibody](https://www.kerafast.com/MediaStorage/Product/Images/Large/1526_2001202001265115250.jpg "Anti-Collagen Alpha-1(III) Carboxy-Propeptide [LF-69] Antibody")
This rabbit IgG polyclonal antibody was generated against peptide and recognizes human and birds type I collagen alpha-1 amino-propeptide.
Highlights:
- Recognizes human and birds type I collagen alpha-1 amino-propeptide - Epitope DIGGPDQEFGVDVGPVCFL
- 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 this gene are associated with type II Stickler syndrome and with Marshall syndrome.
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.
This rabbit IgG polyclonal antibody was generated against peptide and recognizes human and birds type I collagen alpha-1 amino-propeptide.
Highlights:
- Recognizes human and birds type I collagen alpha-1 amino-propeptide - Epitope DIGGPDQEFGVDVGPVCFL
- 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 this gene are associated with type II Stickler syndrome and with Marshall syndrome.
From the laboratory of Larry W. Fisher, PhD, National Institute of Dental and Craniofacial Research/NIH.
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| Product Type: | Antibody |
| Antigen: | Type I collagen alpha,1 amino-propeptide, human |
| Accession ID: | P02461 |
| Molecular Weight: | 138555 Da |
| Clonality: | Polyclonal |
| Clone Name: | LF-69 |
| Reactivity: | Human tested but peptide conserved in mammals, birds |
| Immunogen: | Peptide |
| Species Immunized: | Rabbit |
| Epitope: | DIGGPDQEFGVDVGPVCFL |
| Buffer: | Whole serum |
| Tested Applications: | WB 1:2000, IHC 1:400 |
| Storage: | -80C |
| Shipped: | Cold Packs (Domestic, Overnight); Dry Ice (International) |
- Fisher LW et al. Antisera and cDNA probes to human and certain animal model bone matrix noncollagenous proteins. Acta Orthop Scand Suppl. 1995 Oct;266:61-5
- Bernstein EF, Chen YQ, Kopp JB, Fisher L, Brown DB, Hahn PJ, Robey FA, Lakkakorpi J, Uitto J. Long-term sun exposure alters the collagen of the papillary dermis. Comparison of sun-protected and photoaged skin by northern analysis, immunohistochemical staining, and confocal laser scanning microscopy. J Am Acad Dermatol. 1996 Feb;34(2 Pt 1):209-18.
- Wang WM, Lee S, Steiglitz BM, Scott IC, Lebares CC, Allen ML, Brenner MC, Takahara K, Greenspan DS. Transforming growth factor-beta induces secretion of activated ADAMTS-2. A procollagen III N-proteinase. J Biol Chem. 2003 May 23;278(21):19549-57
- Bekhouche M, Leduc C, Dupont L, Janssen L, Delolme F, Vadon-Le Goff S, Smargiasso N, Baiwir D, Mazzucchelli G, Zanella-Cleon I, Dubail J, De Pauw E, Nusgens B, Hulmes DJ, Moali C, Colige A. Determination of the substrate repertoire of ADAMTS2, 3, and 14 significantly broadens their functions and identifies extracellular matrix organization and TGF-? signaling as primary targets. FASEB J. 2016 May;30(5):1741-56.
- Muir AM, Massoudi D, Nguyen N, Keene DR, Lee SJ, Birk DE, Davidson JM, Marinkovich MP, Greenspan DS. BMP1-like proteinases are essential to the structure and wound healing of skin. Matrix Biol. 2016 Dec;56:114-131.
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