Abcam, ab244326, Anti-LEPRE1/P3H1 antibody

Size: 100µL
Rabbit Polyclonal LEPRE1/P3H1 antibody. Suitable for IHC-P, WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Recombinant Fragment Protein within Human P3H1 aa 300-450.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human P3H1 aa 300-450. The exact immunogen used to generate this antibody is proprietary information.Q32P28

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Storage buffer-pH: 7.2Preservative: 0.02% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
LEPRE1 also known as P3H1 or prolyl 3-hydroxylase 1 is an enzyme involved in collagen synthesis with a molecular mass of approximately 71 kDa. It is a member of the prolyl hydroxylase family and carries out 3-hydroxylation of proline residues in collagen. The enzyme localizes largely to the endoplasmic reticulum where it contributes to the post-translational modification of collagen. LEPRE1 is ubiquitously expressed with higher concentrations observed in tissues rich in collagen such as skin bone and cartilage.
Biological function summary
LEPRE1 plays a fundamental role in the maturation of collagen which is an important structural protein in connective tissues. This enzyme functions as a part of the collagen prolyl 3-hydroxylation complex which includes cartilage-associated protein (CRTAP) and cyclophilin B (PPIB). The complex is responsible for the correct folding and stability of collagen molecules ensuring the proper formation of the extracellular matrix. This structural role is essential for maintaining tissue integrity and function.
Pathways
LEPRE1 is important in the collagen biosynthesis and modifying pathways. It interacts with other biosynthesis enzymes like lysyl oxidase and procollagen-proline dioxygenase. These proteins coordinate to execute post-translational modifications which stabilize the collagen triple helix structure. Pirh2 and Hsp47 act along with LEPRE1 in similar pathways helping in folding and secretion of collagen.
LEPRE1 mutations have been linked to connective tissue disorders most notably osteogenesis imperfecta a genetic disorder causing brittle bones. Such mutations impair collagen modification leading to defective collagen formation and bone fragility. Additionally dysregulation of LEPRE1 activity appears connected to disorder Ehlers-Danlos syndrome noted for joint hypermobility and skin elasticity issues. COL1A1 and COL1A2 two primary components of type I collagen often associate with LEPRE1 in disease contexts as mutations in these collagens lead to similar clinical manifestations.