HPAT3 Antibody
Description
Introduction to HPAT3 Antibody
HPAT3 antibody is a polyclonal antibody developed against the Hydroxyproline O-arabinosyltransferase 3 protein found in Arabidopsis thaliana (Mouse-ear cress). Commercially available preparations typically consist of rabbit-derived polyclonal antibodies that have undergone antigen-affinity purification to ensure high specificity and sensitivity. The antibody recognizes and binds to epitopes present on the HPAT3 protein, enabling its detection in various experimental settings. Currently, HPAT3 antibodies are manufactured by several biotechnology companies and serve as important reagents for researchers studying plant cellular biochemistry, particularly post-translational modifications of plant proteins .
HPAT3 Target Protein: Structure and Function
The target of HPAT3 antibody is Hydroxyproline O-arabinosyltransferase 3, a transmembrane protein localized in the Golgi apparatus that belongs to the glycosyltransferase GT8 family. This enzyme plays a fundamental role in plant biology by catalyzing the transfer of L-arabinose to the hydroxyl group of hydroxyproline residues in plant glycoproteins .
Biological Significance
HPAT3 belongs to a family of enzymes responsible for hydroxyproline O-arabinosylation, a prominent post-translational modification found in plant extracellular glycoproteins. This modification typically manifests as linear oligoarabinoside chains attached to hydroxyproline residues and significantly contributes to the conformational stability of these glycoproteins .
Research has demonstrated that HPAT enzymes, including HPAT3, are structurally similar to the glycosyltransferase GT8 family and are localized in the Golgi apparatus, where they participate in the secretory pathway for plant glycoproteins. The presence of these enzymes is crucial for proper extracellular matrix formation in plants .
HPAT3 Antibody Applications in Research
HPAT3 antibodies serve as valuable tools in multiple experimental applications focused on understanding the role of hydroxyproline O-arabinosylation in plant biology. The demonstrated applications include enzyme-linked immunosorbent assays (ELISA) and Western blot analyses, which enable researchers to detect and quantify HPAT3 protein in various plant tissue samples .
Western Blot Applications
Western blot analysis employing HPAT3 antibodies allows researchers to identify and semi-quantify HPAT3 protein expression in plant tissue extracts. This technique provides insights into protein expression levels across different developmental stages, tissue types, or experimental conditions .
ELISA Applications
Enzyme-linked immunosorbent assays utilizing HPAT3 antibodies enable the quantitative determination of HPAT3 protein concentrations in complex biological samples. This application is particularly valuable for high-throughput screening and precise quantification of expression levels .
Research Findings on HPAT3 Function
Studies employing loss-of-function mutations in HPAT-encoding genes, including HPAT3, have revealed the significant physiological importance of these enzymes in plant development and function. Research has demonstrated that disruption of HPAT function results in a range of phenotypic alterations in Arabidopsis thaliana.
Phenotypic Effects of HPAT Disruption
When HPAT function is compromised through genetic mutations, plants exhibit several distinctive phenotypic changes:
| Phenotypic Effect | Description |
|---|---|
| Enhanced hypocotyl elongation | Abnormal elongation of the embryonic stem |
| Cell wall thickening defects | Structural abnormalities in plant cell walls |
| Early flowering | Premature transition to reproductive growth phase |
| Early senescence | Accelerated aging and deterioration of plant tissues |
| Impaired pollen tube growth | Reproductive dysfunction due to abnormal pollen development |
These findings underscore the essential roles of hydroxyproline O-arabinosylation in both vegetative and reproductive growth processes in plants .
Molecular Mechanism
HPAT3 and related enzymes catalyze the transfer of L-arabinose to hydroxyproline residues in target proteins. This post-translational modification contributes significantly to the structural integrity and function of extracellular matrix proteins in plants. The arabinoside chains attached to hydroxyproline residues are believed to enhance the conformational stability of these proteins, which is critical for their proper functioning in the plant cell wall and extracellular matrix .
HPAT3 Protein Characterization
The HPAT3 protein has been characterized as a Golgi-localized transmembrane protein that shares structural similarities with members of the glycosyltransferase GT8 family. This localization is consistent with its role in the post-translational modification of secreted and cell wall proteins .
Research Significance and Future Directions
The development and application of HPAT3 antibodies have significantly contributed to our understanding of plant glycobiology, particularly the role of hydroxyproline O-arabinosylation in plant development and physiology. These antibodies serve as important tools for investigating the expression, localization, and function of HPAT3 in normal and experimental conditions.
Potential Research Applications
Future research employing HPAT3 antibodies may focus on several promising areas:
-
Comparative analysis of HPAT3 expression across different plant species
-
Investigation of HPAT3 regulation under various environmental stresses
-
Exploration of potential interacting partners of HPAT3 in the Golgi apparatus
-
Development of improved crop varieties through manipulation of HPAT3 function
-
Detailed structural analysis of HPAT3 to understand its catalytic mechanism
These research directions could potentially yield valuable insights into plant cell wall biology, stress responses, and crop improvement strategies.
Product Specs
Constituents: 50% Glycerol, 0.01M Phosphate-Buffered Saline (PBS), pH 7.4
Target Background
HPAT3 is a glycosyltransferase enzyme that participates in the O-arabinosylation of various proteins, including extensins and small signaling peptides. Its primary function is to catalyze the transfer of the initial L-arabinose residue to the hydroxyl group of hydroxyproline (Hyp) residues within these proteins. While functionally redundant with HPAT1 and HPAT2 in the arabinosylation of EXT3, HPAT3 is the primary contributor to the arabinosylation of CLE peptides.
