Product Details

Full Product Name

Rabbit anti-Drosophila melanogaster (Fruit fly) drpr Polyclonal antibody

Uniprot No.

Q9W0A0

Target Names

drpr

Alternative Names

drpr antibody; Megf10 antibody; CG2086Protein draper antibody

Raised in

Rabbit

Species Reactivity

Drosophila melanogaster (Fruit fly)

Immunogen

Recombinant Drosophila melanogaster (Fruit fly) drpr protein

Immunogen Species

Drosophila melanogaster (Fruit fly)

Conjugate

Non-conjugated

Clonality

Polyclonal

Isotype

IgG

Purification Method

Antigen Affinity Purified

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4

Form

Liquid

Tested Applications

ELISA, WB (ensure identification of antigen)

Protocols

ELISA Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Value-added Deliverables

① 200ug * antigen (positive control);
② 1ml * Pre-immune serum (negative control);

Quality Guarantee

① Antibody purity can be guaranteed above 90% by SDS-PAGE detection;
② ELISA titer can be guaranteed 1: 64,000;
③ WB validation with antigen can be guaranteed positive;

Lead Time

Made-to-order (14-16 weeks)

Target Background

Function

Receptor which is involved in the phagocytosis of a variety of cells including apoptotic cells, severed and pruned axons, degenerating dendrites, salivary gland cells, germline cells and bacteria. Binds to the ligand prtp which relocates from the endoplasmic reticulum to the cell surface during apoptosis. Ligand-binding may promote tyrosine phosphorylation mediated by Src42a, interaction with shark and subsequent activation of phagocytosis. Also binds to the membrane phospholipid phosphatidylserine which is exposed on the surface of apoptotic cells. Required for the phagocytosis of apoptotic cells by macrophages. Also required for the phagocytosis of apoptotic neurons by glial cells in the embryonic nervous system. Acts downstream of NimC4/simu in the glial phagocytosis of apoptotic neurons. Plays a role in the glial engulfment of larval axons as part of programmed axon pruning during metamorphosis. Also mediates glial cell clearance of severed axons following axonal injury. Required for the engulfment of degenerating dendrites by epidermal cells. Required in the ovary for the engulfment and subsequent processing of dying germline cells by follicular epithelial cells through activation of the JNK/bsk pathway. Plays a role in neuromuscular junction development by mediating the clearance of presynaptic debris and immature boutons which are shed by growing synapses. Required for larval salivary gland cell death which occurs following a rise in steroid levels after puparium formation. Also involved in bacterial phagocytosis. Required for hemocyte phagocytosis of the Gram-positive bacterium S.aureus. Lipoteichoic acid, synthesized by the S.aureus lipoteichoic acid synthase ltaS, acts as a ligand for drpr in this process. Together with Src42a and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects production of hydrogen peroxide at wound sites which triggers phosphorylation of drpr and subsequent recruitment and activation of shark. Also required for macrophage priming which occurs following phagocytosis of apoptotic cells and ensures that macrophages develop a form of molecular memory that allows them to later mount an inflammatory response to tissue damage and bacterial infection. Is also an essential factor in the regulation of muscle development and myogenesis, and as a consequence is required for normal locomotion. Likely to control the balance between skeletal muscle satellite cells proliferation and differentiation through regulation of the notch signaling pathway.; Promotes engulfment of axonal debris by glial cells following axonal injury.; Potently inhibits glial cell engulfment of axonal debris produced following axonal injury.

Gene References into Functions

During metamorphosis, Draper plays a critical role in apoptotic cell clearance by glia, whereas SIMU, which is mostly expressed in pupal macrophages outside the brain, is not involved in glial phagocytosis: Draper activates Drosophila c-Jun N-terminal kinase (dJNK) signaling predominantly in the ensheathing glia and astrocytes, where it is required for efficient removal of apoptotic neurons. PMID: 29520845
Glial clearance of damaged axons is significantly delayed in aged animals due to an age-dependent decline in translation of the critical glial recognition engulfment receptor Draper, which results from reduced phosphoinositide-3-kinase signalling. PMID: 27647497
The glial engulfment receptor Draper is protective in a Drosophila model of Alzheimer's Disease. PMID: 29109235
INR signaling promotes glial phagocytic clearance of degenerating axons through regulation of Draper. PMID: 27498858
Src42A-Draper-Shark-mediated signaling axis is homologous to the well-established SFK-ITAM-Syk-signaling pathway used in vertebrate adaptive immune responses PMID: 26028435
plays role in innate immune responses against viral infection PMID: 26546607
Our analysis of drpr mutant flies revealed muscle degeneration with fiber size variability and vacuolization, as well as reduced motor performance, features that have been observed in human MEGF10 myopathy. PMID: 25111228
Glia regulate steady-state numbers of Htt aggregates expressed in neurons through a clearance mechanism that requires the glial scavenger receptor Draper and downstream phagocytic machinery. PMID: 25866135
signaling through the injury-responsive Draper receptor leads to Stat92E-dependent, transcriptional activation of the draper gene PMID: 25369313
axonal injury in the Drosophila brain activates a glial signaling pathway composed of Slipper and Tak, MKK4, dJNK and the dAP-1 complex, which ultimately leads to increased levels of Draper in glia and activation of phagocytic function. PMID: 23618811
The results indicated that phosphatidylserine serves as an eat-me signal in the phagocytic removal of apoptotic cells in Drosophila and that Draper is a phosphatidylserine-binding receptor for phagocytosis. PMID: 23420848
Draper binds to its ligand Pretaporter using EGF-like sequences, and that the NPxY motif in the intracellular region of Draper plays an essential role in its actions as an engulfment receptor. PMID: 23337816
Draper is also required in engulfing follicle cells, and activates the JNK pathway PMID: 22992958
Draper (Drpr), the Drosophila homolog of C. elegans engulfment receptor CED-1, is required for autophagy induction. PMID: 20864812
Draper (Drpr), the Drosophila melanogaster orthologue of the Caenorhabditis elegans engulfment receptor CED-1, is required for autophagy during cell death PMID: 20577216
Results indicate that Drosophila hemocytes/macrophages execute Draper-mediated phagocytosis to eliminate apoptotic cells. PMID: 15342648
Draper is essential in the glial engulfment of larval axons during Drosophila metamorphosis. PMID: 16772168
Draper appears to act as a glial receptor for severed axon-derived molecular cues that drive recruitment of glial processes to injured axons for engulfment. PMID: 16772169
Phenotypic analysis reveals that simu acts upstream of drpr in the same pathway and affects the recognition and engulfment of apoptotic cells, while drpr affects their subsequent degradation. PMID: 18455990
Undertaker (UTA), a Drosophila Junctophilin protein, is required for Draper (CED-1 homolog)-mediated phagocytosis. PMID: 18984163
lipoteichoic acid serves as a ligand for Draper in the phagocytosis of S. aureus by Drosophila hemocytes PMID: 19890048

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Subcellular Location

Cell membrane; Single-pass type I membrane protein. Cell projection, axon. Cytoplasm. Cell junction, synapse, postsynaptic cell membrane. Cytoplasm, cell cortex. Cell projection, phagocytic cup. Cytoplasmic vesicle, phagosome.

Tissue Specificity

Expressed in adult head (at protein level). Expressed in glia, macrophages and ectoderm (at protein level). Detected in glia around the mushroom body dorsal lobe and in glial processes infiltrating the medial lobe (at protein level). Expressed in adult br

Database Links

KEGG: dme:Dmel_CG2086

UniGene: Dm.3167

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drpr Antibody

Product Details

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Target Background