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Mouse WARP Antibody

R&D Systems, part of Bio-Techne | Catalog # AF4927

R&D Systems, part of Bio-Techne
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AF4927
AF4927-SP

Key Product Details

Species Reactivity

Validated:

Mouse

Cited:

Mouse

Applications

Validated:

Western Blot

Cited:

Immunohistochemistry, Western Blot

Label

Unconjugated

Antibody Source

Polyclonal Goat IgG

Product Specifications

Immunogen

Mouse myeloma cell line NS0-derived recombinant mouse WARP isoform 1
Arg19-Pro415
Accession # Q8R2Z5

Specificity

Detects mouse WARP in direct ELISAs and Western blots. In direct ELISAs, approximately 20% cross‑reactivity with recombinant human WARP is observed.

Clonality

Polyclonal

Host

Goat

Isotype

IgG

Scientific Data Images for Mouse WARP Antibody

Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

WARP expression pattern in the heart.(a) WARP mRNA levels were induced 3 and 7 days after MI. WARP mRNA levels peaked at 7 days after MI and then decreased again at 14 days. (b) Western blot analysis and (c) immunohistochemistry also showed an induction of WARP protein levels in the infarcted LV at 3, 7, and 14 days after MI. Because of different sample-loading, the blots of the 14 days MI were cut and pasted in the same order as the blots of the 3 and 7 days MI. Images of the original unadjusted blots are provided in S1 Fig (d and e) Confocal microscopy confirmed the co-localization of WARP with perlecan in the uninfarcted heart, showing a network of WARP and perlecan as a honeycomb-structure surrounding the cardiomyocytes. In the infarcted LV zones, the WARP-perlecan honeycomb-structure is reduced at 3 days after MI and completely absent at 7 and 14 days after MI and the interaction between WARP and perlecan is disrupted. (e) WARP did not localize on CD45 positive leukocytes or in alpha smooth muscle cells lining the vessels in the remote, border and infarcted zone of the heart 14 days after MI. n≥3; *p≤0.05; **p≤0.005; ***p≤0.001 versus sham, ##p≤0.005; ###p≤0.001 versus remote, bars 1000 μm for (c) and 100 μm for (d) and (e). Image collected and cropped by CiteAb from the following publication (https://dx.plos.org/10.1371/journal.pone.0139199), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

WARP expression pattern in the heart.(a) WARP mRNA levels were induced 3 and 7 days after MI. WARP mRNA levels peaked at 7 days after MI and then decreased again at 14 days. (b) Western blot analysis and (c) immunohistochemistry also showed an induction of WARP protein levels in the infarcted LV at 3, 7, and 14 days after MI. Because of different sample-loading, the blots of the 14 days MI were cut and pasted in the same order as the blots of the 3 and 7 days MI. Images of the original unadjusted blots are provided in S1 Fig (d and e) Confocal microscopy confirmed the co-localization of WARP with perlecan in the uninfarcted heart, showing a network of WARP and perlecan as a honeycomb-structure surrounding the cardiomyocytes. In the infarcted LV zones, the WARP-perlecan honeycomb-structure is reduced at 3 days after MI and completely absent at 7 and 14 days after MI and the interaction between WARP and perlecan is disrupted. (e) WARP did not localize on CD45 positive leukocytes or in alpha smooth muscle cells lining the vessels in the remote, border and infarcted zone of the heart 14 days after MI. n≥3; *p≤0.05; **p≤0.005; ***p≤0.001 versus sham, ##p≤0.005; ###p≤0.001 versus remote, bars 1000 μm for (c) and 100 μm for (d) and (e). Image collected and cropped by CiteAb from the following publication (https://dx.plos.org/10.1371/journal.pone.0139199), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

Detection of Mouse WARP/VWA1 by Immunocytochemistry/Immunofluorescence

WARP expression pattern in the heart.(a) WARP mRNA levels were induced 3 and 7 days after MI. WARP mRNA levels peaked at 7 days after MI and then decreased again at 14 days. (b) Western blot analysis and (c) immunohistochemistry also showed an induction of WARP protein levels in the infarcted LV at 3, 7, and 14 days after MI. Because of different sample-loading, the blots of the 14 days MI were cut and pasted in the same order as the blots of the 3 and 7 days MI. Images of the original unadjusted blots are provided in S1 Fig (d and e) Confocal microscopy confirmed the co-localization of WARP with perlecan in the uninfarcted heart, showing a network of WARP and perlecan as a honeycomb-structure surrounding the cardiomyocytes. In the infarcted LV zones, the WARP-perlecan honeycomb-structure is reduced at 3 days after MI and completely absent at 7 and 14 days after MI and the interaction between WARP and perlecan is disrupted. (e) WARP did not localize on CD45 positive leukocytes or in alpha smooth muscle cells lining the vessels in the remote, border and infarcted zone of the heart 14 days after MI. n≥3; *p≤0.05; **p≤0.005; ***p≤0.001 versus sham, ##p≤0.005; ###p≤0.001 versus remote, bars 1000 μm for (c) and 100 μm for (d) and (e). Image collected and cropped by CiteAb from the following publication (https://dx.plos.org/10.1371/journal.pone.0139199), licensed under a CC-BY license. Not internally tested by R&D Systems.

Applications for Mouse WARP Antibody

Application
Recommended Usage

Western Blot

0.1 µg/mL
Sample: Recombinant Mouse WARP

Formulation, Preparation, and Storage

Purification

Antigen Affinity-purified

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Reconstitution Buffer Available:
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Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: WARP

WARP (von Willebrand factor A [vWFA] domain-related protein) is a 50 kDa glycoprotein member of the vWFA domain superfamily of extracellular matrix proteins. It is expressed in embryonic articular cartilage, skeletal muscle and basement membranes in the PNS. WARP forms disulfide-linked homodimers and multimers, and complexes with perlecan. Secreted mouse WARP is 397 amino acids (aa) in length. It contains a vWFA domain (aa 34‑209), and two fibronectin type III domains (aa 211‑394) that likely bind to the GAG modification of perlecan. Cys369 and Cys393 contribute to intermolecular bond formation. There is one alternate start site at Met213. Mature mouse WARP (aa 19‑415) is 93% and 78% aa identical to rat and human WARP, respectively.

Long Name

von Willebrand factor A Domain-related Protein

Alternate Names

VWA1

Entrez Gene IDs

64856 (Human); 246228 (Mouse); 298683 (Rat)

Gene Symbol

VWA1

UniProt

Additional WARP Products

Product Documents for Mouse WARP Antibody

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Mouse WARP Antibody

For research use only

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