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anti rabbit timp4 (Novus Biologicals)

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Novus Biologicals anti rabbit timp4
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Anti Rabbit Timp4, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+rabbit+timp4/Human%2FMouse+TIMP-4+Antibody/pmc08276117-4-0-3
Average 90 stars, based on 3 article reviews

anti rabbit timp4 - by Bioz Stars, 2026-09

90/100 stars

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1) Product Images from "Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis"

Article Title: Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis

Journal: Cell reports

doi: 10.1016/j.celrep.2019.07.045

Figure Legend Snippet: KEY RESOURCES TABLE

Techniques Used: FLAG-tag, Recombinant, Bradford Assay, cDNA Synthesis, SYBR Green Assay, Enzyme-linked Immunosorbent Assay, Sandwich ELISA, LDH Cytotoxicity Assay, Software

FLAG-tag:

Article Title: Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis
Article Snippet: Anti-rabbit TIMP4 , NOVUS Biologicals , Cat# AF974; RRID: AB_2205240.

Recombinant:

Bradford Assay:

cDNA Synthesis:

SYBR Green Assay:

Enzyme-linked Immunosorbent Assay:

Sandwich ELISA:

LDH Cytotoxicity Assay:

Software:

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Journal: Cell reports

Article Title: Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis

doi: 10.1016/j.celrep.2019.07.045

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Anti-rabbit TIMP4 , NOVUS Biologicals , Cat# AF974; RRID: AB_2205240.

Techniques: FLAG-tag, Recombinant, Bradford Assay, cDNA Synthesis, SYBR Green Assay, Enzyme-linked Immunosorbent Assay, Sandwich ELISA, LDH Cytotoxicity Assay, Software

Sequences and predicted structures of zebrafish metalloproteinase 11 (Mmp11) and tissue inhibitors of metalloproteinase-4 (Timp4) paralogues exhibit both conserved and divergent features. ( A ) Inferred amino acid sequences of zebrafish Mmp11a and Mmp11b paralogues aligned with human MMP11 for reference. Secretory signals are boxed in light blue, propeptide in purple (with cysteine switch motif highlighted in bold and furin recognition sequence underlined), catalytic domain in red (with S-loop in orange, zinc binding motif in bold italic, and specificity loop in light blue), and the carboxyl hemopexin domain is boxed in green. ( B ) Structural homology models of zebrafish Mmp11a and Mmp11b rendered as ribbon diagrams and colored as in the sequence alignment. ( C ) Inferred amino acid sequences of zebrafish Timp4a and Timp4b paralogues aligned with human TIMP4 for reference. Secretory signals are boxed in light blue, the N-terminal domain in blue (with the seven-residue charged insertion of Timp4a highlighted in orange), and the C-terminal domain in red. ( D ) Structural homology models of zebrafish Timp4a and Timp4b rendered as ribbon diagrams and colored as in the sequence alignment.

Journal: Journal of Developmental Biology

Article Title: Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo

doi: 10.3390/jdb7040022

Figure Lengend Snippet: Sequences and predicted structures of zebrafish metalloproteinase 11 (Mmp11) and tissue inhibitors of metalloproteinase-4 (Timp4) paralogues exhibit both conserved and divergent features. ( A ) Inferred amino acid sequences of zebrafish Mmp11a and Mmp11b paralogues aligned with human MMP11 for reference. Secretory signals are boxed in light blue, propeptide in purple (with cysteine switch motif highlighted in bold and furin recognition sequence underlined), catalytic domain in red (with S-loop in orange, zinc binding motif in bold italic, and specificity loop in light blue), and the carboxyl hemopexin domain is boxed in green. ( B ) Structural homology models of zebrafish Mmp11a and Mmp11b rendered as ribbon diagrams and colored as in the sequence alignment. ( C ) Inferred amino acid sequences of zebrafish Timp4a and Timp4b paralogues aligned with human TIMP4 for reference. Secretory signals are boxed in light blue, the N-terminal domain in blue (with the seven-residue charged insertion of Timp4a highlighted in orange), and the C-terminal domain in red. ( D ) Structural homology models of zebrafish Timp4a and Timp4b rendered as ribbon diagrams and colored as in the sequence alignment.

Article Snippet: Embryos were incubated in primary antibodies (mouse anti-α-actinin (catalogue #A7811; Sigma, Oakville, ON Canada), rabbit anti-laminin (catalogue #PA1-16730; ThemoFisher Scientific, Waltham, Massachusetts, USA) mouse anti-GFP (catalogue #11814460001, Roche, Basel, Switzerland), rat anti-HA (Roche catalogue #1186742300), rabbit anti-zebrafish-Mmp11a (catalogue #55688; AnaSpec, Freemont, CA, USA), rabbit anti-zebrafish-Mmp11b (AnaSpec catalogue #55690), and rabbit anti-Zebrafish-Timp4 (AnaSpec catalogue #55501)) diluted 1:1000 in blocking buffer overnight.

Techniques: Sequencing, Binding Assay

Timp4 and Mmp11 paralogues accumulate dynamically during development and co-localize at the myotendinous junctions (MTJs). Composite confocal projections of 24, 36, 48, 72 and 96 hpf embryos labeled with antibodies against Timp4, Mmp11a, or Mmp11b. ( A – E ) Timp4 immunoreactivity is abundant at the MTJ at all stages examined (arrowhead), and accumulates dynamically in ectodermal epithelia of the head, fin folds, otic vesicle, the posterior notochord and muscle attachments in the jaws and pectoral fins in later stages. ( F – J ) Mmp11a is present at the MTJs in 24 hpf embryos ( F ) (arrowhead) but becomes localized within muscle cells in later stages ( G , H ). ( K – O ) Mmp11b becomes concentrated in MTJs at later stages ( L – O ) (arrowhead). Insets show higher magnification views of MTJs dorsal to the yolk extension in 24 and 96 hpf embryos for comparison. Scale bar = 500 µm.

Journal: Journal of Developmental Biology

Article Title: Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo

doi: 10.3390/jdb7040022

Figure Lengend Snippet: Timp4 and Mmp11 paralogues accumulate dynamically during development and co-localize at the myotendinous junctions (MTJs). Composite confocal projections of 24, 36, 48, 72 and 96 hpf embryos labeled with antibodies against Timp4, Mmp11a, or Mmp11b. ( A – E ) Timp4 immunoreactivity is abundant at the MTJ at all stages examined (arrowhead), and accumulates dynamically in ectodermal epithelia of the head, fin folds, otic vesicle, the posterior notochord and muscle attachments in the jaws and pectoral fins in later stages. ( F – J ) Mmp11a is present at the MTJs in 24 hpf embryos ( F ) (arrowhead) but becomes localized within muscle cells in later stages ( G , H ). ( K – O ) Mmp11b becomes concentrated in MTJs at later stages ( L – O ) (arrowhead). Insets show higher magnification views of MTJs dorsal to the yolk extension in 24 and 96 hpf embryos for comparison. Scale bar = 500 µm.

Techniques: Labeling

Timp4 and both Mmp11 paralogues are present in the MTJ at 28 hpf. High-resolution confocal micrographs of MTJs in the trunk skeletal musculature dorsal to the yolk extension of 28 hpf embryos stained with antibodies against ( A ) Mmp11a, ( B ) Mmp11b, ( C ) Timp4, and ( D ) Laminin (green) as well as anti-α-actinin (red) reveal that both Mmp11 paralogues are detectable in MTJs at this stage, and that they accumulate in the periphery of the MTJ (arrowheads), whereas Timp4 accumulates in the core of the MTJ. Scale bars are 10 µm. Anterior to the left in all images.

Journal: Journal of Developmental Biology

Article Title: Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo

doi: 10.3390/jdb7040022

Figure Lengend Snippet: Timp4 and both Mmp11 paralogues are present in the MTJ at 28 hpf. High-resolution confocal micrographs of MTJs in the trunk skeletal musculature dorsal to the yolk extension of 28 hpf embryos stained with antibodies against ( A ) Mmp11a, ( B ) Mmp11b, ( C ) Timp4, and ( D ) Laminin (green) as well as anti-α-actinin (red) reveal that both Mmp11 paralogues are detectable in MTJs at this stage, and that they accumulate in the periphery of the MTJ (arrowheads), whereas Timp4 accumulates in the core of the MTJ. Scale bars are 10 µm. Anterior to the left in all images.

Techniques: Staining

Interactions between domains of Mmp11 and Timp4 detected by yeast two-hybrid assay.

Journal: Journal of Developmental Biology

Article Title: Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo

doi: 10.3390/jdb7040022

Figure Lengend Snippet: Interactions between domains of Mmp11 and Timp4 detected by yeast two-hybrid assay.

Techniques:

Schematic representation of hypothesized activities and interactions between Mmp11 and Timp4 paralogues at early and late MTJs. The hemopexin-like domain of Mmp11a interacts with the C-terminal domain of Timp4b in the early MTJ, facilitating the degradation of fibronectin. In the mature MTJ, Mmp11b is inhibited by Timp4a, constraining its activity in the maintenance of the ECM, while Mmp11a localizes to the Z-discs of the sarcomeres within the myocytes.

Journal: Journal of Developmental Biology

Article Title: Paralogues of Mmp11 and Timp4 Interact during the Development of the Myotendinous Junction in the Zebrafish Embryo

doi: 10.3390/jdb7040022

Figure Lengend Snippet: Schematic representation of hypothesized activities and interactions between Mmp11 and Timp4 paralogues at early and late MTJs. The hemopexin-like domain of Mmp11a interacts with the C-terminal domain of Timp4b in the early MTJ, facilitating the degradation of fibronectin. In the mature MTJ, Mmp11b is inhibited by Timp4a, constraining its activity in the maintenance of the ECM, while Mmp11a localizes to the Z-discs of the sarcomeres within the myocytes.

Techniques: Activity Assay

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anti rabbit timp4 (Novus Biologicals)

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Images

1) Product Images from "Co-chaperones TIMP2 and AHA1 Competitively Regulate Extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis"

Related Articles

FLAG-tag:

Recombinant:

Bradford Assay:

cDNA Synthesis:

SYBR Green Assay:

Enzyme-linked Immunosorbent Assay:

Sandwich ELISA:

LDH Cytotoxicity Assay:

Software:

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