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mo anti human rd systems mab1663 (R&D Systems)

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R&D Systems mo anti human rd systems mab1663
List of the 20 proteins quantified using the Reverse Phase Protein Array (RPPA) technique. The suppliers and conditions for each primary antibody used in this study after western blotting validation are given.

List of the 20 proteins quantified using the Reverse Phase Protein Array (RPPA) technique. The suppliers and conditions for each primary antibody used in this study after western blotting validation are given.

Mo Anti Human Rd Systems Mab1663, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/MAB1663/Human%2FMouse%2FRat+HSP70%2FHSPA1A+Antibody/pmc05994332-13-7-9
Average 93 stars, based on 20 article reviews

mo anti human rd systems mab1663 - by Bioz Stars, 2026-09

93/100 stars

Images

1) Product Images from "Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect"

Article Title: Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect

Journal: PeerJ

doi: 10.7717/peerj.4891

Figure Legend Snippet: List of the 20 proteins quantified using the Reverse Phase Protein Array (RPPA) technique. The suppliers and conditions for each primary antibody used in this study after western blotting validation are given.

Techniques Used: Protein Array, Western Blot, Biomarker Discovery, Protein Binding

SDS Page:

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation
Article Snippet: .. Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam). ..

Marker:

Article Title: Plasma- and Saliva Exosome Profile Reveals a Distinct MicroRNA Signature in Chronic Periodontitis
Article Snippet: The automated western blot was run according manufacturer’s protocol (JESS’s assay module Protein Normalization: AM-PN01), using 25 capillary cartridges (R&D Systems, United States: part number = SM-PN01-1). .. About 3 μg of protein was used per sample, per marker: CD9 (Novus Biologicals, United States: catalog number = NBP2-2217), CD63 (R&D Systems, United States: catalog number = MAB50482), Hsp70 (R&D Systems, United States: catalog number = MAB1663) and CD81 (Novus Biological, United States: catalog number = NB100-65805). ..

Western Blot:

Article Title: Analyzing the interactome of human CK2β in prostate carcinoma cells reveals HSP70-1 and Rho guanin nucleotide exchange factor 12 as novel interaction partners.
Article Snippet: Human CK2β is an 24.9 kDa protein with 215 amino acids encoded by the gene CSNK2B.. It is usually considered as an integral part of human protein kinase CK2, with a CK2α2β2 composition.. The CK2β amino acid sequence is highly conserved among species,1– 3 however, no other homologous protein has been described so far for CK2β, except the stellate protein from Drosophila melanogaster.4 It is known to interact with CK2α as well, but of unknown function.5 In human, single point mutations within CSNK2B leads to developmental disorders and reduced brain function, such as in the PoirierBienvenu syndrome.6,7 In mice, a complete knockout of CSNK2B results Received: 20 September 2022 | Revised: 19 December 2022 | Accepted: 9 January 2023 DOI: 10.1096/fba.2022-00098

Expressing:

Article Title: Cyclin E1 in Murine and Human Liver Cancer: A Promising Target for Therapeutic Intervention during Tumour Progression
Article Snippet: For immunoblot analysis, determination of GAPDH (MCA4739, AbD Sero-Tec, Düsseldorf, Germany) or beta actin (ab8227, Abcam, Cambridge, United Kingdom) expression was used as loading control. .. Discrimination between human non-tumorous liver, matching HCC and adenoma in small human sample cohort was validated by heat-shock protein 70 (HSP70, MAB1663, R&D Systems, Minneapolis, MN, USA) expression, an accepted biomarker for early HCC diagnosis [ ]. .. Immunoblots were visualised by ECL Prime Western Blotting System RPN2232 using an ImageQuant LAS 4000 System with LAS 4000 v1.2 Control Software (GE Healthcare, Chicago, IL, USA), according to the manufacturer’s protocol (see ).

Biomarker Discovery:

Isolation:

Article Title: Unraveling the Hsp70-ROS-autophagy axis in pentachlorophenol-challenged lung and liver epithelial cells.
Article Snippet: Pentachlorophenol (PCP) was extensively utilized as an organochlorine pesticide and wood preservative in the United States from the 1930s until the Environmental Protection Agency (EPA) imposed restrictions due to concerns about its toxicity and potential carcinogenic properties.. Although it is no longer widely used, PCP remains a concern due to its environmental persistence and potential for long-term health effects.. Significant occupational and environmental exposures have likely occurred, with the health and economic costs of PCP exposure potentially being substantial given its known toxicity.

Real-time Polymerase Chain Reaction:

Control:

Image Search Results

RFA vigorously stimulates HSP70 synthesis in DCs. C57BL/6 mice were subjected to RFA treatment. Single-cell suspensions were prepared at different timepoints followed by staining with fluorescence-conjugated viability dye, anti-CD11c, and anti-F4/80 antibodies. Cells were then permeabilized followed by intracellular staining with fluorescence-conjugated anti-HSP70 antibodies. (A) Representative dot plots showing dynamic increase of percentage of HSP70+ cells in DCs, macrophages, and non-immune cells in the first 6 h after RFA treatment or non-treated skin (baseline). (B) Percentage of HSP70+ DCs, macrophages, and non-immune cells at different timepoints till 24 h n=4. Data are representative of two independent experiments with similar results.

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: RFA vigorously stimulates HSP70 synthesis in DCs. C57BL/6 mice were subjected to RFA treatment. Single-cell suspensions were prepared at different timepoints followed by staining with fluorescence-conjugated viability dye, anti-CD11c, and anti-F4/80 antibodies. Cells were then permeabilized followed by intracellular staining with fluorescence-conjugated anti-HSP70 antibodies. (A) Representative dot plots showing dynamic increase of percentage of HSP70+ cells in DCs, macrophages, and non-immune cells in the first 6 h after RFA treatment or non-treated skin (baseline). (B) Percentage of HSP70+ DCs, macrophages, and non-immune cells at different timepoints till 24 h n=4. Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Staining, Fluorescence

Separation of RFA-induced HSP70 from constitutively expressed HSc70. (A) Lateral back skin of WT and HSP70 KO mice were subjected to RFA or Sham treatment. RFA and Sham-treated skin (1×1 cm 2 ) was collected 18 h later, homogenized, and purified with ADP-Agarose column. Eluted samples were concentrated and adjusted to the same volume of 100 µl. The same volume (10 µl) of WT samples isolated from 4 pieces of skin, KO samples isolated from one piece of skin, and recombinant murine HSP70 were subjected to SDS-PAGE separation and silver staining. (B) WT (10 µl) and KO samples (30 µl), both purified from one piece of skin, and recombinant murine HSP70 were subjected to SDS-PAGE separation and western blotting analysis with anti-HSP70 antibodies (upper) or anti-HSc70 antibodies (lower). The volume of KO samples was increased for readiness detection of HSP70 if there was any. 1. Recombinant mouse HSP70; 2. Purified sample from RFA-treated WT skin; 3. Purified sample from Sham-treated WT skin; 4. Purified sample from RFA-treated HSP70 KO skin; 5. Purified sample from Sham-treated HSP70 KO skin. Full membrane pictures were shown in <xref ref-type=

Supplementary Figure S2 . (C, D) Densitometry analysis of relative HSP70 (C) and HSc70 levels (D) of Figure 2B in WT and HSP70 KO mice using ImageJ. Results were the combination of two independent experiments with similar results. Two-way ANOVA with uncorrected Fisher’s LSD test was used to compare differences between Sham and RFA groups. N.D., not detectable. NS, not significant. ***, p<0.001. " width="100%" height="100%">

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: Separation of RFA-induced HSP70 from constitutively expressed HSc70. (A) Lateral back skin of WT and HSP70 KO mice were subjected to RFA or Sham treatment. RFA and Sham-treated skin (1×1 cm 2 ) was collected 18 h later, homogenized, and purified with ADP-Agarose column. Eluted samples were concentrated and adjusted to the same volume of 100 µl. The same volume (10 µl) of WT samples isolated from 4 pieces of skin, KO samples isolated from one piece of skin, and recombinant murine HSP70 were subjected to SDS-PAGE separation and silver staining. (B) WT (10 µl) and KO samples (30 µl), both purified from one piece of skin, and recombinant murine HSP70 were subjected to SDS-PAGE separation and western blotting analysis with anti-HSP70 antibodies (upper) or anti-HSc70 antibodies (lower). The volume of KO samples was increased for readiness detection of HSP70 if there was any. 1. Recombinant mouse HSP70; 2. Purified sample from RFA-treated WT skin; 3. Purified sample from Sham-treated WT skin; 4. Purified sample from RFA-treated HSP70 KO skin; 5. Purified sample from Sham-treated HSP70 KO skin. Full membrane pictures were shown in Supplementary Figure S2 . (C, D) Densitometry analysis of relative HSP70 (C) and HSc70 levels (D) of Figure 2B in WT and HSP70 KO mice using ImageJ. Results were the combination of two independent experiments with similar results. Two-way ANOVA with uncorrected Fisher’s LSD test was used to compare differences between Sham and RFA groups. N.D., not detectable. NS, not significant. ***, p<0.001.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Purification, Isolation, Recombinant, SDS Page, Silver Staining, Western Blot, Membrane

RFA stimulates HSP70 synthesis and extracellular release. (A, B) Lateral back skin (1.2×1.2 cm 2 ) of C57BL/6 mice was subjected to RFA or Sham treatment. Skin was dissected right after treatment and further cut into 1 mm wide slices for culture in 24-well plates. A small volume (100 µl) of medium was added to just cover the tissue. Culture medium was harvested 18 h later to measure HSP70 levels (A) . Skin was also harvested at the same time and homogenized in T-PER buffer for measurement of HSP70 levels (B) . (C, D) Lateral back skin (1.2×1.2 cm 2 ) of C57BL/6 mice was subjected to RFA or Sham treatment. Skin was then subjected to one pulse of AFL treatment at 5mJ energy and 10% coverage. Powder mannitol-coated reservoir patches were then topically applied to extract interstitial fluid via skin microchannels. Powder reservoir patches (C) and underneath skin (D) were harvested 24 h later for measurement of HSP70 levels. n=5 in A, B and n=6 in (C, D) Two-tailed student’s t-test was used to compare differences between groups. *, p<0.05; **, p<0.01. Data are representative of two independent experiments with similar results.

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: RFA stimulates HSP70 synthesis and extracellular release. (A, B) Lateral back skin (1.2×1.2 cm 2 ) of C57BL/6 mice was subjected to RFA or Sham treatment. Skin was dissected right after treatment and further cut into 1 mm wide slices for culture in 24-well plates. A small volume (100 µl) of medium was added to just cover the tissue. Culture medium was harvested 18 h later to measure HSP70 levels (A) . Skin was also harvested at the same time and homogenized in T-PER buffer for measurement of HSP70 levels (B) . (C, D) Lateral back skin (1.2×1.2 cm 2 ) of C57BL/6 mice was subjected to RFA or Sham treatment. Skin was then subjected to one pulse of AFL treatment at 5mJ energy and 10% coverage. Powder mannitol-coated reservoir patches were then topically applied to extract interstitial fluid via skin microchannels. Powder reservoir patches (C) and underneath skin (D) were harvested 24 h later for measurement of HSP70 levels. n=5 in A, B and n=6 in (C, D) Two-tailed student’s t-test was used to compare differences between groups. *, p<0.05; **, p<0.01. Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Two Tailed Test

Evidence of in situ HSP70/OVA association. Lateral back skin of WT or HSP70 KO mice was subjected to RFA or Sham treatment followed by ID injection of 1 µg OVA into RFA or Sham-treated skin. Skin was collected 6 h later. (A–C) Skin was subjected to cryo-sectioning and PLA analysis of HSP70/OVA binding. Representative HSP70/OVA PLA results in WT mice were shown in A . Quantitative analysis of HSP70/OVA PLA signals in randomly selected regions of 1.6 mm 2 in WT mice and HSP70 KO mice was shown in (B, C) , respectively. (D, E) Lateral back skin of WT and HSP70 KO mice (n=2) were exposed to RFA (left) or Sham treatment (right) followed by ID OVA injection. Skin was collected 6 h later and homogenized in RIPA buffer. The same amounts of total proteins were incubated with anti-OVA antibodies and then protein A/G agarose followed by centrifugation and washing. After boiling, IP samples and tissue lysates were subjected to SDS-PAGE and IB detection of HSP70 and OVA in WT (D) and HSP70 KO mice (E) . Intact membrane pictures were shown in <xref ref-type=

Supplementary Figure S4 . Arrows in A point to positive PLA signals. Scale in A : 100 µm. Two-tailed student’s t-test was used to compare differences between groups in (B, C) . n=31–33 in B and n=7 in C . ***, p<0.001. NS, not significant. Data are representative of two independent experiments with similar results. " width="100%" height="100%">

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: Evidence of in situ HSP70/OVA association. Lateral back skin of WT or HSP70 KO mice was subjected to RFA or Sham treatment followed by ID injection of 1 µg OVA into RFA or Sham-treated skin. Skin was collected 6 h later. (A–C) Skin was subjected to cryo-sectioning and PLA analysis of HSP70/OVA binding. Representative HSP70/OVA PLA results in WT mice were shown in A . Quantitative analysis of HSP70/OVA PLA signals in randomly selected regions of 1.6 mm 2 in WT mice and HSP70 KO mice was shown in (B, C) , respectively. (D, E) Lateral back skin of WT and HSP70 KO mice (n=2) were exposed to RFA (left) or Sham treatment (right) followed by ID OVA injection. Skin was collected 6 h later and homogenized in RIPA buffer. The same amounts of total proteins were incubated with anti-OVA antibodies and then protein A/G agarose followed by centrifugation and washing. After boiling, IP samples and tissue lysates were subjected to SDS-PAGE and IB detection of HSP70 and OVA in WT (D) and HSP70 KO mice (E) . Intact membrane pictures were shown in Supplementary Figure S4 . Arrows in A point to positive PLA signals. Scale in A : 100 µm. Two-tailed student’s t-test was used to compare differences between groups in (B, C) . n=31–33 in B and n=7 in C . ***, p<0.001. NS, not significant. Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: In Situ, Injection, Binding Assay, Incubation, Centrifugation, SDS Page, Membrane, Two Tailed Test

HSP70 contributes to RFA-enhanced antigen uptake in skin and draining LNs. WT and HSP70 KO were subjected to RFA or Sham treatment followed by ID injection of 2 µg AF647-OVA into RF or Sham-treated skin. Skin and draining LNs were dissected 20 h later followed by single-cell suspension preparation, immunostaining, and flow cytometry analysis. Gating strategies were shown in <xref ref-type=

Supplementary Figures S1B, C . (A) Percentages of AF647-OVA+ cells in skin DCs (CD11c+ MHC II+) in WT and HSP70 KO mice. (B) Representative histogram of AF647-OVA levels in skin DCs of different groups in WT and HSP70 KO mice. (C) Representative dot plots of AF647-OVA+ migDCs of different groups in WT and HSP70 KO mice. (D) Percentage of AF647-OVA+ cells in migDC (D) , cDC (E) , and pDC (F) in WT and HSP70 KO mice. Two-way ANOVA with Fisher’s LSD test was used to compare differences between groups. n=8. *, p<0.05; **, p<0.01; ***, p<0.001. Data are representative of two independent experiments with similar results. " width="100%" height="100%">

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: HSP70 contributes to RFA-enhanced antigen uptake in skin and draining LNs. WT and HSP70 KO were subjected to RFA or Sham treatment followed by ID injection of 2 µg AF647-OVA into RF or Sham-treated skin. Skin and draining LNs were dissected 20 h later followed by single-cell suspension preparation, immunostaining, and flow cytometry analysis. Gating strategies were shown in Supplementary Figures S1B, C . (A) Percentages of AF647-OVA+ cells in skin DCs (CD11c+ MHC II+) in WT and HSP70 KO mice. (B) Representative histogram of AF647-OVA levels in skin DCs of different groups in WT and HSP70 KO mice. (C) Representative dot plots of AF647-OVA+ migDCs of different groups in WT and HSP70 KO mice. (D) Percentage of AF647-OVA+ cells in migDC (D) , cDC (E) , and pDC (F) in WT and HSP70 KO mice. Two-way ANOVA with Fisher’s LSD test was used to compare differences between groups. n=8. *, p<0.05; **, p<0.01; ***, p<0.001. Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Injection, Suspension, Immunostaining, Flow Cytometry

RFA-induced HSP70 lacks the ability to induce DC maturation. (A) The same skin cell samples in <xref ref-type=

Figures 5A, B were analyzed for expression of surface co-stimulatory molecules (CD40, CD80, and CD86) in CD11c+ DCs of WT and HSP70 KO mice. MFI of CD40, CD80, and CD86 was compared between groups. (B–D) . The same LN samples as in Figures 5C, D were analyzed for expression of surface co-stimulatory molecules (CD40, CD80, and CD86) in cDC (B) , migDC (C) , and pDC (D) of WT and HSP70 KO mice. MFI of CD40, CD80, and CD86 was compared between groups. (E) BMDCs were incubated with AF647-OVA alone (control) or in the presence of HSc70 or HSP70-rich elutes or LPS. Cells were analyzed for their surface expression of CD40, CD80, and CD86 24 h later. MFI of CD40, CD80, and CD86 was compared between groups. Two-way ANOVA with Newman-Keuls’s multiple comparison test was used to compare differences between groups in A-D. One-way ANOVA with Tukey’s multiple comparison test was used to compare differences between groups in (E) n=6–8 in A-D. n=6 in (E) *, p<0.05; **, p<0.01; ***, p<0.001. Data are representative of two independent experiments with similar results. " width="100%" height="100%">

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: RFA-induced HSP70 lacks the ability to induce DC maturation. (A) The same skin cell samples in Figures 5A, B were analyzed for expression of surface co-stimulatory molecules (CD40, CD80, and CD86) in CD11c+ DCs of WT and HSP70 KO mice. MFI of CD40, CD80, and CD86 was compared between groups. (B–D) . The same LN samples as in Figures 5C, D were analyzed for expression of surface co-stimulatory molecules (CD40, CD80, and CD86) in cDC (B) , migDC (C) , and pDC (D) of WT and HSP70 KO mice. MFI of CD40, CD80, and CD86 was compared between groups. (E) BMDCs were incubated with AF647-OVA alone (control) or in the presence of HSc70 or HSP70-rich elutes or LPS. Cells were analyzed for their surface expression of CD40, CD80, and CD86 24 h later. MFI of CD40, CD80, and CD86 was compared between groups. Two-way ANOVA with Newman-Keuls’s multiple comparison test was used to compare differences between groups in A-D. One-way ANOVA with Tukey’s multiple comparison test was used to compare differences between groups in (E) n=6–8 in A-D. n=6 in (E) *, p<0.05; **, p<0.01; ***, p<0.001. Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Expressing, Incubation, Control, Comparison

$HSP70 suppresses RFA-induced TLR4/IRAK/NFκB signaling. (A, B) WT and HSP70 KO mice were subjected to RFA or Sham treatment or ID injection of LPS or PBS. Skin was collected 6 h later in (A, B) IP and IB were conducted to evaluate TLR4/TIRAP binding (A) and IRAK4/IRAK1 binding in (B, C) . WT, HSP70 KO, MyD88 KO, TLR2 KO, and TLR4 KO mice were subjected to RFA or Sham treatment or ID injection of LPS. Skin was collected 2 h later. Cytosol and nuclear fractions were separated and nuclear fraction was analyzed by WB analysis to detect phosphorylated p65 using Lamin b1 as a loading control. (D) Skin IL-6 levels 6 h after RFA, Sham, or LPS treatment of lateral back skin of WT, HSP70 KO, TLR2 KO, TLR4 KO, and MyD88 KO mice. Two-way ANOVA with Fisher’s LSD test was used to compare differences between groups. n=4-6. *, p<0.05; **, p<0.01; ***, p<0.001. Original membrane pictures were shown in <xref ref-type=$ Supplementary Figure S9 . Data are representative of two independent experiments with similar results. " width="100%" height="100%">

Journal: Frontiers in Immunology

Article Title: Dual roles of in situ generated HSP70 in antigen delivery and immunoregulation

doi: 10.3389/fimmu.2025.1638948

Figure Lengend Snippet: HSP70 suppresses RFA-induced TLR4/IRAK/NFκB signaling. (A, B) WT and HSP70 KO mice were subjected to RFA or Sham treatment or ID injection of LPS or PBS. Skin was collected 6 h later in (A, B) IP and IB were conducted to evaluate TLR4/TIRAP binding (A) and IRAK4/IRAK1 binding in (B, C) . WT, HSP70 KO, MyD88 KO, TLR2 KO, and TLR4 KO mice were subjected to RFA or Sham treatment or ID injection of LPS. Skin was collected 2 h later. Cytosol and nuclear fractions were separated and nuclear fraction was analyzed by WB analysis to detect phosphorylated p65 using Lamin b1 as a loading control. (D) Skin IL-6 levels 6 h after RFA, Sham, or LPS treatment of lateral back skin of WT, HSP70 KO, TLR2 KO, TLR4 KO, and MyD88 KO mice. Two-way ANOVA with Fisher’s LSD test was used to compare differences between groups. n=4-6. *, p<0.05; **, p<0.01; ***, p<0.001. Original membrane pictures were shown in Supplementary Figure S9 . Data are representative of two independent experiments with similar results.

Article Snippet: Supernatants were subjected to SDS-PAGE and IB detection of HSP70 (MAB1663, R & D Systems), TLR4 (sc-293072, Santa Cruz), and IRAK1 (Ab238, Abcam).

Techniques: Injection, Binding Assay, Control, Membrane

Review

mo anti human rd systems mab1663 (R&D Systems)

Structured Review

Images

1) Product Images from "Beef tenderness and intramuscular fat proteomic biomarkers: muscle type effect"

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Marker:

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Expressing:

Biomarker Discovery:

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Control:

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