Anti type 1 collagen

Manufactured by Southern Biotech

Sourced in United States

Anti-type I collagen is a laboratory product used for the detection and quantification of type I collagen in biological samples. It functions as a specific antibody that binds to type I collagen, allowing researchers to measure the presence and concentration of this structural protein.

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Lab products found in correlation

Anti phospho smad2, by Cell Signaling Technology (2 mentions) Anti α tubulin, by Merck Group (2 mentions) Anti α smooth muscle actin anti α sma, by Merck Group (2 mentions) Anti f4 80, by Bio-Rad (1 mentions) Anti β actin, by Cell Signaling Technology (1 mentions) Anti fibronectin, by Santa Cruz Biotechnology (1 mentions) Anti nlrp3, by Cell Signaling Technology (1 mentions) β actin, by Merck Group (1 mentions) Anti α smooth muscle actin, by Merck Group (1 mentions) Ultra resolution digital scanning system, by Leica (1 mentions) Anti phospho gsk3β ser9, by Cell Signaling Technology (1 mentions) Anti yap taz d24e4, by Cell Signaling Technology (1 mentions) Anti phospho akt ser473, by Cell Signaling Technology (1 mentions) Anti smad1, by Cell Signaling Technology (1 mentions) Anti smad2 3, by Cell Signaling Technology (1 mentions) Anti akt c67e7, by Cell Signaling Technology (1 mentions) Anti phospho smad2 ser465 467, by Cell Signaling Technology (1 mentions) Anti gapdh, by Thermo Fisher Scientific (1 mentions) Anti sirt1, by Santa Cruz Biotechnology (1 mentions) Anti β actin, by Santa Cruz Biotechnology (1 mentions)

Spelling variants of this product

Collagen I (29 citations) Type I collagen (19 citations) Anti-collagen I (12 citations)

6 protocols using anti type 1 collagen

Inflammatory Pathway Protein Analysis

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We purchased and used the following commercially available antibodies: anti-interleukin-1β, anti-ASC (apoptosis-associated speck-like protein containing a CARD), anti-caspase-1 (p10), anti-fibronectin (Santa Cruz Biotechnology, Inc., Dallas, TX), anti-NLRP3 (Cell Signalling Technology, Danvers, MA), anti-F4/80 (Bio-Rad Laboratories, Hercules, CA), anti-type I collagen (SouthernBiotech, Birmingham, AL), and anti-β-actin (protein loading control, Cell Signalling Technology).

Ikeda Y., Horinouchi Y., Hamano H., Hirayama T., Kishi S., Izawa-Ishizawa Y., Imanishi M., Zamami Y., Takechi K., Miyamoto L., Ishizawa K., Aihara K.I., Nagasawa H., Tsuchiya K, & Tamaki T. (2017). Dietary iron restriction alleviates renal tubulointerstitial injury induced by protein overload in mice. Scientific Reports, 7, 10621.

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Western Analysis of Fibroblast Proteins

Cited 1 time

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At the end of each experiment, fibroblasts were harvested and whole-cell lysates subjected to western analysis as described [12 (link)]. The following antibodies were used: anti-phospho-Smad2 (Cell Signaling Technology, Boston, MA, USA), anti-type I collagen (Southern Biotech, Birmingham, AL, USA), A20 (Santa Cruz, Dallas, TX, USA), anti-α smooth muscle-actin (αSMA), beta actin and tubulin (all from Sigma, St. Louis, MO, USA). Proteins were visualized using ECL reagents (Pierce, Rockford, IL, USA) and levels were quantitated by determining band intensities normalized to loading controls in each lane using ImageJ software.

Bhattacharyya S., Wang W., Graham L.V, & Varga J. (2016). A20 suppresses canonical Smad-dependent fibroblast activation: novel function for an endogenous inflammatory modulator. Arthritis Research & Therapy, 18, 216.

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Quantitative Analysis of Collagen and SMA

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At the end of the experiments, fibroblast cultures were harvested, and whole cell protein lysates were subjected to Western blot analysis. The following antibodies were used: anti–type I collagen (SouthernBiotech), anti–α-smooth muscle actin (anti–α-SMA) (Sigma), anti-GAPDH (Zymed), and anti–α-tubulin (Sigma). Bands were visualized using enhanced chemiluminescence reagents (Pierce), and images were captured using a Fujifilm (Fuji). In each sample, band intensities were quantified with ImageJ software and normalized to GAPDH.

Fang F., Marangoni R.G., Zhou X., Yang Y., Ye B., Shangguang A., Qin W., Wang W., Bhattacharyya S., Wei J., Tourtellotte W.G, & Varga J. (2016). Toll-like Receptor 9 Signaling Is Augmented in Systemic Sclerosis and Elicits Transforming Growth Factor β–Dependent Fibroblast Activation. Arthritis & rheumatology (Hoboken, N.J.), 68(8), 1989-2002.

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Cardiac Myocyte Hypertrophy Measurement

Cited 2 times

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The extent of cardiac myocyte hypertrophy was determined on haematoxylin and eosin stained sections, as previously reported [11 (link)]. In brief, stained sections were scanned digitally by high resolution microscopy (Ultra-Resolution Digital Scanning System, Aperio Technologies Inc., Vista, CA), and images analyzed with The NDP view2 software (Hamamatsu Photonics, Hamamatsu City, Shizuoka Pref., Japan). Cardiac myocytes with elliptical nuclei in transverse section were selected. Diameter measurements were taken membrane to membrane across the narrowest point that crosses the nucleus. The average diameter of 30–50 myocytes per animal was measured, as previously described [12 (link)].
Changes in cardiac structure were assessed in a masked protocol in animals from each group. Sections were stained with fibrillar collagen subtypes I and III using specific antibodies (anti-type I collagen: Southern Biotechnology Associates, Inc. Birmingham, AL; anti-type III collagen: Biogenex, San Ramon, CA), and quantified as previously reported [7 (link)].

Connelly K.A., Zhang Y., Desjardins J.F., Nghiem L., Visram A., Batchu S.N., Yerra V.G., Kabir G., Thai K., Advani A, & Gilbert R.E. (2020). Load-independent effects of empagliflozin contribute to improved cardiac function in experimental heart failure with reduced ejection fraction. Cardiovascular Diabetology, 19, 13.

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Protein Expression and Quantification

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Cells were lysed and processed as described previously (Pannu et al., 2006 (link)), using anti-type I collagen (SouthernBiotech, Birmingham, AL), anti-phosho-Smad1/5 (Ser463/465) (41D10; Cell Signaling TECHNOLOGY, Danvers, MA), anti-Smad1 (Cell Signaling Technology), anti-phospho-Smad2 (Ser465/467) (Cell Signaling Technology), anti-Smad2/3 (Cell Signaling Technology), anti-CTGF (L-20; Santa Cruz Biotechnology, Dallas, TX), anti-YAP/TAZ (D24E4; Cell Signaling Technology), anti-phospho-GSK3β (Ser9) (119A11; Cell Signaling Technology), anti-GSK3β (H-76; Santa Cruz Biotechnology), anti-phospho-Akt (Ser473) (193H12; Cell Signaling Technology), anti-phospho-YAP (S127) (D9W2I; Cell Signaling Technology) and anti-Akt (C67E7; Cell Signaling Technology) antibodies. Densitometric quantification was done using Image J.

Toyama T., Looney A.P., Baker B.M., Stawski L., Haines P., Simms R., Szymaniak A.D., Varelas X, & Trojanowska M. (2017). Therapeutic targeting of TAZ and YAP by dimethyl fumarate in systemic sclerosis fibrosis. The Journal of investigative dermatology, 138(1), 78-88.

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Protein Expression Analysis in Cell Cultures

Cited 1 time

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At the end of the incubation periods, cultures were harvested, and equal amounts of whole-cell lysates (5–15 µg) were subjected to electrophoresis in Tris–glycine 4–15% gradient gels and transferred to PVDF membranes (15 (link)). Membranes were incubated with the primary antibodies anti–type I collagen (1:400; SouthernBiotech), anti–phospho-Smad2 (1:1,000; Cell Signaling Technology), anti-SIRT1, anti–histone H4, anti–β-actin, and anti-p300 (all 1:200; all from Santa Cruz Biotechnology), anti–α-smooth muscle actin (anti–α-SMA) and anti–α-tubulin (both 1:3,000; both from Sigma), and anti-GAPDH (1:3,000; Invitrogen), followed by appropriate secondary antibodies. Antigen–antibody complexes were visualized by enhanced chemiluminescence (Pierce). Protein levels were quantitated by determining band intensities normalized to loading controls in each lane using ImageJ software (http://rsb.info.nih.gov/ij/).

Wei J., Ghosh A.K., Chu H., Fang F., Hinchcliff M.E., Wang J., Marangoni R.G, & Varga J. (2015). The Histone Deacetylase Sirtuin 1 Is Reduced in Systemic Sclerosis and Abrogates Fibrotic Responses by Targeting Transforming Growth Factor β Signaling. Arthritis & rheumatology (Hoboken, N.J.), 67(5), 1323-1334.

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