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AB229425

Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent

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(4 Publications)

Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent is a single-wash 90-min Simplestep used to quantify Mouse Pro-Collagen I alpha 1 with a sensitivity of 2.6 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step.

- Fluorescent Sandwich ELISA - 530/570/590 nm readout : works on any standard plate reader

View Alternative Names

Cola1, Col1a1, Collagen alpha-1(I) chain, Alpha-1 type I collagen

3 Images
Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)
  • sELISA

Unknown

Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)

Interpolated concentrations of native Pro-Collagen I alpha 1 in mouse NIH 3T3 cell extract based on a 10 μg/mL extract load and mouse skin tissue extract based on a 20 μg/mL extract load. The concentrations of Pro-Collagen I alpha 1 were measured in duplicate and interpolated from the Pro-Collagen I alpha 1 standard curve and corrected for sample dilution. The interpolated dilution factor corrected values are plotted (mean +/- SD, n=2). The mean Pro-Collagen I alpha 1 concentration was determined to be 1,751 pg/mL in NIH 3T3 cell extract and 851 pg/mL in mouse skin tissue extract.

Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)
  • sELISA

Unknown

Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)

Example of mouse Pro-Collagen I alpha 1 standard curve in Sample Diluent NS.

The Pro-Collagen I alpha 1 standard curve was prepared as described in Section 10.

Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)
  • sELISA

Unknown

Sandwich ELISA - Mouse Pro-Collagen I alpha 1 ELISA Kit, Fluorescent (AB229425)

Interpolated concentrations of native Pro-Collagen I alpha 1 in mouse serum and plasma samples.

The concentrations of Pro-Collagen I alpha 1 were measured in duplicates, interpolated from the Pro-Collagen I alpha 1 standard curves and corrected for sample dilution. Undiluted samples are as follows : serum 1 : 1,200, plasma (citrate) 1 : 1,200, plasma (EDTA) 1 : 1,200 and plasma (heparin) 1 : 1,200. The interpolated dilution factor corrected values are plotted (mean +/- SD, n=2). The mean Pro-Collagen I alpha 1 concentration was determined to be 1,822 ng/mL in serum, 1,128 ng/mL in plasma (citrate), 1,628 ng/mL in plasma (EDTA), and 1,734 ng/mL in plasma (heparin).

Key facts

Detection method

Fluorescent

Sample types

Cell culture extracts, Tissue Extracts, Heparin Plasma, Citrate plasma, Serum, EDTA Plasma

Reacts with

Mouse

Assay type

Sandwich

Results type

Quantitative

Sensitivity

= 2.6 pg/mL

Range

3.91 - 16000 pg/mL

Assay time

1h 30m

Assay Platform

Pre-coated microplate (12 x 8 well strips)

Reactivity data

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Product details

Pro-Collagen I alpha 1 in vitro CatchPoint SimpleStep ELISA (Enzyme-Linked Immunosorbent Assay) kit is designed for the quantitative measurement of Pro-Collagen I alpha 1 protein in mouse serum, plasma, and cell and tissue extract samples.

This CatchPoint SimpleStep ELISA kit has been optimized for Molecular Devices Microplate Readers. Click here for a list of recommended Microplate Readers.
If using a Molecular Devices' plate reader supported by SoftMax® Pro software, a preconfigured protocol for these CatchPoint SimpleStep ELISA Kits is available with all the protocol and analysis settings at www.softmaxpro.org.

The CatchPoint SimpleStep ELISA employs an affinity tag labeled capture antibody and a reporter conjugated detector antibody which immunocapture the sample analyte in solution. This entire complex (capture antibody/analyte/detector antibody) is in turn immobilized via immunoaffinity of an anti-tag antibody coating the well. To perform the assay, samples or standards are added to the wells, followed by the antibody mix. After incubation, the wells are washed to remove unbound material. CatchPoint HRP Development Solution containing the Stoplight Red Substrate is added. During incubation, the substrate is catalyzed by HRP generating a fluorescent product. Signal is generated proportionally to the amount of bound analyte and the intensity is measured in a fluorescence plater reader at 530/570/590 nm Excitation/Cutoff/Emission.

Type I collagen is the most abundant structural protein of connective tissues such as skin, bone and tendon. It is synthesized as a pro-collagen molecule that is characterized by a 300 nm triple helical domain flanked by globular N- and C-terminal propeptides. Specifically, mouse Pro-Collagen I alpha 1 consists of a signal peptide (amino acids (aa) 1-22), a propeptide (aa 23-151), the mature chain (aa 152-1207), and another propeptide (aa 1208 – 1453). The non-helical propeptides are removed by procollagen N- and C-proteinase activities so that the mature triple helices can self-assemble into collagen fibrils that provide tensile strength to tissues.

REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.

Precision

[ { "reproducibilityType": "Inter", "sample": "Sample 3", "replicates": 0, "mean": null, "standardDeviation": null, "coefficientOfVariability": "5.6" }, { "reproducibilityType": "Intra", "sample": "Sample 8", "replicates": 0, "mean": null, "standardDeviation": null, "coefficientOfVariability": "2.4" } ]

Recovery

[ { "sample": "Serum", "range": "102 - 109 %", "average": "= 106" }, { "sample": "EDTA Plasma", "range": "102 - 116 %", "average": "= 109" }, { "sample": "Heparin Plasma", "range": "104 - 115 %", "average": "= 111" }, { "sample": "Citrate plasma", "range": "113 - 116 %", "average": "= 115" } ]

What's included?

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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Storage information
+4°C

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Collagen type I also called collagen I is a structural protein expressed mainly in connective tissues such as skin tendon bone and ligaments. It serves as an important component in providing mechanical strength and integrity to these tissues. Collagen I is a fibrillar collagen known for its triple-helix structure composed of two alpha-1 chains and one alpha-2 chain and has a molecular mass of approximately 300 kDa. Researchers often employ collagen western blot and collagen ELISA techniques for its detection. Collagen suppliers offer various collagen antibodies used in these assays to study its distribution and function.
Biological function summary

Collagen type I plays a central role in maintaining the extracellular matrix and supporting cellular environments. It interacts with other matrix proteins and cells forming complexes that help in tissue development and repair. Type I collagen is especially important in bone matrix working alongside minerals like hydroxyapatite to provide rigidity and support. Anti-collagen antibodies aid in studying its biological functions and interactions which are critical to understanding tissue dynamics.

Pathways

Collagen type I interacts with multiple signaling cascades involved in tissue remodeling and repair. It is a significant player in the TGF-β pathway which regulates fibrosis and wound healing processes. In these pathways proteins such as fibronectin and integrins work in concert with collagen type I to orchestrate cellular responses to damage. Researchers often examine its role in these pathways to uncover therapeutic possibilities for disease interventions.

Collagen type I has strong connections to conditions like osteogenesis imperfecta and fibrosis. Mutations or irregularities in collagen I production can lead to osteogenesis imperfecta a genetic disorder characterized by brittle bones. In fibrosis excessive collagen deposition disrupts normal tissue architecture contributing to organ dysfunction. In both conditions type I collagen interacts with other proteins like matrix metalloproteinases which modulate its breakdown and remodeling highlighting its importance in disease pathology.

Product protocols

Target data

Type I collagen is a member of group I collagen (fibrillar forming collagen).
See full target information Col1a1

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Nature communications 14:5529 PubMed37684243

2023

Fasting mimicking diet in mice delays cancer growth and reduces immunotherapy-associated cardiovascular and systemic side effects.

Applications

Unspecified application

Species

Unspecified reactive species

S Cortellino,V Quagliariello,G Delfanti,O Blaževitš,C Chiodoni,N Maurea,A Di Mauro,F Tatangelo,F Pisati,A Shmahala,S Lazzeri,V Spagnolo,E Visco,C Tripodo,G Casorati,P Dellabona,V D Longo

Cardiovascular diabetology 20:150 PubMed34301253

2021

The SGLT-2 inhibitor empagliflozin improves myocardial strain, reduces cardiac fibrosis and pro-inflammatory cytokines in non-diabetic mice treated with doxorubicin.

Applications

Unspecified application

Species

Unspecified reactive species

Vincenzo Quagliariello,Michelino De Laurentiis,Domenica Rea,Antonio Barbieri,Maria Gaia Monti,Andreina Carbone,Andrea Paccone,Lucia Altucci,Mariarosaria Conte,Maria Laura Canale,Gerardo Botti,Nicola Maurea

Biomedicines 8: PubMed33322134

2020

The Inhibition of Prolyl Oligopeptidase as New Target to Counteract Chronic Venous Insufficiency: Findings in a Mouse Model.

Applications

Unspecified application

Species

Unspecified reactive species

Giovanna Casili,Marika Lanza,Sarah Adriana Scuderi,Salvatore Messina,Irene Paterniti,Michela Campolo,Emanuela Esposito

Communications biology 2:20 PubMed30675518

2019

Stigmasterol accumulation causes cardiac injury and promotes mortality.

Applications

Unspecified application

Species

Unspecified reactive species

Caroline Tao,Artem A Shkumatov,Shawn T Alexander,Brandon L Ason,Mingyue Zhou
View all publications
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