Matrix Protein Assays

Background

The extracellular matrix (ECM) is the scaffolding of life—providing structural support, biochemical cues, and dynamic regulation of cell behavior. Matrix proteins like collagen are central to tissue architecture, fibrosis, cancer progression, wound healing, and organ development.

Accurate quantification of matrix proteins is essential to study ECM remodeling, monitor fibrosis, validate drug targets, and characterize engineered tissues. That’s where our matrix protein assay suite comes in—targeted, quantitative, and publication-ready.

At Creative BioMart, our Matrix Protein Assay Services offer high-sensitivity, reproducible quantification of total and soluble collagen, hydroxyproline (a key collagen component), and total protein from tissue, cell culture, or engineered constructs.

With robust platforms and expert execution, we support studies in fibrosis, tissue engineering, oncology, and regenerative medicine. Whether you're quantifying matrix accumulation or normalizing ECM protein content, our assays are designed for precision and speed.

What We Offer?

Service Details

	Total Collagen Assay	Hydroxyproline Assay	Soluble Collagen Assay	Total Protein Assay
Details	This assay is to determine the total quantity of collagen precisely. It can be used to measure all forms of collagen (mature, immature, procollagen, degraded collagen, cross-linked collagen, collagen from various source). Our testing can cover a broad spectrum of samples including tissue extracts, cellular extracts, tissue culture supernatant and among others.	This assay is used to determine the quantity of hydroxyproline. Hydroxyproline results from (acid) hydrolysis of collagen. Usually from this analysis special equipment is required for removal of the HCl. Our assay does not need this step.	This assay detects soluble or (acid/pepsin) solubilized collagen in a variety of biological fluids and can be used for multiple animal species. It is intended for the use of conditioned cell culture medium and cellular extract samples. The assay is not affected by serum up to 10%.	This assay is used for the quantitative determination of all types of protein in hydrolyzed samples. The assay is based on the formation of a blue colored dye from genipin with free amino acids. It measures the total amount of amino acids present in the hydrolyzed sample, with the exception of proline and hydroxyproline.
Advantages	Quantitative measurement of all types and all forms of collagen Species independent Broad dynamic range Based on analysis of hydroxyproline	Quantitative measurement of hydroxyproline Can be applied to collagen analysis in all types of tissues	Measures all types of fibrillar collagen Species independent Not affected by serum Range: 0.5 to 10ug/ml. Sensitivity: 0.69ng/ml	Quantitative measurement of protein in acid hydrolysates of fresh, frozen, fixed and paraffin embedded tissues Species independent Broad dynamic range Range: 0.05 to 3.0 mg/ml. Sensitivity: 0.007mg/ml

Service Procedure

Why Choose Us?

Expert ECM Handling: Specialization in ECM-rich and fibrotic tissues—no clogged pipettes here.

Broad Target Range: Quantify key ECM components including collagens, elastin, fibronectin, laminin, and more.

Flexible Formats: Microplate-compatible assays for low or high sample volumes.

Custom Sample Prep: On-demand decellularization, digestion, or hydrolysis protocols.

Comprehensive Reports: Includes raw data, statistical analysis, standard curves, and interpretation.

Rapid Turnaround: Results in as little as 5 business days.

Case Study

* NOTE: We prioritize confidentiality to safeguard our clients’ technology and intellectual property. As an alternative, we present selected published research articles as representative case studies. For details on the assay services and products used in these studies, please refer to the relevant sections of the cited literature.

Case 1: Collagen constitutes in females and males of the total protein in mice

Tarnutzer et al., 2023. doi:10.1038/s41598-023-31566-z

This study revisits the common claim that collagen is the most abundant protein in mammals by directly measuring total collagen levels in entire mice using hydroxyproline content as a proxy. While collagen is highly abundant in specific tissues—up to 50% in tendons and around 30% in bones and skin—it accounts for only about 12% of total protein in female mice and 17% in male mice, which is less than previously assumed. Surprisingly, proteins like albumin, hemoglobin, histones, and actin are more abundant than collagen type I overall. Additionally, glycine was identified as the most abundant amino acid. These findings offer detailed reference data on collagen, protein, and amino acid composition in healthy wild-type mice.

Figure 1. Protein and collagen content of a mouse and its mean body weight. (a) The protein content (mg) of mice. (b) Illustrates the collagen content(mg) of mice. (c) depicts the mice's body weight (g). (Tarnutzer et al., 2023)

Case 2: Bone alkaline phosphatase and urine hydroxyproline assay in pre and postmenopausal women

Rai et al., 2021. doi:10.4103/jmh.jmh_73_21

This cross-sectional study conducted in Sikkim evaluated biochemical markers of bone turnover—bone-specific alkaline phosphatase (BALP) and urinary hydroxyproline—in 50 premenopausal and 50 postmenopausal women to assess their correlation with bone mineral density (BMD). Findings revealed significantly higher serum calcium, total ALP, and urinary hydroxyproline levels in postmenopausal women, while BALP was unexpectedly higher in premenopausal women. Postmenopausal women also exhibited significantly lower BMD, with tribal women showing greater BMD loss than nontribal counterparts.

The study supports using BALP and urinary hydroxyproline as effective, non-invasive biomarkers for early screening and prediction of osteoporosis, especially in postmenopausal women. These markers can complement existing diagnostic methods by reflecting the underlying metabolic changes rather than just structural bone loss.

Customer Testimonials

“Creative BioMart’s ECM protein profiling helped us unravel collagen subtype dynamics in our lung fibrosis model. Their custom assay for collagen VI was a game-changer—we’d been flying blind without it. Fast turnaround, solid data, and great communication throughout.”

— Principal Investigator | Pulmonary Research Institute

“We needed multiplex analysis of MMPs and TIMPs across tissue biopsies, and Creative BioMart’s Luminex-based matrix protein panel delivered exactly what we needed. Their team even helped us customize the panel to include osteopontin.”

— Director of Translational Science | Biotech Startup

“Analyzing ECM remodeling in our cartilage regeneration project was challenging until we collaborated with Creative BioMart. Their decellularization and ELISA protocols for fibronectin and aggrecan worked beautifully on our complex hydrogel scaffolds.”

— Senior Scientist | Regenerative Medicine Division, Academic Lab

“Our group needed accurate quantification of matrix proteins from decalcified bone tissue—Creative BioMart not only handled the tough sample prep but also delivered consistent ELISA data for osteocalcin and collagen I.”

— R&D Manager | Orthopedic Biopharma Company

“From laminin quantification in neural tissues to validating MMP-2 levels post-injury, Creative BioMart’s matrix protein assays have been an essential part of our neuroinflammation research. Their Simple Western analysis saved us weeks of optimization.”

— Neuroscience Research Lead | University Research Center

FAQs

• Q: What kind of samples do you accept?

  A: We accept frozen or fresh tissue, paraffin sections, cell lysates, culture supernatants, and even hydrogel scaffolds.

• Q: Can I get both collagen and hydroxyproline data from the same sample?

  A: Yes—depending on the assay combination, we can process parallel aliquots or run dual detection protocols.

• Q: What’s the minimum sample requirement?

  A: As little as 10–20 mg of tissue or 100 µL of supernatant is typically sufficient. Contact us for specific guidelines.

• Q: Are these assays species-specific?

  A: No—they are compatible with mouse, human, rat, and other species, as long as collagen/hydroxyproline is present.

References:

1. Rai AD, Sherpa ML, Singh A, Thejaswi SG, Bhutia RD. Bone alkaline phosphatase and urine hydroxyproline assay in pre and postmenopausal women in the state of Sikkim and its correlation with bone mineral density. Journal of Mid-life Health. 2021;12(4):304-309. doi:10.4103/jmh.jmh_73_21
2. Tarnutzer K, Siva Sankar D, Dengjel J, Ewald CY. Collagen constitutes about 12% in females and 17% in males of the total protein in mice. Sci Rep. 2023;13(1):4490. doi:10.1038/s41598-023-31566-z