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Collagenase Substrate (Highly Pure) Chemicals Molecular Depot
Collagenase Substrate (Highly Pure) Chemicals Molecular Depot
Collagenase Substrate (Highly Pure) Chemicals Molecular Depot
Collagenase Substrate (Highly Pure) Chemicals Molecular Depot

Collagenase Substrate (Highly Pure)

$1,395.00

    Catalog Number: B2012711 (25 mg)

    Collagenase Substrate (Highly Pure) is a high quality substrate for quantitative collagenase determination. This product has been used as molecular tool for various biochemical applications. It has also been used in a wide array of other chemical and immunological applications. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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Collagenase Substrate (Highly Pure) – Catalog #B2012711 (25 mg)

Catalog # B2012711
Lot # Batch dependent
Expiration Batch dependent
Amount 25 mg
Molecular Weight 588.6 g/mol
Supplied As Lyophilized Powder
Applications Highly pure substrate for quantitative collagenase activity assays and biochemical applications
Storage –20 °C
Grade Biotechnology grade; prepared with Type I ultrapure water (>18 MΩ·cm); 0.22 µm filtered
Keywords Z-Gly-Pro-Gly-Gly-Pro-Ala-OH

Precision collagenase substrate engineered for rigorous quantification and sensitive biochemical analysis. Collagenase Substrate (Highly Pure) – Catalog #B2012711 (25 mg) is a meticulously crafted lyophilized peptide substrate (Z-Gly-Pro-Gly-Gly-Pro-Ala-OH) specifically tailored for quantitative determination of collagenase enzymatic activity. Its high purity and defined molecular weight (588.6 g/mol) make it an optimal choice for researchers analyzing collagenase kinetics, screening inhibitors, or optimizing enzyme-linked assays of structural proteases.

The substrate's formulation supports robust and reproducible activity measurement across diverse systems, including in vitro enzymatic assays, biochemical reaction networks, and immunologic applications. It serves as a molecular-level tool to benchmark collagenase efficiency, define enzyme kinetics, or compare batch performance of collagenase enzymes. Supplied as a lyophilized powder, it offers long-term stability and flexible reconstitution for both low-volume analytical and high-throughput screening workflows.

Manufactured under biotechnology-grade conditions—using ultrapure Type I water and microfiltration—the product guarantees low contamination and high reproducibility. Whether you are profiling enzyme inhibitors, validating batch consistency, or conducting comparative proteolytic analyses, this substrate enables precise and quantifiable assessment of collagenase activity.

Why researchers choose this product:

  • High-purity substrate for accurate collagenase activity quantification
  • Defined molecular weight ensures reliable kinetic modeling
  • Lyophilized form maintains stability and accommodates flexible assay design
  • Biotech-grade preparation supports repeatable results in RUO environments
  • Ideal for enzymology, inhibitor screening, and protease activity profiling

Indication for Use:
This product is for Research Use Only (RUO). It is not intended for diagnostic, therapeutic, or clinical use.

References:

  • 1: De Souza SJ, Pereira HM, Jacchieri S, Brentani RR. Collagen/collagenase interaction: does the enzyme mimic the conformation of its own substrate? FASEB J. 1996 Jun;10(8):927-30.
  • 2: Ikeuchi T, Yasumoto M, Takita T, Tanaka K, Kusubata M, Hayashida O, Hattori S, Mizutani K, Mikami B, Yasukawa K. Crystal structure of Grimontia hollisae collagenase provides insights into its novel substrate specificity toward collagen. J Biol Chem. 2022 Aug;298(8):102109.
  • 3: Leber TM, Balkwill FR. Zymography: a single-step staining method for quantitation of proteolytic activity on substrate gels. Anal Biochem. 1997 Jun 15;249(1):24-8.
  • 4: Bhattacharya S, Bhattacharya S, Gachhui R, Hazra S, Mukherjee J. U32 collagenase from Pseudoalteromonas agarivorans NW4327: Activity, structure, substrate interactions and molecular dynamics simulations. Int J Biol Macromol. 2019 Mar 1;124:635-650.
  • 5: Tsu CA, Craik CS. Substrate recognition by recombinant serine collagenase 1 from Uca pugilator. J Biol Chem. 1996 May 10;271(19):11563-70.
  • 6: Al-Abdullah IH, Bagramyan K, Bilbao S, Qi M, Kalkum M. Fluorogenic Peptide Substrate for Quantification of Bacterial Enzyme Activities. Sci Rep. 2017 Mar 13;7:44321.
  • 7: Deng SJ, Bickett DM, Mitchell JL, Lambert MH, Blackburn RK, Carter HL 3rd, Neugebauer J, Pahel G, Weiner MP, Moss ML. Substrate specificity of human collagenase-3 assessed using a phage-displayed peptide library. J Biol Chem. 2000 Oct 6;275(40):31422-7.
  • 8: Saikumari YK, Balaram P. An internally quenched fluorescent substrate for collagenase. Biopolymers. 2008;90(2):131-8.
  • 9: Shima H, Inagaki A, Imura T, Yamagata Y, Watanabe K, Igarashi K, Goto M, Murayama K. Collagen V Is a Potential Substrate for Clostridial Collagenase G in Pancreatic Islet Isolation. J Diabetes Res. 2016;2016:4396756.
  • 10: Hasty KA, Jeffrey JJ, Hibbs MS, Welgus HG. The collagen substrate specificity of human neutrophil collagenase. J Biol Chem. 1987 Jul 25;262(21):10048-52.

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    Products are for in vitro research use only (RUO). They are not intended for human or animal use, diagnosis, therapy, resale to consumers, or residential delivery. Sales are limited to verified business addresses.

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Product Resources:

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Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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