MMP-9 Protein, Human (HEK293, C-His)

Customer Review

Based on 1 Customer Validation

MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (HEK293, C-His) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-6*His labeled tag.

For research use only. We do not sell to patients.
  • Species: Human
  • Source: HEK293
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • Help & FAQs

Biological Activity

Description

MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (HEK293, C-His) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-6*His labeled tag.

Background

MMP-9 protein, a matrix metalloproteinase, plays a crucial role in the localized breakdown of the extracellular matrix and facilitates leukocyte migration. It has been suggested that MMP-9 may also be involved in bone osteoclastic resorption. Additionally, MMP-9 cleaves KiSS1 at a Gly-|-Leu bond and NINJ1 to generate the secreted form of ninjurin-1. Furthermore, it is known to cleave type IV and type V collagen, resulting in the production of large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. While MMP-9 degrades fibronectin, it does not have an impact on laminin or Pz-peptide.

Verified Bioactivity

Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2. The specific activity is ≥12000 pmol/min/µg, as measured under the described conditions. (Activation description: The proenzyme needs to be activated by APMA (HY-148905) for an activated form.)

MCE Validation Data

  • Purity - SDS-PAGE

    Purity - SDS-PAGE

    ≥ 95%, as determined by reducing SDS-PAGE.

Technical Parameters

  • Species Human
  • Source HEK293
  • Tag C-6*His
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • MMP-9 (A19-D707)
      Accession # P14780
    • 6*His
    • C-term
  • Protein Length

    Full Length of Isoform-1 (with Propeptide)

  • Synonyms

    MMP9; Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); Prev. CLG4B; Macrophage Gelatinase; Matrix Metalloproteinase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); Type V Collagenase; Matrix Metalloprot

  • AA Sequence

    AAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED

  • Predicted Molecular Mass

    76.4 kDa

  • Molecular Weight

    Approximately 80-97 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

  • Glycosylation

    Yes

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, 2 mM CaCl2, pH 7.5.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

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Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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