MMP9 Human, HEK

Matrix Metalloproteinase-9 Human Recombinant, HEK
Cat. No.
BT9516
Source

HEK293 Cells.

Synonyms

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

MMP9 Human Recombinant is a single, glycosylated polypeptide chain containing 694 amino acids (20-707a.a) and having a molecular mass of 77.2kDa (calculated). MMP9 is fused to a 6 a.a His tag at C-terminal.

Product Specs

Introduction
Matrix metalloproteinases (MMPs) are enzymes that play a crucial role in the breakdown of extracellular matrix proteins. MMP9, a member of this family, is initially synthesized as an inactive precursor (zymogen) and becomes activated through cleavage. It is involved in various physiological processes like inflammation, tissue remodeling, and wound healing, and its dysregulation is implicated in conditions such as tumor growth and intervertebral disc disease. MMP9 exhibits specific activity against collagen types IV and V, contributing to extracellular matrix degradation and influencing cell migration.
Description
This product consists of a recombinant human MMP9 protein, modified to include a 6-amino acid His tag at its C-terminus. The protein is glycosylated and has a molecular weight of 77.2 kDa.
Physical Appearance
White powder, obtained through lyophilization (freeze-drying) after filtration.
Formulation
The MMP9 protein was filtered through a 0.4 μm filter and subsequently lyophilized. The lyophilization buffer consists of 0.5 mg/ml MMP9 in phosphate-buffered saline (PBS) at pH 7.5, with 5% (w/v) Threalose added.
Solubility
To prepare a working solution, add deionized water to the lyophilized protein to achieve a concentration of approximately 0.5 mg/ml. Allow time for the pellet to dissolve completely.
Stability
For long-term storage, keep the lyophilized protein at -20°C. Once reconstituted, it is recommended to aliquot the protein solution to minimize freeze-thaw cycles. The reconstituted protein can be stored at 4°C for up to two weeks without significant degradation.
Purity
The purity of this protein is greater than 95%, as determined by SDS-PAGE analysis.
Synonyms

Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

Source

HEK293 Cells.

Amino Acid Sequence

APRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPET

GELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAF

ALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDD

ELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFG

FCPSERLYTRDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTR

ADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQ

GYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTT

PQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAE

IGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGAS

VLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLD

THDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPEDHHHHHH.

Product Science Overview

Structure and Expression

Recombinant human MMP-9 is expressed in human embryonic kidney (HEK) 293 cells. This expression system allows for human-like glycosylation and folding, which often supports higher specific activity of the protein . The recombinant MMP-9 is a glycoprotein with a calculated molecular mass of 76 kDa, but it migrates as a ~92 kDa polypeptide on SDS-PAGE due to glycosylation . The protein is produced without artificial tags, ensuring its natural structure and function .

Functional Domains

MMP-9 is one of the most complex members of the MMP family in terms of domain structure and regulation of its activity. It can be divided into five distinct domains:

  1. Pro-domain: Cleaved upon activation.
  2. Gelatin-binding domain: Consists of three contiguous fibronectin type II units.
  3. Catalytic domain: Contains the zinc-binding site.
  4. Proline-rich linker region.
  5. Carboxyl-terminal hemopexin-like domain .
Biological Functions

MMP-9 is involved in the degradation of type IV and V collagens, elastin, and gelatin, which are components of the ECM. This degradation is essential for various physiological processes, including:

  • Embryonic development: MMP-9 facilitates tissue remodeling and cell migration.
  • Reproduction: It plays a role in the breakdown of the ECM during ovulation and implantation.
  • Tissue remodeling: MMP-9 is involved in wound healing and the remodeling of tissues .

In pathological conditions, MMP-9 is implicated in:

  • Arthritis: Degradation of cartilage and joint tissues.
  • Cancer metastasis: Breakdown of the ECM, allowing cancer cells to invade surrounding tissues and spread to other parts of the body .
Research and Clinical Implications

Studies in rhesus monkeys suggest that MMP-9 is involved in interleukin-8 (IL-8)-induced mobilization of hematopoietic progenitor cells from bone marrow. In murine models, MMP-9 has been shown to play a role in tumor-associated tissue remodeling . Additionally, thrombospondins, intervertebral disc proteins, regulate the effective levels of MMP-2 and MMP-9, which are key effectors of ECM remodeling .

Recombinant human MMP-9 expressed in HEK 293 cells is widely used in research to study its structure, function, and role in various diseases. It is also used as a standard in gelatin zymography, a technique to detect proteolytic activity .

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