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AB310787

Recombinant Human MMP9 Protein (His tag)

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Recombinant Human MMP9 Protein (His tag) is a Human Fragment protein, in the 20 to 469 aa range, expressed in HEK 293 cells, with >95%, <0.005 EU/µg endotoxin level, suitable for HPLC, SDS-PAGE, Mass Spec.

View Alternative Names

CLG4B, MMP9, Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB

2 Images
HPLC - Recombinant Human MMP9 Protein (His tag) (AB310787)
  • HPLC

Supplier Data

HPLC - Recombinant Human MMP9 Protein (His tag) (AB310787)

HPLC analysis of ab310787

SDS-PAGE - Recombinant Human MMP9 Protein (His tag) (AB310787)
  • SDS-PAGE

Lab

SDS-PAGE - Recombinant Human MMP9 Protein (His tag) (AB310787)

SDS-PAGE analysis of ab310787

Key facts

Purity

>95% HPLC

SDS-PAGE >= 95%

Endotoxin level

<0.005 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

HPLC, SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P14780

Animal free

Yes

Carrier free

No

Species

Human

Reconstitution

Lyophilized contents may appear as either a translucent film or a white powder. This variance does not affect the quality of the product. Store lyophilized form at room temperature. Reconstitute in phosphate buffered saline, aliquot and store at -80°C for 12 months or +4°C for 1 week. Avoid repeated freeze-thaw.

Storage buffer

pH: 7.4 Constituents: 10.26% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"linker":null,"sequence":"APRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCP","proteinLength":"Fragment","predictedMolecularWeight":"51.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":469,"aminoAcidStart":20,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P14780","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Form
Lyophilized
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
Ambient
Appropriate long-term storage conditions
Ambient
False

Supplementary information

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

The MMP-9 protein also known as matrix metalloproteinase-9 or gelatinase B functions as an enzyme involved in the breakdown of extracellular matrix proteins. It consists of a zinc ion at its active site and facilitates the degradation of type IV and V collagens fibronectin and elastin. MMP-9 has a molecular weight of approximately 92 kDa and is expressed in a variety of tissues including the liver lungs and immune cells. This enzyme can exist in monomer and dimer forms with its activity regulated by tissue inhibitors of metalloproteinases (TIMPs).
Biological function summary

Matrix metalloproteinase-9 profoundly influences tissue remodeling inflammation and angiogenesis. It does not form part of a larger protein complex but interacts closely with substrates in the extracellular matrix. MMP-9 plays important roles in processes such as embryogenesis reproduction and wound healing through the remodeling of surrounding tissues. The MMP-9 protein is often measured using assays like ELISA or analyzed via techniques such as Western blotting to determine its expression levels and activity in different biological contexts.

Pathways

MMP-9 participates in the matrix metalloproteinase pathway and the NF-kB signaling pathway. These pathways are essential in orchestrating processes such as tissue remodeling and inflammatory responses. MMP-9 acts alongside other matrix metalloproteinases including MMP-2 and is regulated by factors like cytokines growth factors and hormones ensuring the precision of extracellular matrix degradation during physiological processes.

Matrix metalloproteinase-9 has associations with cancer invasion and metastasis as well as chronic inflammatory diseases like rheumatoid arthritis. In cancer upregulated MMP-9 expression aids tumor cells in breaching the basement membrane facilitating metastasis. The disorder-associated pathways often involve interactions with proteins like vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta). Understanding MMP-9's role in these conditions can contribute to developing targeted therapies that inhibit its activity potentially mitigating disease progression.

General info

Function

Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed : 12879005, PubMed : 1480034, PubMed : 2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed : 12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed : 32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed : 1480034). Degrades fibronectin but not laminin or Pz-peptide.

Sequence similarities

Belongs to the peptidase M10A family.

Post-translational modifications

Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.. N- and O-glycosylated.

Product protocols

Target data

Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed : 12879005, PubMed : 1480034, PubMed : 2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed : 12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed : 32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed : 1480034). Degrades fibronectin but not laminin or Pz-peptide.
See full target information MMP9

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