MMP-9
Recombinant ID:
3929
Request Datasheet
Gene of Interest
Gene Synonyms:
Protein Names:
Accession Data
Organism:
Homo sapiens (Human)
Mass (kDa):
78458
Length (aa):
707
Sequence:
MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED
Proteomics (Proteome ID):
Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]
Proteomics (Chromosome):
UP000005640
Mass Spectrometry:
N/A
Function [CC]:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide. {ECO:0000269|PubMed:1480034}.
Metal Binding:
METAL 99 99 Zinc 2; in inhibited form. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 131 131 Calcium 1.; METAL 165 165 Calcium 2; via carbonyl oxygen.; METAL 175 175 Zinc 1; structural. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 177 177 Zinc 1; structural. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 182 182 Calcium 3.; METAL 183 183 Calcium 3; via carbonyl oxygen.; METAL 185 185 Calcium 3; via carbonyl oxygen.; METAL 187 187 Calcium 3; via carbonyl oxygen.; METAL 190 190 Zinc 1; structural. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 197 197 Calcium 2; via carbonyl oxygen.; METAL 199 199 Calcium 2; via carbonyl oxygen.; METAL 201 201 Calcium 2.; METAL 203 203 Zinc 1; structural. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 205 205 Calcium 3.; METAL 206 206 Calcium 1.; METAL 208 208 Calcium 1.; METAL 208 208 Calcium 3.; METAL 401 401 Zinc 2; catalytic. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 405 405 Zinc 2; catalytic. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.; METAL 411 411 Zinc 2; catalytic. {ECO:0000269|PubMed:12051944, ECO:0000269|PubMed:12077439}.
Site:
SITE 59 60 Cleavage; by MMP3.; SITE 106 107 Cleavage; by MMP3.
Tissue Specificity:
Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes. {ECO:0000269|PubMed:7683678}.
Disease:
Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain. {ECO:0000269|PubMed:18455130}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.; Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. {ECO:0000269|PubMed:19615667}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Mutagenesis:
MUTAGEN 402 402 E->Q: Loss of activity. {ECO:0000269|PubMed:12051944}.
Reagent Data
Name:
Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]
Class:
Subcategory:
Recombinant
Molecular Weight:
Source:
Species:
Human
Amino Acid Sequence:
Tag:
Format:
Lyophilized
Formulation:
Sterile-filtered colorless solution
Formulation Concentration:
1mg/ml
Buffer Volume:
Standard
Buffer Solution:
PBS
pH:
7.4-7.5
Stabilizers
NaCl:
Null
Metal Chelating Agents
EDTA:
Null
Purity:
> 98%
Determined:
SDS-PAGE
Stained:
Inquire
Validated:
RP-HPLC
Sample Handling
Storage:
-20°C
Stability:
This bioreagent is stable at 4°C (short-term) and -70°C(long-term). After reconstitution, sample may be stored at 4°C for 2-7 days and below -18°C for future use.
Preparation:
Reconstitute in sterile distilled H2O to no less than 100ug/ml; dilute reconstituted stock further in other aqueous solutions if needed. Please review COA for lot-specific instructions. Final measurements should be determined by the end-user for optimal performance.