MMP-1 active protein

Human MMP-1

Cat. Num. AAA692133

• Gene Names: MMP1; CLG; CLGN
• Reactivity: Human
• Purity: > 90% by SDS-PAGE & HPLC analysis
• Synonyms: MMP-1; Human MMP-1; Matrix metalloproteinase-1; fibroblast collagenase; interstitial collagenase; MMP-1 active protein

• Host: E Coli
• Reactivity: Human
• Purity/Purification: > 90% by SDS-PAGE & HPLC analysis
• Form/Format: Lyophilized
• Sequence: MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEKAF QLWSNV TPLT FTKVSEGQAD IMISFVRGDH RDNSPFDGPG GNLAHAFQPG P GIGGDAHFD EDERWTNNFR EYNLHRVAAH ELGHSLGLSH STDIGAL MYP SYTFSGDVQL AQDDIDGIQA IYGRSQNPVQ PIGPQTPKAC DS KLTFDAIT TIRGEVMFFK DRFYMRTNPF YPEVELNFIS VFWPQLPN GL EAAYEFADRD EVRFFKGNKY WAVQGQNVLH GYPKDIYSSF GFP RTVKHID AALSEENTGK TYFFVANKYW RYDEYKRSMD PGYPKMIAH D FPGIGHKVDA VFMKDGFFYF FHGTRQYKFD PKTKRILTLQ KANS WFNCRK N
• Sequence Length: 469

• Biological Activity: MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 concentration of 2.5 ug/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes

Related Product Information for MMP-1 active protein

Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain which is involved in substrate specificity and in binding TIMP-1.

Product Categories/Family for MMP-1 active protein

Cytokines & Growth Factors

NCBI and Uniprot Product Information

• NCBI GI #: 4505215
• NCBI GeneID: 4312
• NCBI Accession #: NP_002412.1
• NCBI GenBank Nucleotide #: NM_002421.3
• UniProt Accession #: P03956; P08156
• Molecular Weight: 54,007 Da
• NCBI Official Full Name: interstitial collagenase isoform 1 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 1 (interstitial collagenase)
• NCBI Official Symbol: MMP1
• NCBI Official Synonym Symbols: CLG; CLGN
• NCBI Protein Information: interstitial collagenase; fibroblast collagenase; matrix metalloprotease 1; matrix metalloproteinase 1
• UniProt Protein Name: Interstitial collagenase
• UniProt Gene Name: MMP1
• UniProt Synonym Gene Names: CLG; MMP-1
• UniProt Entry Name: MMP1_HUMAN

NCBI Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes a secreted enzyme which breaks down the interstitial collagens, types I, II, and III. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Mar 2009]

Uniprot Description

Function: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity. Ref.12

Catalytic activity: Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

Cofactor: Binds 4 calcium ions per subunit.Binds 2 zinc ions per subunit.

Enzyme regulation: Can be activated without removal of the activation peptide.

Subunit structure: Interacts with HIV-1 Tat. Ref.14

Subcellular location: Secreted › extracellular space › extracellular matrix

Probable Ref.1.

Domain: There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Post-translational modification: Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase. Ref.13

Sequence similarities: Belongs to the peptidase M10A family.Contains 4 hemopexin repeats.