Analytical Data
-
Gene name
MMP1
- Application
-
Alternative Names
MMP1;CLG;Interstitial collagenase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P03956
-
Expression Region
20-469aa
-
AA Sequence
FPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQE FFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIE NYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHR DNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHE LGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQP IGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISV FWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFG FPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDF PGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN HHHHHHHHHH
-
Molecular Weight
53 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MMP1, or Matrix Metalloproteinase-1, is a crucial enzyme involved in the degradation of the extracellular matrix, playing a significant role in tissue remodeling and repair processes. Its study has garnered attention due to its implications in various physiological and pathological conditions, including wound healing, inflammation, and cancer metastasis. MMP1 is responsible for the cleavage of collagen, particularly type I collagen, which is a fundamental component of the extracellular matrix in connective tissues. Dysregulation of MMP1 activity has been linked to the progression of several diseases, including rheumatoid arthritis and various forms of cancer where it facilitates tumor invasion and metastasis. Researchers have been focused on developing recombinant MMP1 protein for various applications, including the investigation of its biochemical properties, functional roles in cellular processes, and potential therapeutic interventions. The recombinant protein allows for detailed studies on enzyme kinetics, inhibitor design, and the development of specific MMP1 antagonists. Understanding the structure-function relationship of MMP1 can enable the identification of novel therapeutic targets and strategies for diseases characterized by aberrant matrix remodeling. Additionally, MMP1 serves as a model for studying the broader family of matrix metalloproteinases, contributing to the understanding of their diverse roles in health and disease. This research area holds promise for developing innovative treatments that can manipulate MMP1 activity to improve tissue repair, combat cancer spread, and manage other disorders associated with extracellular matrix dysregulation.
