Recombinant Rat Stromelysin-1(Mmp3) CSB-EP014676RA
Specifications
| 20ug / 100ug / 1mg price = 100ug |
Alternative Name(s):
(SL-1)(Matrix metalloproteinase-3)(MMP-3)(PTR1 protein)(Transin-1)
Species: (Organism)
Rattus norvegicus (Rat)
Gene Names:
Mmp3
Tag info:
N-terminal 6xHis-tagged
Target Protein AA Sequence:
FSTFPGSPKWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVEEHGDFIPFDGPGMVLAHAYAPGPGTNGDAHFDDDERWTDDVTGTNLFLVAAHELGHSLGLFHSANAEALMYPVYKSSTDLARFHLSQDDVDGIQSLYGPPTESPDVLVVPTKSNSLDPETLPMCSSALSFDAVSTLRGEVLFFKDRHFWRKSLRTPEPGFYLISSFWPSLPSNMDAAYEVTNRDTVFILKGNQIWAIRGHEELAGYPKSIHTLGLPETVQKIDAAISLKDQKKTYFFVEDKFWRFDEKKQSMDPEFPRKIAENFPGIGTKVDAVFEAFGFLYFFSGSSQLEFDPNAGKVTHILKSNSWFNC
Expression Region:
98-475aa
Subcellular Location:
Tissue Specificity:
Protein Length:
Full Length of Mature Protein
Pathway:
Mol. Weight:
48.5 kDa
Purity:
Greater than 85% as determined by SDS-PAGE.
Form:
Liquid or Lyophilized powder
Buffer:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Research Areas:
Cancer
Function:
Involvement in disease:
Relevance:
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Reconstitution:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Protein Families:
Reference:
"Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin." Umenishi F., Yasumitsu H., Ashida Y., Yamauti J., Umeda M., Miyazaki K. J. Biochem. 108:537-543(1990)
