Analytical Data
-
Gene name
MFAP2
- Application
-
Alternative Names
MFAP2;MAGP1;Microfibrillar-associated Protein 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P55001
-
Expression Region
76-158aa
-
AA Sequence
PAPTPEPGNAELEPTEPGPLDCREEQYPCTRLYSIHRPCKQCLNEVCFYS LRRVYVINKEICVRTVCAHEELLRADLCRDKFS
-
Molecular Weight
35 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
MFAP2, or Microfibril-Associated Protein 2, is a crucial component of the extracellular matrix and plays a significant role in connective tissue structure and function. It is primarily found in tissues rich in elastic fibers, such as the aorta and skin, where it contributes to the stability and maintenance of elastic fibers. Recent research has highlighted MFAP2's involvement in various physiological and pathological processes, including cardiovascular health, tissue repair, and fibrosis. Additionally, aberrant expression of MFAP2 has been linked to several diseases, including cardiovascular disorders and certain types of cancer. The study of recombinant MFAP2 protein offers valuable insights into its molecular functions and potential therapeutic applications. By utilizing recombinant technologies, researchers can produce purified MFAP2 for in-depth functional studies, enabling a better understanding of its role in disease mechanisms and the development of innovative strategies for treatment. Therefore, MFAP2 serves as a vital target not only to elucidate the complexities of extracellular matrix interactions but also to pave the way for novel therapeutic approaches in regenerative medicine and disease management.
