Analytical Data
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Gene name
MFAP5
- Application
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Alternative Names
MFAP5；MAGP2；Microfibrillar-associated Protein 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13361
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Expression Region
22-173aa
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AA Sequence
IPLGVNSQRGDDVTQATPETFTEDPNLVNDPATDETVLAVLADIAPSTDDLASLSEKNTTAECWDEKFTCTRLYSVHRPVKQCIHQLCFTSLRRMYIVNKEICSRLVCKEHEAMKDELCRQMAGLPPRRLRRSNYFRLPPCENVDLQRPNGL
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Molecular Weight
33.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
MFAP5 (Microfibril-Associated Protein 5) is a crucial extracellular matrix protein that plays a significant role in the structural integrity and function of various tissues, particularly in the cardiovascular system. Its involvement in the formation and maintenance of elastic fibers highlights its importance in connective tissue biology. Studies have indicated that MFAP5 may be linked to various pathological conditions, including vascular diseases and some forms of cancer, due to its regulatory role in cell adhesion, migration, and proliferation. This has spurred interest in understanding the molecular mechanisms underlying its function and its potential as a biomarker or therapeutic target. The production of recombinant MFAP5 protein has facilitated biochemical and biophysical analyses, allowing researchers to explore its interactions with other extracellular matrix components and cells. By employing techniques such as protein engineering and structural biology, scientists aim to elucidate the precise role of MFAP5 in normal physiology and disease contexts. Overall, MFAP5 represents a promising area of research with implications for developing novel strategies in regenerative medicine and tissue engineering, as well as for understanding the molecular basis of diseases associated with the extracellular matrix.
