Analytical Data
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Gene name
Maspin
- Application
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Alternative Names
SERPINB5;PI5;Serpin B5
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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
P36952
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Expression Region
1-375aa
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AA Sequence
MDALQLANSA FAVDLFKQLC EKEPLGNVLF SPICLSTSLS LAQVGAKGDT ANEIGQVLHF ENVKDVPFGF QTVTSDVNKL SSFYSLKLIK RLYVDKSLNL STEFISSTKR PYAKELETVD FKDKLEETKG QINNSIKDLT DGHFENILAD NSVNDQTKIL VVNAAYFVGK WMKKFSESET KECPFRVNKT DTKPVQMMNM EATFCMGNID SINCKIIELP FQNKHLSMFI LLPKDVEDES TGLEKIEKQL NSESLSQWTN PSTMANAKVK LSIPKFKVEK MIDPKACLEN LGLKHIFSED TSDFSGMSET KGVALSNVIH KVCLEITEDG GDSIEVPGAR ILQHKDELNA DHPFIYIIRH NKTRNIIFFG KFCSP
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Molecular Weight
46 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
Maspin (Mammary Serine Protease Inhibitor) is a member of the serpin superfamily and is primarily known for its role as a tumor suppressor in breast cancer. Its expression is often downregulated in various malignant tumors, correlating with poorer prognosis and aggressive disease. Maspin is thought to exert its effects by inhibiting serine proteases, modulating cell motility, and influencing apoptosis, thereby impacting tumor growth and progression. Research has shown that maspin can disrupt the interaction between cancer cells and the extracellular matrix, reducing invasion and metastasis, which underscores its potential therapeutic significance. Additionally, maspin has been implicated in regulating immune responses within the tumor microenvironment. Given these multifaceted roles, the study of recombinant maspin protein has gained traction, focusing on its structural properties, functional mechanisms, and potential applications in cancer therapy. Efforts to develop recombinant maspin proteins are aimed at exploring their utility as therapeutic agents or biomarkers in oncology. Understanding the biology and applications of maspin could lead to innovative strategies for the prevention and treatment of breast cancer and possibly other malignancies, highlighting the need for continued research into its reconstitution and clinical relevance.
