Analytical Data
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Gene name
ADAM5
- Application
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Alternative Names
ADAM5；ADAM5P；TMDC2；Putative disintegrin and metalloProteinase domain-containing 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
Q6NVV9
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Expression Region
1-412aa
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AA Sequence
MQTSILIKSS CRPQFQRRFH HRMQKQIQNI ISILSSASVI NSYDENDIRH SKPLLVQMDC NYNGYVAGIP NSLVTLSVCS GLRGTMQLKN ISYGIEPMEA VSGFIHKIYE EKYADTNILL EENDTYTWFN SEYQVRKSSE KTDFIKLFPR YIEMHIVVDK NLFKPANMIC RKSVGKECDF TEYCNGDLPY CLPDTYVRDG EYCDSGGAFC FQGKCRTFDK QCDDLIGRGS RGAPVFCYDE INTRGDNFGN CGTAHCLFQH ILCGKLVCTW EHRDLISRPN LSVIYAHVRD QTCVSTYLPR RTPPPVNSPI SITSYYSAED RDETFVQDGS MCGPDMYCFE MHCKHVRFLM NLKLCDASNH CDRHGVCNNF NHCHCEKGYN PPYCQPKQGA FGSIDDGHLV PPTERSYMEE GR
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Molecular Weight
47.1 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
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Protein Description
ADAM5 (A Disintegrin And Metalloproteinase 5) is part of a family of membrane-bound proteinases that play a significant role in various biological processes, including cell adhesion, migration, and signaling pathways. It is known for its involvement in the cleavage of extracellular matrix proteins and has been implicated in several physiological and pathological conditions, such as inflammation, cancer metastasis, and neurodegenerative diseases. Recent studies have highlighted the potential of ADAM5 in cellular interactions and its regulatory mechanisms, which can influence tumor growth and progression. The recombinant expression of ADAM5 protein is essential for investigating its structural and functional characteristics, allowing researchers to study its enzymatic activity, substrate specificity, and interactions with other proteins. Developing recombinant ADAM5 not only facilitates the understanding of its biological roles but also opens avenues for therapeutic interventions targeting ADAM5 in diseases where its dysregulation is implicated. Understanding the mechanisms through which ADAM5 operates may lead to novel strategies in cancer treatment and regenerative medicine. Overall, the research on ADAM5 recombinant proteins is crucial in elucidating its contributions to cellular dynamics and potential as a biomarker or therapeutic target in various diseases.
