protein

Recombinant A Disintegrin And Metalloprotease 10 (ADAM10)

MBS2009286

0.01 mg

285 USD

Recombinant Protein

Recombinant A Disintegrin And Metalloprotease 10 (ADAM10)

A Disintegrin And Metalloprotease 10 (ADAM10)

Disintegrin and metalloproteinase domain-containing protein 10; Disintegrin and metalloproteinase domain-containing protein 10; disintegrin and metalloproteinase domain-containing protein 10; ADAM 10; kuzbanian protein homolog; mammalian disintegrin-metalloprotease; a disintegrin and metalloprotease domain 10; a disintegrin and metallopeptidase domain 10; ADAM metallopeptidase domain 10; Kuzbanian protein homolog; Mammalian disintegrin-metalloprotease

ADAM10

Adam10; Adam10; MADM; Madm; ADAM 10

ADA10_RAT

E Coli

544

The target protein is fused with N-terminal His-Tag, its sequence is listed below. MGHHHHHHSGSEF-TSG DKLNNNKFSL CSIRNISQVL EKKRNNCFVE SGQPICGNGM VEQGEECDCG YSDQCKDECC FDANQPEGKK CKLKPGKQCS PSQGPCCTAQ CAFKSKSEKC RDDSDCAKEG ICNGFTALCP ASDPKPNFTD CNRHTQVCIN GQCAGSICEK YDLEECTCAS SDGKDDKELC HVCCMKKMAP STCASTGSLQ WNKQFTGRTI TLQPGSPCND FRGYCDVFMR CRLVD

> 95%

Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.

Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months. Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

Organism: Rattus norvegicus (Rat). Expression System: Prokaryotic expression. Residues: Thr218~Asp445 (Accession # Q10743) with N-terminal His-Tag. Subcellular Location: Membrane; Single-pass type I membrane protein

Endotoxin Level: <1.0EU per 1ug (determined by the LAL method). Predicted Isoelectric Point: 6.4. Reconstitution: Reconstitute in sterile PBS, pH7.2-pH7.4.

About the Marker: Effective Size Range: 10kDa to 70kDa. Protein bands: 10kDa, 14kDa, 18kDa, 22kDa, 26kDa, 33kDa, 44kDa and70kDa. Double intensity bands: The 26kDa, 18kDa, 10kDa bands are at doubleintensity to make location and size approximation of proteins of interestquick and easy. Ready-to-use: No need to heat, dilute or add reducing agents before use.

37096570

Q10743.1

Q10743

26.5kDa

Alzheimer's Disease Pathway 83489!!Alzheimer's Disease Pathway 509!!Delta-Notch Signaling Pathway 198480!!Hypertrophy Model Pathway 198527

Function: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. May regulate the EFNA5-EPHA3 signaling . By similarity. Catalytic activity: Endopeptidase of broad specificity. Cofactor: Binds 1 zinc ion . By similarity. Subunit structure: Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts with EPHA2, the cleavage occurs in trans, with ADAM10 and its substrate being on the membranes of opposing cells . By similarity. Subcellular location: Membrane; Single-pass type I membrane protein. Tissue specificity: Expressed in brain, kidney, lung, spleen, ovary and testis. Domain: The Cys-rich region C-terminal to the disintegrin domain functions as a substrate-recognition module, it recognizes the EFNA5-EPHA3 Complex but not the individual proteins . By similarity. Post-translational modification: The precursor is cleaved by a furin endopeptidase . By similarity. Sequence similarities: Contains 1 disintegrin domain.Contains 1 peptidase M12B domain.

0.01 mg

285 USD