"ADAM8" Related Products


Recombinant Human ADAM Metallopeptidase Domain 8, His-tagged

Cat. No.: ADAM8-525H
Product Overview: Recombinant Human ADAM8protein was expressed in Murine myeloma cell line with a C-terminal 6-His tag.Met1-Pro497.
Description: ADAM8, also known ascell surface antigen MS2 or CD156a, is a member of the ADAM family that containsa disintegrin and metalloproteaselike domain. ADAM8 can cleave a variety of substratesand has been shown as a sheddase for the low affinity IgE receptor CD23 andthe neural recognition molecule CHL1. Expression and regulation studiessuggest that ADAM8 is a novel osteoclast stimulating factor and may play arole in asthma.
Source: Murine myeloma cellline, NS0-derived.
Form: Supplied as a 0.2 μmfiltered solution in Glycerol, Tris, NaCl and CaCl2.
N-terminalSequence: Glu158
Molecular Weight: 38 kDa
Activity: Measuredby its ability to cleave a fluorogenic peptide substrate Mca-PLAQAV-DpaRSSSR-NH2,The specific activity is > 1 pmol/min/μg, as measured under the described conditions.
Endotoxin Level: < 1.0 EU per 1 μgof the protein by the LAL method.
SDS-PAGE: 42 kDa, reducingconditions.
Purity: > 90%, by SDSPAGEunder reducing conditions and visualized by silver stain.
Storage: Use a manual defrostfreezer and avoid repeated freeze-thaw cycles. 6 months from date of receipt,-20 to -70°C as supplied. 3 months, -20 to -70°C under sterile conditionsafter opening.
Gene Name: ADAM8 ADAM metallopeptidasedomain 8 [ Homo sapiens ]
Official Symbol: ADAM8
Synonyms: ADAM8; ADAMmetallopeptidase domain 8; MS2; CD156; CD156a; disintegrin andmetalloproteinase domain-containing protein 8; cell surface antigen MS2;human leukocyte differentiation antigen; a disintegrin and metalloproteinasedomain 8; EC 3.4.24.-
Gene ID: 101
mRNA Refseq: NM_001109
Protein Refseq: NP_001100
MIM: 602267
UniProt ID: P78325
Chromosome Location: 10q26.3
Function: calcium ion binding;cell adhesion molecule binding; metalloendopeptidase activity;metallopeptidase activity; peptidase activity; protein binding; protein self-association;zinc ion binding

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