ADAMTS13 Antibody - #DF9171
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製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# DF9171, RRID:AB_2842367.
折りたたみ／展開
A disintegrin and metalloproteinase with thrombospondin motifs 13; A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 13; A disintegrin like and metalloprotease with thrombospondin type 1 motif 13; ADAM metallopeptidase with thrombospondin type 1 motif 13; ADAM TS; ADAM-TS 13; ADAM-TS13; ADAMTS 13; ADAMTS-13; ADAMTS13; ADAMTS13 protein; ATS13_HUMAN; C9orf8; TTP; Von Willebrand factor cleaving protease; von Willebrand factor-cleaving protease; vWF cleaving protease; vWF CP; vWF-cleaving protease; vWF-CP; vWFCP;
免疫原
- Q76LX8 ATS13_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MHQRHPRARCPPLCVAGILACGFLLGCWGPSHFQQSCLQALEPQAVSSYLSPGAPLKGRPPSPGFQRQRQRQRRAAGGILHLELLVAVGPDVFQAHQEDTERYVLTNLNIGAELLRDPSLGAQFRVHLVKMVILTEPEGAPNITANLTSSLLSVCGWSQTINPEDDTDPGHADLVLYITRFDLELPDGNRQVRGVTQLGGACSPTWSCLITEDTGFDLGVTIAHEIGHSFGLEHDGAPGSGCGPSGHVMASDGAAPRAGLAWSPCSRRQLLSLLSAGRARCVWDPPRPQPGSAGHPPDAQPGLYYSANEQCRVAFGPKAVACTFAREHLDMCQALSCHTDPLDQSSCSRLLVPLLDGTECGVEKWCSKGRCRSLVELTPIAAVHGRWSSWGPRSPCSRSCGGGVVTRRRQCNNPRPAFGGRACVGADLQAEMCNTQACEKTQLEFMSQQCARTDGQPLRSSPGGASFYHWGAAVPHSQGDALCRHMCRAIGESFIMKRGDSFLDGTRCMPSGPREDGTLSLCVSGSCRTFGCDGRMDSQQVWDRCQVCGGDNSTCSPRKGSFTAGRAREYVTFLTVTPNLTSVYIANHRPLFTHLAVRIGGRYVVAGKMSISPNTTYPSLLEDGRVEYRVALTEDRLPRLEEIRIWGPLQEDADIQVYRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVRGPCSVSCGAGLRWVNYSCLDQARKELVETVQCQGSQQPPAWPEACVLEPCPPYWAVGDFGPCSASCGGGLRERPVRCVEAQGSLLKTLPPARCRAGAQQPAVALETCNPQPCPARWEVSEPSSCTSAGGAGLALENETCVPGADGLEAPVTEGPGSVDEKLPAPEPCVGMSCPPGWGHLDATSAGEKAPSPWGSIRTGAQAAHVWTPAAGSCSVSCGRGLMELRFLCMDSALRVPVQEELCGLASKPGSRREVCQAVPCPARWQYKLAACSVSCGRGVVRRILYCARAHGEDDGEEILLDTQCQGLPRPEPQEACSLEPCPPRWKVMSLGPCSASCGLGTARRSVACVQLDQGQDVEVDEAACAALVRPEASVPCLIADCTYRWHVGTWMECSVSCGDGIQRRRDTCLGPQAQAPVPADFCQHLPKPVTVRGCWAGPCVGQGTPSLVPHEEAAAPGRTTATPAGASLEWSQARGLLFSPAPQPRRLLPGPQENSVQSSACGRQHLEPTGTIDMRGPGQADCAVAIGRPLGEVVTLRVLESSLNCSAGDMLLLWGRLTWRKMCRKLLDMTFSSKTNTLVVRQRCGRPGGGVLLRYGSQLAPETFYRECDMQLFGPWGEIVSPSLSPATSNAGGCRLFINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVLYWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT
PTMs - Q76LX8 基板として
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| T358 | Phosphorylation | Uniprot | |
| T435 | Phosphorylation | Uniprot | |
| N552 | N-Glycosylation | Uniprot | |
| N614 | N-Glycosylation | Uniprot | |
| N667 | N-Glycosylation | Uniprot | |
| S696 | Phosphorylation | Uniprot | |
| S698 | O-Glycosylation | Uniprot | |
| S698 | Phosphorylation | Uniprot | |
| N707 | N-Glycosylation | Uniprot | |
| S757 | O-Glycosylation | Uniprot | |
| S907 | O-Glycosylation | Uniprot | |
| S965 | O-Glycosylation | Uniprot | |
| S1027 | O-Glycosylation | Uniprot | |
| S1087 | O-Glycosylation | Uniprot | |
| T1294 | Phosphorylation | Uniprot | |
| Y1296 | Phosphorylation | Uniprot | |
| N1354 | N-Glycosylation | Uniprot | |
| S1356 | Phosphorylation | Uniprot | |
| Y1357 | Phosphorylation | Uniprot |
研究背景
Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.
Glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion.
The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.
Secreted.
Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats.
Plasma. Expressed primarily in liver.
The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency.
The globular cysteineless spacer domain adopts a jelly-roll topology, and is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction.
参考文献
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