alpha 2 Macroglobulin/A2M Antibody - #DF8174
Product: | alpha 2 Macroglobulin/A2M Antibody |
Catalog: | DF8174 |
Description: | Rabbit polyclonal antibody to alpha 2 Macroglobulin/A2M |
Application: | WB |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 180 kDa; 163kD(Calculated). |
Uniprot: | P01023 |
RRID: | AB_2841493 |
Product Info
*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.
Cite Format: Affinity Biosciences Cat# DF8174, RRID:AB_2841493.
Fold/Unfold
A2m; A2MG_HUMAN; Alpha 2 M; Alpha 2M; Alpha-2-M; Alpha-2-macroglobulin; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5; CPAMD5; DKFZp779B086; FWP007; S863 7;
Immunogens
- P01023 A2MG_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFRQGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLTVRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHYILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARLLIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAVDQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDNEDCINRHNVYINGITYTPVSSTNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARLVHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVEKEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVIKPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQNTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKHYDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCFRSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDHGSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQAPSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHALSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEGCVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAIVDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVRDLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA
PTMs - P01023 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
N55 | N-Glycosylation | Uniprot | |
N70 | N-Glycosylation | Uniprot | |
N247 | N-Glycosylation | Uniprot | |
T346 | Phosphorylation | Uniprot | |
N396 | N-Glycosylation | Uniprot | |
N410 | N-Glycosylation | Uniprot | |
Y497 | Phosphorylation | Uniprot | |
T679 | Phosphorylation | Uniprot | |
Y695 | Phosphorylation | Uniprot | |
Y708 | Phosphorylation | Uniprot | |
S710 | Phosphorylation | Uniprot | |
Y817 | Phosphorylation | Uniprot | |
K820 | Acetylation | Uniprot | |
T861 | Phosphorylation | Uniprot | |
N869 | N-Glycosylation | Uniprot | |
T898 | Phosphorylation | Uniprot | |
N991 | N-Glycosylation | Uniprot | |
Y1007 | Phosphorylation | Uniprot | |
Y1012 | Phosphorylation | Uniprot | |
Y1021 | Phosphorylation | Uniprot | |
Y1025 | Phosphorylation | Uniprot | |
K1147 | Acetylation | Uniprot | |
K1162 | Acetylation | Uniprot | |
K1164 | Acetylation | Uniprot | |
K1168 | Acetylation | Uniprot | |
S1387 | Phosphorylation | Uniprot | |
T1395 | Phosphorylation | Uniprot | |
N1424 | N-Glycosylation | Uniprot |
Research Backgrounds
Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.
Secreted.
Secreted in plasma.
Homotetramer; disulfide-linked.
Belongs to the protease inhibitor I39 (alpha-2-macroglobulin) family.
Research Fields
· Organismal Systems > Immune system > Complement and coagulation cascades. (View pathway)
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