SAB4502973
Anti-TIMP3 antibody produced in rabbit
affinity isolated antibody
Szinonimák:
Metalloproteinase inhibitor 3, Protein MIG-5, TIMP-3, Tissue inhibitor of metalloproteinases 3
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
biológiai forrás
rabbit
Minőségi szint
konjugátum
unconjugated
antitest forma
affinity isolated antibody
antitest terméktípus
primary antibodies
klón
polyclonal
form
buffered aqueous solution
molekulatömeg
antigen 24 kDa
faj reaktivitás
mouse, rat, human
koncentráció
~1 mg/mL
technika/technikák
ELISA: 1:10000
western blot: 1:500-1:1000
NCBI elérési szám
UniProt elérési szám
kiszállítva
wet ice
tárolási hőmérséklet
−20°C
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... TIMP3(7078)
Általános leírás
Tissue inhibitor of metalloproteinases 3 (TIMP3) belongs to the matrix metalloproteinases inhibitor family. TIMP3 gene is mapped to human chromosome 22q12.3. TIMP3 possesses a C-terminal N-linked glycosylation site at asparagine residue. This protein comprises 12 conserved cysteine residues stabilized by six disulfide bonds in its secondary structure. TIMP-3 gene expression is higher in murine lung and kidney.
Immunogen
The antiserum was produced against synthesized peptide derived from human TIMP3.
Immunogen Range: 91-140
Immunogen Range: 91-140
Biokémiai/fiziológiai hatások
Tissue inhibitor of metalloproteinases 3 (TIMP3) inhibits membrane-type matrix metalloproteinases (MT-MMPs) and the tumor necrosis factor α–converting enzyme (TACE). It displays a high affinity for the proteoglycans associated with extracellular matrix (ECM) and displays tight binding with sulfated glycosaminoglycans. Mutations in the TIMP-3 gene is implicated in Sorsby′s fundus dystrophy which is characterized by choroidal neovascularization, vision loss, and abnormal Bruch′s membrane thickening. Downregulation of TIMP3 gene due to allelic losses on 22q12 chromosomal location is correlated to meningiomas. TIMP3 participates in cardiac remodeling. Low levels of TIMP3 protein are observed in scenarios of ischemic and dilated cardiomyopathy. This protein elicits proapoptotic activity and is an inhibitor of angiogenesis and tumor growth.
Tulajdonságok és előnyök
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Fizikai forma
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Jogi nyilatkozat
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Tárolási osztály kódja
10 - Combustible liquids
WGK
nwg
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Anne M Macgregor et al.
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 57(3), 207-213 (2008-10-29)
Tissue inhibitor of matrix metalloproteinase-3 (TIMP-3) is an important regulator of matrix metalloproteinase activity in many types of disease, including atherosclerosis, neoplasia, and inflammatory conditions. Among TIMPs, TIMP-3 uniquely binds the extracellular matrix (ECM). We performed IHC staining on 17
Robert Visse et al.
Circulation research, 92(8), 827-839 (2003-05-06)
Matrix metalloproteinases (MMPs), also designated matrixins, hydrolyze components of the extracellular matrix. These proteinases play a central role in many biological processes, such as embryogenesis, normal tissue remodeling, wound healing, and angiogenesis, and in diseases such as atheroma, arthritis, cancer
Dimitri Barski et al.
Brain pathology (Zurich, Switzerland), 20(3), 623-631 (2009-11-20)
The gene for the tissue inhibitor of metalloproteinase 3 (TIMP3) on 22q12.3 had been reported to be inactivated by promoter methylation in various types of cancers, with controversial findings in meningiomas. We performed direct sodium bisulfite sequencing in a series
Dong Fan et al.
Frontiers in physiology, 11, 661-661 (2020-07-03)
Tissue inhibitor of metalloproteinase 3 (TIMP3) is unique among the four TIMPs due to its extracellular matrix (ECM)-binding property and broad range of inhibitory substrates that includes matrix metalloproteinases (MMPs), a disintegrin and metalloproteinases (ADAMs), and ADAM with thrombospondin motifs
Jian Hua Qi et al.
Nature medicine, 9(4), 407-415 (2003-03-26)
Tissue inhibitor of metalloproteinases-3 (TIMP3) is one of four members of a family of proteins that were originally classified according to their ability to inhibit matrix metalloproteinases (MMP). TIMP3, which encodes a potent angiogenesis inhibitor, is mutated in Sorsby fundus
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