SRP6445
TIMP1 human
recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)
Sinónimos:
CLGI, EPA, EPO, FLJ90373, HCI, TIMP, TIMP metallopeptidase inhibitor 1, TIMP-1
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About This Item
Código UNSPSC:
12352202
NACRES:
NA.32
Productos recomendados
origen biológico
human
recombinante
expressed in HEK 293 cells
etiqueta
6-His tagged (C-terminus)
Análisis
≥95% (SDS-PAGE)
formulario
lyophilized
mol peso
calculated mol wt 24 kDa
observed mol wt 28-32 kDa by SDS-PAGE (DTT-reduced.)
envase
pkg of 10 μg
impurezas
<1 EU/μg endotoxin (LAL test)
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
Información sobre el gen
human ... TIMP1(7076)
Descripción general
TIMP1 (tissue inhibitor of metalloproteinase 1) is a glycoprotein and is a member of TIMP family of endogenous MMP (matrix metalloproteinase) inhibitors. Humans contain four TIMPs. All TIMPs contain an N-terminal of 125 residues, a 65-residue C-terminal, and both these domains contain three disulfide bonds. The N-terminal domain inhibits MMPs by folding into a separate unit. TIMP1 is encoded by the gene mapped to human chromosome Xp11.23.
Acciones bioquímicas o fisiológicas
TIMP1 functions as a poor inhibitor of MT1 (membrane type 1)-MMP, MT3-MMP, MT5-MMP and MMP-19. It inhibits ADAM10 (a disintegrin and metalloproteinase domain-containing protein 10) protein. In human umbilical vein endothelial cells (HUVECs), the down-regulation of TIMP1 and up-regulation of MMP-3 results in aberrant endothelium-dependent vasodilation, EC (endothelial cell) death, and endothelial interruption in a FOXO3 (forkhead box O3)-mediated manner. In patients with CAD (coronary artery disease) and acute coronary syndrome (ACS), the urine levels of this protein are elevated. This protein interacts with Bcl-2 (B cell lymphoma) protein, and induces apoptosis in lung adenocarcinoma cells. The plasma levels of this protein are increased in patients with obesity and obesity-related disorders, such as steatosis, where it participates in pathogenesis of diet-induced hepatic steatosis and glucose intolerance.
Forma física
Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.
Reconstitución
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Pierre Kunz et al.
BMC cancer, 16, 223-223 (2016-03-17)
Matrix metalloproteinases (MMPs) are crucially involved in the regulation of multiple stages of cancer progression. Elevated MMP levels have been associated with the development of metastases and poor prognosis in several types of cancer. However, the role of MMPs in
Polymorphic X-chromosome inactivation of the human TIMP1 gene.
Anderson CL and Brown CJ
American Journal of Human Genetics, 65(3), 699-708 (1999)
T Y Ho et al.
Domestic animal endocrinology, 59, 1-10 (2016-11-21)
Nursing for 2 d from birth supports neonatal porcine uterine and cervical development. However, it is not clear how timing or duration of lactocrine signaling from birth (postnatal day = PND 0) affects development of neonatal female reproductive tract tissues. Therefore
M Okamoto et al.
International endodontic journal, 52(7), 1051-1062 (2019-02-15)
To evaluate the dentinogenetic effects of tissue inhibitor of metalloprotease (TIMP1) on human pulp cells in vitro and rat pulp tissue in vivo. The effect of TIMP1 on pulp cell functions related to hard tissue formation as part of the wound healing
Christian Benzing et al.
BMC cancer, 19(1), 1214-1214 (2019-12-15)
Monocytes are a major component of the tumor microenvironment (TME) in pancreatic ductal adenocarcinoma (PDAC). However, the complex interactions between tumor cells and monocytes and their role in tumor invasion have not been fully established. To specifically test the impact
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