Recombinant Rat 72 Kda Type Iv Collagenase (MMP2) Protein (His-KSI)

Name: Recombinant Rat 72 Kda Type Iv Collagenase (MMP2) Protein (His-KSI)
Brand: Beta LifeScience
SKU: BLC-07091P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat 72 Kda Type Iv Collagenase (MMP2) Protein (His-KSI) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P33436
Target Symbol	MMP2
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His-KSI
Target Protein Sequence	EHSQDPGALMAPIYTYTKNFRLSNDDIKGIQELYGPSPDADTDTGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQQVDAAFNWSKNKKTYIFSGDKFWRYNEVKKKMDPGFPKLIADSWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
Expression Range	412-662aa
Protein Length	Partial
Mol. Weight	43.6 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-\|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues.; PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta3 on the surface of blood vessels.
Subcellular Location	Secreted, extracellular space, extracellular matrix. Membrane. Nucleus.
Protein Families	Peptidase M10A family
Database References	KEGG: rno:81686 STRING: 10116.ENSRNOP00000022679 UniGene: PMID: 30061060 Suggest roles for MMP2/9 in the morphological evolution of vasculature in surgical fl aps. PMID: 27902934 MMP2 expression mediates the development of cyclophosphamide-induced cardiomyopathy. PMID: 29504102 Data show that retinoic acid receptor alpha (RARalpha) improved the renal function and attenuated the progression of glomerulosclerosis (GS) that was associated with the over-expression of matrix metalloproteinases MMP2 and MMP9. PMID: 28645189 Secretagogin-dependent MMP2 release from neurons regulates neuroblast migration. PMID: 28223495 High MMP2 expression is associated with seizures. PMID: 28501723 Studied effect of all-trans retinoic acid (ATRA) on matrix metalloproteinase 2 (MMP-2), and MMP-9 expression/ activity, and rat bone marrow-derived mesenchymal stem cell migration. MMP-2/-9 expression levels were higher in ATRA-treated MSCs; MMP-2/-9 activity was enhanced with increasing doses. Scratch test showed ATRA promoted cell migration of MSCs. PMID: 28488074 immediate postnatal nutritional programming induces increases in circulating and aortic MMP-2 activity with parallel aortic wall alterations, such as decreased elastin integrity and enhanced thickening PMID: 26547079 This study showed that in addition to the general reduction in placental and fetal growth during uteroplacental ischemia, localized angiogenic imbalance and diminished MMP-2 and MMP-9 could cause further decrease in placental and myoendometrial vascularization and placental and fetal growth in distal vs proximal uterus in hypertensive pregnant rats. PMID: 28912068 Thus, similar to pharmaceutical ACE inhibitor captopril the dipeptide IW may effectively inhibit ACE activity and prevent the age and hypertension associated rise of aortic stiffness. PMID: 27239047 Hyperglycemic animals showed an increased area of collagen fibers in the prostate, which was composed both types of collagens. MMP-2 activity was significantly reduced in the hyperglycemic animals, while MMP-9 activity was very low and showed no alteration. PMID: 28989027 High MMP2 expression is associated with uraemic vascular calcifications. PMID: 26333546 High mmp2 expression is associated with Retinitis Pigmentosa. PMID: 27893855 MMP-2 mediates sarcomere degeneration in oncostatin M-induced cardiomyocyte dedifferentiation. PMID: 27199120 conclusion, this study revealed a novel function of canstatin for inducing cell migration of adult rat cardiac fibroblasts at least in part by ERK phosphorylation through MMP-2 secretion, possibly via actin cytoskeletal change. PMID: 28003226 The increase in nuclear MMP-2 activity seen during stunning injury here, indicates yet unknown biological actions, other than lamin proteolysis, which may require more severe ischemia to effect. PMID: 27079252 The present study investigated rat models of Feeney's freefall-induced brain injury combined with Achilles tendon rupture-induced heterotopic ossification. It analyzed the altered curves of MMP-9, MMP-2 and tissue inhibitor of metalloproteinase-1 (TIMP-1) in addition to the curves of gene expression. PMID: 28259914 indicated that fibulin3 may reduce the levels of MMP2 and 9 and oxidative stress in hypertensive vascular remodeling. PMID: 27035767 a role of miR-29b-3p in vascular calcification involves targeting MMP2. PMID: 28164126 the endothelium under ANGII stimulation acts as a novel and key activator of latent pro-MT1MMP and pro-MMP2 in smooth muscle cells of rat aorta PMID: 26598508 the D/P Cr ratio was correlated with effluent levels of TN-C (rho = 0.57, p < 0.001) and MMP-2 (rho = 0.73, p < 0.001). We suggest that TN-C in the effluents may be a diagnostic marker for peritoneal deterioration with EMT-like change PMID: 26770971 cardiomyocytes in 2D culture synthesize matrix metalloproteinases MMP-2 and MMP-9 PMID: 26567576 Report cross-talk between macrophages, smooth muscle cells, and endothelial cells in response to cigarette smoke alters MMP2/9 levels. PMID: 26318311 Nuclear factor kappaB inhibitor pyrrolidine dithiocarbamate modulates myocardial MMP-2 expression and ameliorates cardiac remodelling in renovascular hypertension. PMID: 25816715 High phosphate/calcium induces vascular smooth muscle cell calcification and differentiation to an osteochondrogenic phenotype with an associated increase in MMP-2 expression. PMID: 25987498 Angiotensin II regulates MMP-2, MMP-9, and TIMP-1 expression and affects collagen deposition. PMID: 25867313 Rosiglitazone attenuates the increased MMP2/9 activity induced by cigarette smoke. PMID: 25897215 High matrix Methaloproteinase 2 expression is associated with oral cancer. PMID: 25605162 Ischemia/reperfusion-activated MMP-2 leads to the degradation of cardiac MLCK. PMID: 25451385 MMP-2 degraded Titin fragment in serum is related to induction of skeletal muscle atrophy. PMID: 25077715 The increased activationof MMP2 in spontaneously hypertensive rat may also lead to endothelial hypermeability, apoptosis and vascular rarefaction. PMID: 23481598 Effects of maternal diabetes on male offspring: high cell proliferation and increased activity of MMP-2 in the ventral prostate. PMID: 24988912 MMP2 seems to contribute to early brain elevation of IL-1beta after transient ischemia PMID: 25108165 Our results, taken together, demonstrated that MMP-2 and MMP-9 were involved in the development of H2S-induced acute lung injury and dexamethaxone exerted protective effects by alleviating the expression of MMP-2 and MMP-9. PMID: 24722316 MMP-2 may have a functionally significant role in the etiology of degenerative disc disease PMID: 23621950 The data suggest that Matrix metalloproteinases, and more specifically MMP-2, influence the growth of developing afferent neurites in the mammalian inner ear in vivo. PMID: 24935409 Results suggest that MMP-2 and MMP-9 may play a significant role in blood-brain barrier disruption after alcohol abuse. PMID: 24966898 Aortic dissection is initiated by MMP-2 overexpression as a result of increased NA release from sympathetic nervous endings in response to Ang II. PMID: 24194850 intracellular inhibition of MMP-2 in cardiomyocytes increases contractility of aerobically perfused myocytes PMID: 24769238 these results described a novel mechanism in atherosclerosis through PDGF-BB signaling in VSMC, in which MMP-2 expression is induced via extracellular signal-regulated kinases and p38 mitogen-activated protein kinase phosphorylation, as well as ROCK PMID: 24792035 Brain MMMP-2 activity levels are increased following withdrawal from self-administered cocaine. PMID: 25326689 MMP-2 -1306 C/T was shown to be involved in the pathogenesis of prostate cancer in a Turkish population. PMID: 25539555 Demonstrate that ANGII regulates pro-MMP-2 protein expression via cell-specific pathways in rat aorta. PMID: 24907869 In a rat mammary neoplasm model matrix metalloproteinase 2 localization, was localized to cancer cells and fibroblasts than in the stroma. PMID: 25343559 The levels of active MMP-2 are downregulated in peripheral nerve during diabetes and with treatment withminocycline. PMID: 25158309 The location of Mmp2 and activity can be detected by means of in situ zymography and confocal microcopy, and this methodology may provide a useful tool in studies on the role of gelatinases in tooth development, maturation and in pathological conditions. PMID: 22897943 LA modulated increased MMP-2 and MMP-9 activities and decreased TIMP-1 and TIMP-2 levels during renal I-R. PMID: 24160412 This study demonistrated that mmp2 throughout hippocampus at all ages but expression levels were highest during the first postnatal week. PMID: 24114974 I/R injury in steatotic livers resulted in significant increases in expression of YKL-40 (9 fold), and activation of MMP-2 (15 fold)/MMP-9 (12 fold). PMID: 24380732 Data indicate that mechanical stretch induces MMP-2 production in vascular smooth muscle cells (VSMC) via activation of Akt pathway, that is mediated by activation of PDGFR-beta signaling pathways. PMID: 23950935

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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