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MMP2 Antibody (MA1-779) in IHC (P)
Immunohistochemistry analysis of MMP2 showing staining in the cytoplasm and membrane of paraffin-embedded human breast tissue (right) compared to a negative control without primary antibody (left). To expose target proteins, antigen retrieval was performed using 10mM sodium citrate (pH 6.0), microwaved for 8-15 min. Following antigen retrieval, tissues were blocked in 3% H2O2-methanol for 15 min at room tem... View More
Product Details
MA1-779
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human
Host/Isotype
Mouse
/ IgG1, kappa
Class
Monoclonal
Type
Antibody
Clone
MMP2/2C1-1D12
Immunogen
Activated rhMMP-2
Conjugate
Form
Liquid
Concentration
1 mg/mL
Purification
Protein A
Storage buffer
PBS with 1mg/mL BSA
Contains
0.05% sodium azide
Storage conditions
-20° C, Avoid Freeze/Thaw Cycles
Shipping conditions
Ambient (domestic); Wet ice (international)
RRID
AB_889474
Product Specific Information
MA1-779 contains 100 µg of in vitro produced, protein A purified antibody (1 mg/mL) in PBS containing 1 mg/mL BSA and 0.05% sodium azide.
MA1-779 has been successfully used in Western blot applications. By Western blot, MA1-779 detects a ~66 kDa band representing purified recombinant human MMP-2.
The MA1-779 immunogen is activated rhMMP-2.
Target Information
MMP (matrix metalloproteinase) are proteolytic enzymes capable of degrading connective tissue components. MMP have a common mode of activation, a conserved amino acid sequence in the putative metal binding-active site region, and are inhibited by specific tissue inhibitors of metalloproteinases (TIMPs). MMPa and TIMPs play a significant role in regulating angiogenesis. MMP2 is synthesized as a 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids, and contains the basic structure of propeptide, catalytic, and hemopexin domains. The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. Functionally, MMP2 is involved in tissue remodeling. Mutations in MMP-2 gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome. Two transcript variants encoding different isoforms of MMP-2 have been found.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: 72 kDa gelatinase; 72 kDa type IV collagenase; CLG 4A; Collagenase; collagenase type IV-A; Gelatinase A; Gelatinase alpha; Mat; matrix metallo protease; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP; MMP-2; MMPs; neutrophil gelatinase; Progelatinase A; TBE-1; TBE1
Gene Aliases: CLG4; CLG4A; MMP-2; MMP-II; MMP2; MONA; TBE-1
UniProt ID: (Human) P08253
Entrez Gene ID: (Human) 4313
angiogenesis
response to hypoxia
blood vessel maturation
intramembranous ossification
proteolysis
embryo implantation
extracellular matrix disassembly
collagen catabolic process
endodermal cell differentiation
cellular protein metabolic process
positive regulation of innate immune response
ephrin receptor signaling pathway
face morphogenesis
bone trabecula formation
cellular response to amino acid stimulus
positive regulation of vascular smooth muscle cell proliferation
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If an Invitrogen™ antibody doesn't perform as described on our website or datasheet,we'll replace the product at no cost to you, or provide you with a credit for a future purchase.*
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