MAB13406
Anti-MMP-2 Antibody, pro and active form, clone VB3
clone VB3, Chemicon®, from mouse
别名:
Gelatinase A, 72 kDa Type IV Collagenase
产品名称
Anti-MMP-2 Antibody, pro and active form, clone VB3, clone VB3, Chemicon®, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified antibody
antibody product type
primary antibodies
clone
VB3, monoclonal
species reactivity
human
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunofluorescence: suitable
western blot: suitable
isotype
IgG1
suitability
not suitable for immunohistochemistry
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... MMP2(4313)
Analysis Note
Control
POSITIVE CONTROL: Conditioned, serum-free medium from (dexametha-sone-treated) human fibrosarcoma HT-1080 or endothelial HUVEC cells. Placenta. Bladder, breast and ovarian carcinomas.
POSITIVE CONTROL: Conditioned, serum-free medium from (dexametha-sone-treated) human fibrosarcoma HT-1080 or endothelial HUVEC cells. Placenta. Bladder, breast and ovarian carcinomas.
Application
Research Category
Cell Structure
Cell Structure
Research Sub Category
MMPs & TIMPs
MMPs & TIMPs
This Anti-MMP-2 Antibody, pro & active form, clone VB3 is validated for use in ELISA, IF, WB for the detection of MMP-2.
Western blot: 1:200-1:400 for 2 hours at room temperature
ELISA
Immunofluorescence
Does not work for immunohistochemistry Optimal working dilutions must be determined by end user.
ELISA
Immunofluorescence
Does not work for immunohistochemistry Optimal working dilutions must be determined by end user.
Biochem/physiol Actions
The antibody recognizes proteins of 72kDa and 66kDa which are identified as pro (latent) and active forms of matrix metalloproteinase-2 (MMP-2; also known as 72 kDa collagenase IV or gelatinase A). Shows no cross-reactivity with pro and active forms of other MMPs. MMPs are proteolytic enzymes capable of degrading connective tissue components. Degradation of the extracellular matrix (ECM) is an essential step in tumor invasion and metastasis. MMPs each have different substrate specificities within the ECM and are important in its degradation. MMP-2 mainly degrades type IV collagen and denatured collagens. MMP activity is modulated by tissue inhibitors of metalloproteinases (TIMP). Imbalanced secretion of certain MMP or disturbances in the differential control of MMP by TIMP have been implicated in the invasive potential of malignant tumors.Cellular Localization: cytoplasmic
Disclaimer
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.
Immunogen
Epitope: pro and active form
Human native 72 kDa Gelatinase A.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 04-1048
Physical form
200 μg/mL. of antibody purified from ascites fluid by Protein G chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 0.09% sodium azide.
Format: Purified
Preparation Note
Maintain refrigerated at 2-8°C in undiluted aliquots for up to 12 months.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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存储类别
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Type IV collagen ?1-chain noncollagenous domain blocks MMP-2 activation both in-vitro and in-vivo.
Sudhakar, YA; Verma, RK; Pawar, SC
Scientific Reports null
Eliana Pivetta et al.
Breast cancer research : BCR, 13(5), R105-R105 (2011-10-29)
The increased bone degradation in osteolytic metastases depends on stimulation of mature osteoclasts and on continuous differentiation of new pre-osteoclasts. Metalloproteinases (MMP)-13 is expressed in a broad range of primary malignant tumours and it is emerging as a novel biomarker.
Basudeb Das et al.
Biology of the cell, 112(3), 73-91 (2019-12-28)
Piwi-interacting RNAs (piRNAs) are a novel class of ∼23-36 nts long endogenous small non-coding RNAs, earlier known to maintain germline genome integrity during development by regulating transposable elements. Recently, piRNAs are known to regulate cell proliferation, apoptosis and metastasis in
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