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Merck

MAB13405

Sigma-Aldrich

Anti-MMP-2 Proform Antibody, NT, clone CA-4001

clone CA-4001, Chemicon®, from mouse

Synonym(s):

Gelatinase A, 72 kDa Type IV Collagenase

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

antibody form

purified antibody

antibody product type

primary antibodies

clone

CA-4001, monoclonal

species reactivity

rat, human, mouse

manufacturer/tradename

Chemicon®

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG1

NCBI accession no.

NM_004530.2

UniProt accession no.

P08253

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... MMP2(4313)

Immunogen

N-terminal peptide APSPIIKFPGDVAPKTDK of procollagenase IV, coupled to KLH.{Marqulies, et al 1992}

Application

Anti-MMP-2 Proform Antibody, N-terminus, clone CA-4001 detects level of MMP-2 Proform & has been published & validated for use in WB, IH(P).
Western Blot (0.5-1.0 μg/mL for 2 hours at room temperature, non-reduced conditions. However, chicken samples react best when fully reduced. Antibody dilution buffers should be simple for best results, PBS or TBS with 0.05% tween only. Immunogen used is highly conserved between species, thus immunoabsorption to pro-MMP2 in milk may impair reactivity.

Immunohistochemistry on frozen and formalin-fixed, paraffin-embedded tissue sections: 2-10 μg/mL for 30 minutes at room temperature. {Seftor, et al 2001} and Gottsch ML et al 2002}. Antigen retrieval is optional in most cases. Antibody dilution solutions should not contain serum because of possible immunoabsorption of the antibody to proMMP2 present in the solution.

Blocking: Inhibition of MMP-2 Activity (2-4 μg/mL).



Optimal working dilutions must be determined by end user.

Biochem/physiol Actions

It recognizes a protein of 72 kDa which is identified as pro (latent) form (active form is 62 kDa) of matrix metalloproteinase-2 and any fragment with N-terminal (proform) domain still attached. Antibody shows no cross-reaction with pro and active forms of MMP-9. MMP-2 is synthesized as 631 amino acid proenzyme which is activated by cleavage of the first 80 amino acids. MMPs 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). Cellular Localization: Cytoplasmic.

Physical form

Format: Purified
Purified from ascites fluid by Protein G chromatography. Liquid in 10 mM PBS, pH 7.4, with 0.2% BSA and 15 mM sodium azide

Analysis Note

Control
POSITIVE CONTROL: HFL-1 cells. Conditioned, serum-free medium from (TPA-treated) human fetal lung cells. Placenta.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: 04-1048

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Histiocytic sarcomas refer to highly aggressive tumors with a poor prognosis that respond poorly to conventional treatment approaches. Oncolytic viruses, which have gained significant traction as a cancer therapy in recent decades, represent a promising option for treating histiocytic sarcomas
Mark R Morgan et al.
The Journal of biological chemistry, 279(25), 26533-26539 (2004-04-07)
Integrins promote cellular invasion through a combination of activities, including adhesion to an extracellular matrix ligand, which result in the generation of intracellular signals that lead to changes in cell behavior. Until now, there have been no data that identify
Matrix metalloproteinase-2 cleavage of the ?1 integrin ectodomain facilitates colon cancer cell motility.
Kryczka, J; Stasiak, M; Dziki, L; Mik, M; Dziki, A; Cierniewski, C
The Journal of Biological Chemistry null
R Roy et al.
British journal of cancer, 111(9), 1772-1779 (2014-08-20)
A majority of patients with pancreatic malignancies, including both pancreatic ductal adenocarcinoma (PDAC) and pancreatic neuroendocrine tumours (pNETs), present with advanced disease due to a lack of specific symptoms and current diagnostic limitations, making this disease extremely difficult to detect.
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