MMP-2 (D4M2N) Rabbit mAb (BSA and Azide Free) #35814

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)	64, 72
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
IHC-Immunohistochemistry
IF-Immunofluorescence

Species Cross-Reactivity Key:

H-Human

Product Information

Product Usage Information

This product is the carrier free version of product #40994. All data were generated using the same antibody clone in the standard formulation which contains BSA and glycerol.

This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.

BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.

Formulation

Supplied in 1X PBS (10 mM Na₂HPO₄, 3 mM KCl, 2 mM KH₂PO₄, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

For standard formulation of this product see product #40994

Storage

Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

Specificity / Sensitivity

MMP-2 (D4M2N) Rabbit mAb (BSA and Azide Free) recognizes endogenous levels of total MMP-2 protein.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human MMP-2 protein.

Background

The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (5).

Database Links

UniProt ID: P08253

Entrez-Gene Id: 4313

限制使用

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For Research Use Only. Not For Use In Diagnostic Procedures.

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