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MAB3318

Sigma-Aldrich

Anti-TIMP-3 Antibody, a.a. 170-188, clone 136-13H4

clone 136-13H4, Chemicon®, from mouse

Sinónimos:

Tissue Inhibitor of Metalloproteinase-3

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About This Item

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

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

136-13H4, monoclonal

species reactivity

rabbit, human

manufacturer/tradename

Chemicon®

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... TIMP3(7078)

Specificity

Specifically reacts with human TIMP-3. This is a purified mouse monoclonal antibody to an oligopeptide of SWYRGWAPPDKSIINATDP (residue 170-188) on human tissue inhibitor of metalloproteinases-3 (human TIMP-3).
MAB3318 cross-reacts with rabbit TIMP-3, but does not react with human TIMP-1 and human TIMP-2.

Immunogen

Epitope: a.a. 170-188
Oligopeptide of SWYRGWAPPDKSIINATDP (residue 170-188) on human tissue inhibitor of metalloproteinases-3.

Application

Anti-TIMP-3 Antibody, a.a. 170-188, clone 136-13H4 is an antibody against TIMP-3 for use in IH(P) & WB.
Immunoblotting: 2 ug/mL

Immunohistochemistry (Paraffin):10ug/mL

Immunohistochemistry (Frozen): 2 ug/mL
Research Category
Cell Structure
Research Sub Category
MMPs & TIMPs

Target description

26 kDa

Physical form

Format: Purified
Liquid in 0.1 M sodium phosphate buffer, pH 7.0 containing 2% protease free bovine Serum albumin.
Protein A purified

Storage and Stability

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analysis Note

Control
Breast carcinoma tissue

Other Notes

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

Legal Information

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

Disclaimer

Manufactured by Daiichi Fine Chemical Co., Ltd

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.

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Interleukin-10 regulates TNF-alpha-converting enzyme (TACE/ADAM-17) involving a TIMP-3 dependent and independent mechanism.
Fionula M Brennan,Patricia Green,Parisa Amjadi,Heidi J Robertshaw et al.
European Journal of Immunology null
Catabolic properties of microdissected human endosteal bone lining cells.
C Dierkes,M Kreisel,A Schulz,J Steinmeyer,J-C Wolff,L Fink
Calcified Tissue International null
S S Apte et al.
Genomics, 19(1), 86-90 (1994-01-01)
The tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of the matrix metalloproteinases, a group of zinc-binding endopeptidases involved in the degradation of the extracellular matrix. We have isolated overlapping cDNAs encoding a novel human TIMP, TIMP-3. The cDNAs contain
C G Wilde et al.
DNA and cell biology, 13(7), 711-718 (1994-07-01)
The tissue inhibitors of metalloproteinases (TIMPs) comprise a family of proteins, of which two members have so far been described in humans. We have cloned and sequenced a third human TIMP (hTIMP-3) from phorbol ester-differentiated THP-1 cells stimulated with bacterial
Lluis Catasus et al.
Histopathology, 62(4), 632-641 (2013-02-06)
Expression of tissue inhibitor of metalloproteinases-3 (TIMP-3) has been found to be decreased in several types of cancer by promoter gene hypermethylation. However, little is known regarding the silencing effect of TIMP3 promoter hypermethylation on gene and protein expression in

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