Human MMP-10 Alexa Fluor® 405-conjugated Antibody

Catalog #: IC9102V Datasheet
Catalog # Availability Size / Price Qty
IC9102V-100UG
R&D Systems Antibodies
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Human MMP-10 Alexa Fluor® 405-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects the pro and active forms of human MMP-10 in direct ELISAs Western blots. In direct ELISAs and Western blots, approximately 10‑50% cross‑reactivity with recombinant human (rh) MMP-3 and no cross-reactivity with rhMMP-1, -2, -7, -8, -9, -12, or -13 is observed.
Source
Monoclonal Mouse IgG1 Clone # 110316
Immunogen
Mouse myeloma cell line NS0-derived recombinant human MMP-10
Phe99-Cys476
Accession # P09238
Formulation
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Label
Alexa Fluor 405 (Excitation= 405 nm, Emission= 421 nm)

Applications

Recommended Concentration
Sample
Intracellular Staining by Flow Cytometry
0.25-1 µg/106 cells
MG‑63 human osteosarcoma cell line fixed with paraformaldehyde and permeabilized with saponin

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Background: MMP-10

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-10 (stromelysin 2) degrades a broad range of substrates including gelatin, collagen types III, IV and V, fibronectin, aggrecan, and pig cartilage proteoglycan. MMP-10 can activate other MMPs such as MMP-1 and MMP-8. MMP-10 is expressed in keratinocytes, T cells, menstrual endometrium and a few tumor samples. Structurally, MMP-10 may be divided into four distinct domains: a pro-domain which is cleaved upon activation, a catalytic domain containing the zinc binding site; a short linker region, and a carboxyl terminal hemopexin-like domain.

Long Name
Matrix Metalloproteinase 10
Entrez Gene IDs
4319 (Human)
Alternate Names
EC 3.4.24; EC 3.4.24.22; matrix metallopeptidase 10 (stromelysin 2); matrix metalloprotease 10; matrix metalloproteinase 10 (stromelysin 2); Matrix metalloproteinase-10; MMP10; MMP-10; SL-2; STMY2stromelysin-2; Stromelysin 2; transin 2; transin-2

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Product Specific Notices


This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.

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