MCPT-1 (mMCP-1) Rat anti-Mouse, Clone: RF6.1, eBioscience™

Rat Monoclonal Antibody

Overview
Brand: Affymetrix eBioscience

Manufacturer Part Number: 14-5503-82

UNSPSC: 12352200

Code: Z2

Additional Details:
Additional Details: Weight: 0.01000kg



Disclaimers: For Research Use Only.

Product Code. 15217427

Quantity Price
1 £ 109.45 / 100µg
Estimated Shipment date
from Supplier 04-05-2017
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Description and Specification

Specification

Applications ELISA
Applications Immunocytochemistry
Applications Immunohistochemistry
Species Reactivity Mouse
Antigen MCPT-1 (mMCP-1)
Isotype IgG1
Host Species Rat
Conjugate Unlabeled
Formulation aqueous buffer, 0.09% sodium azide, may contain carrier protein/stabilizer
Quantity 100μg
Concentration 0.5mg/mL
Regulatory Status RUO
Primary or Secondary Primary
Monoclonal or Polyclonal Monoclonal
Storage Requirements Store at 2-8°C.
Format Purified
Clone RF6.1
Gene Alias Mast cell protease-1

The monoclonal antibody RF6 recognized MCPT-1 (Mast Cell Protease-1) which is a ß-chymase, a type of serine protease stored and secreted in a tissue-specific manner by mucosal mast cells. MCPT-1 is a chymotryptic protease, referring to its ability to cleave proteins and peptides after an aromatic amino acid. It shares 74% sequence homology with its rat counterpart, rat Mast Cell Protease-II (rMCP-II) and has no direct human counterpart.

MCPT-1 is the only chymase expressed by intestinal mucosal mast cells, which are found in the intestinal epithelium. Although it is expressed constitutively and is detectable in the sera of normal mice, parasites in the gut cause systemic levels to increase dramatically within two days and peak at two weeks following infection. It plays an important role in host defense against intestinal parasites, as mice deficient in MCPT-1 display delayed response upon infection. Elevated MCPT-1 levels are also observed during intestinal allergic hypersensitivity reactions. The mechanism of its action is not fully understood, although it is believed to increase intestinal permeability similarly to rMCP-II, possibly by cleaving the proteins at tight junctions between cells.