Sheep MMP-1 ELISA KIT (96 T)

Specifications

Product Data
Description	Sheep MMP-1 ELISA Kit
Size	96 T
Format	96-well strip plate
Assay Type	Solid Phase Sandwich ELISA
Assay Length	4 hours
Signal	Colorimetric
Curve Range	125-8000 pg/ml
Sample Type	Serum, plasma, Cell culture supernatant
Sample Volume	100 uL
Specificity	This assay recognizes both natural and recombinant Sheep MMP-1
Sensitivity	65 pg/mL
Reactivity	Sheep
Interference	No significant interference observed with available related molecules.
Components	Microwell Plate - antibody coated 96-well Microplate (8 wells ×12 strips),1 plate Standard - lyophilized,8000pg/ml upon reconstitution,2 vials lyophilized, Biotin-Conjugated antibody,2 vials Concentrated Streptavidin-HRP,1 vial Standard /sample Diluent,1 bottle Biotin-Conjugate antibody Diluent,1 bottle Streptavidin-HRP Diluent,1 bottle 20 x Wash Buffer Concentrate,1 bottle Substrate Solution,1 bottle Stop Solution,1 bottle Plate Cover Seals,4 pieces
Background	Matrix metalloproteinase-1 (MMP-1) also known as interstitial collagenase and fibroblast collagenase is an enzyme that in Sheeps is encoded by the MMP1 gene. MMP-1 has an archetypal structure consisting of a pre-domain, a pro-domain, a catalytic domain, a linker region and a hemopexinlike domain. The Catalytic Domains of MMPs share very similar characteristics, having a general shape of oblate ellipsoid with a diameter of ~40 Å. The Catalytic Domain of MMP-1 is composed of five highly twisted β-strands (sI-sV), three α-helix (hA-hC) and a total of eight loops, enclosing a total of five metal ions, three Ca2+ and two Zn2+, one of which with catalytic role. The Catalytic Domain (CAT) of MMP-1 starts with the F100 (non-truncated CAT) as the first amino-acid of the N-terminal loop of the CAT domain. A specific region (183)RWTNNFREY(191) has been identified as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. On C-terminal part of the CAT Domain the hB α-helix, known as the "active-site helix" encompasses part of the "zinc-binding consensus sequence" HEXXHXXGXXH that is characteristic of the Metzincin superfamily. The α-helix hB finishes abruptly at Gly225 where the last loop of the domain starts. This last loop contains the "specificity loop" which is the shortest in the MMPs family. The Catalytic Domain ends at Gly261 with α-helix hC. MMPs are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Specifically, MMP-1 breaks down the interstitial collagens, types I, II, and III. Mechanical force may increase the expression of MMP1 in Sheep periodontal ligament cells. MMP1 has been shown to interact with CD49b.

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