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The antibody against ADAMTS5 was raised in rabbit using the Synthetic peptide of Human ADAMTS5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
The antibody against ADAMTS5 was raised in rabbit using the Synthetic peptide of Human ADAMTS5 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
$299.00
| Cat.No | ADC-28787A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | ADAMTS5 |
| Target Synonyms | 5 (aggrecanase 2) antibody; A disintegrin-like and metalloprotease with thrombospondin type 1 motif | Form | Liquid |
| Species Reactivity | Human, Mouse, Rat | Isotype | IgG |
| Storage Buffer | 0.05% NaN3, 40% Glycerol., pH7.4 PBS | Purification Method | Antigen affinity purified |
| Conjugate | Non-conjugated | Application | ELISA, IHC, WB |
| Storage | Upon receipt |
| Immunogen Description | Synthetic peptide of Human ADAMTS5 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q9UNA0 |
Uniprot Id
Q9UNA0
Target Species
Human
Target Name
ADAMTS5
Target Full Name
A disintegrin and metalloproteinase with thrombospondin motifs 5
Target Function
Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. Participates in development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.
Target Subcellular Location
Secreted, extracellular space, extracellular matrix.
Target Tissue Specificity
Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.
Target Synonyms
A disintegrin and metalloproteinase with thrombospondin motifs 11; A disintegrin and metalloproteinase with thrombospondin motifs 5; A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 5; A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase 2); A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 5; A Disintigrin And Metalloproteinase with ThromboSpondin motif-5; ADAM metallopeptidase with thrombospondin type 1 motif 5; ADAM TS 11; ADAM TS 5; ADAM TS5; ADAM-TS 11; ADAM-TS 5; ADAM-TS5; ADAMTS 11; ADAMTS 5; ADAMTS-11; ADAMTS-5; ADAMTS11; ADAMTS11, formerly; Adamts5; ADMP 2; ADMP-2; ADMP2; Aggrecanase 2; Aggrecanase-2; ATS5_HUMAN; FLJ36738; Implantin; ThromboSpondin motif-5
Target Background
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme contains two C-terminal TS motifs and functions as an aggrecanase that cleaves aggrecan, a major proteoglycan of cartilage, and may mediate cartilage destruction in osteoarthritis.
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