MMP23 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O75900 |
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Other Accession | NP_008914 |
Clone Names | 2090504 |
Gene ID | 8510 |
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Other Names | Matrix metalloproteinase-23, MMP-23, 3424-, Femalysin, MIFR-1, Matrix metalloproteinase-21, MMP-21, Matrix metalloproteinase-22, MMP-22, Matrix metalloproteinase-23, soluble form, MMP23A, MMP21 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP6204a was selected from the N-term region of human MMP23 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | MMP23B |
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Synonyms | MMP21, MMP22 |
Function | Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). |
Cellular Location | Endoplasmic reticulum membrane; Single-pass type II membrane protein. Membrane; Single-pass type II membrane protein. Note=A secreted form produced by proteolytic cleavage may also exist. |
Tissue Location | Predominantly expressed in ovary, testis and prostate. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Matrix Metalloproteases (MMPs) are zinc-dependent endopeptidases that break down the extracellular matrix, and thus play important roles in many physiological processes including embryonic development, wound healing, reproduction, tissue remodeling, arthritis, cancer and cardiovascular disease. Although most MMPs are secreted, the membrane-type MMPs (MT-MMPs) are anchored to the cell membrane by a transmembrane and intracytoplasmic domain. MMP activities are regulated at several levels, including cleavage of proenzyme forms and suppression via tissue inhibitors of metalloproteinases (TIMPs). Matrix Metalloproteinase 23, first identified in tumor cells, features a number of unqie properties among the MMPs: 1) cysteine array unique among the MMPs, 2) sublocalized expression of MMP23 to reproductive organs, 3) a furin cleavage site, 4) and is the sole MMP mapped to chromosome 1.
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