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MMP-26 Polyclonal Antibody

Applications

  • WB
  • ELISA
  • IHC-P
  • IHC-F
  • IF(IHC-P)
  • IF(IHC-F)
  • IF(ICC)

Reactivity

  • Human
Overview
Catalog # bs-1377R
Product Name MMP-26 Polyclonal Antibody
Applications WB, ELISA, IHC-P, IHC-F, IF(IHC-P), IF(IHC-F), IF(ICC)
Reactivity Human
Specifications
Conjugation Unconjugated
Host Rabbit
Source KLH conjugated synthetic peptide derived from human MMP26 intermedial
Immunogen Range 185-261/261
Clonality Polyclonal
Isotype IgG
Concentration 1ug/ul
Purification Purified by Protein A.
Storage Buffer 0.01M TBS(pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage Condition Shipped at 4°C. Store at -20°C for one year. Avoid repeated freeze/thaw cycles.
Target
Gene ID 56547
Subcellular location Secreted
Synonyms MMP26_HUMAN; Endometase; Matrilysin 2; MMP26; Matrix Metalloproteinase 26; MMP 26.
Background Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.
Application Dilution
WB 1:300-5000
ELISA 1:500-1000
IHC-P 1:200-400
IHC-F 1:100-500
IF(IHC-P) 1:50-200
IF(IHC-F) 1:50-200
IF(ICC) 1:50-200