MAB1948P
Anti-Heparan Sulfate Proteoglycan (Perlecan) Antibody, clone A7L6
clone A7L6, from rat
Synonym(s):
heparan sulfate proteoglycan 2, Schwartz-Jampel syndrome 1 (chondrodystrophic myotonia), endorepellin (domain V region), perlecan proteoglycan, heparan sulfate proteoglycan of basement membrane
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All Photos(2)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rat
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
A7L6, monoclonal
species reactivity
human
technique(s)
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... HSPG2(3339)
General description
Heparan sulfate proteoglycans (HSPGs) are found on cell surfaces and in the extracelluar matrix of all mammalian tissues, particularly in the core of the basement membrane. HSPGs found in the brain are dystroglycan, N-syndecan, glypican, and perlecan. The composition of HSPGs differs in the protein core, and is thought to determine the location of HSPG in the cell membrane (syndecan and glypican) and extracellular matrix (perlecan and dystroglycan). The postulated functions of HSPG include cell proliferation, differentiation, adhesion, migration, and morphogenesis.
Heparan Sulfate Proteoglycan antibodies, in tissues, react strongly and uniformly with basement membranes. Clone A7L6 recognizes domain IV of the core protein of the large heparan sulphate proteoglycan or perlecan. The reactivity is independent of the galactosaminoglycan moieties; therefore, the epitope is not sensitive to heparinase treatment.
Heparan Sulfate Proteoglycan antibodies, in tissues, react strongly and uniformly with basement membranes. Clone A7L6 recognizes domain IV of the core protein of the large heparan sulphate proteoglycan or perlecan. The reactivity is independent of the galactosaminoglycan moieties; therefore, the epitope is not sensitive to heparinase treatment.
Specificity
The antibody recognizes a high molecular weight core protein of Heparan Sulfate Proteoglycan (Perlecan). No cross reactivity to laminin, collagen IV, entactin/nidogen, or fibronectin (Horiguchi, 1989).
Immunogen
Epitope: HSPG core protein
Heparan Sulfate Proteoglycan from EHS mouse tumor
Application
Detect Heparan Sulfate Proteoglycan (Perlecan) using this Anti-Heparan Sulfate Proteoglycan (Perlecan) Antibody, clone A7L6 validated for use in IH, IC, WB & IP.
Immunohistochemistry Analysis: 1:100 dilution from a previous lot detected Heparan Sulfate Proteoglycan in large cell carcinoma tissue.
Western Blot Analysis: A previous lot was used in independent laboratories in WB. (Hagen, 1993; Brown, 1999).
Immunoprecipitation Analysis: A previous lot was used by an independent laboratory in IP. (Couchman, 1989).
Western Blot Analysis: A previous lot was used in independent laboratories in WB. (Hagen, 1993; Brown, 1999).
Immunoprecipitation Analysis: A previous lot was used by an independent laboratory in IP. (Couchman, 1989).
Research Category
Cell Structure
Cell Structure
Research Sub Category
ECM Proteins
ECM Proteins
Quality
Evaluated by Immunocytochemistry in HeLa and A431 cells.
Immunocytochemistry Analysis: 1:500 dilution of this antibody detected Heparan Sulfate Proteoglycan in HeLa and A431 cells.
Immunocytochemistry Analysis: 1:500 dilution of this antibody detected Heparan Sulfate Proteoglycan in HeLa and A431 cells.
Linkage
Replaces: MAB1948
Physical form
Format: Purified
Protein G Purified
Purified rat monoclonal IgG2aκ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
HeLa and A431 cells
HeLa and A431 cells
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Shu-Chun Chang et al.
Evidence-based complementary and alternative medicine : eCAM, 2013, 457971-457971 (2013-08-29)
We previously reported that the increased level of perlecan with altered glycosaminoglycan (GAG) substitution was present in the placenta with gestational diabetes mellitus (GDM) and in the trophoblasts cultured under hyperglycemic condition. Trophoblast is the first cell lineage to differentiate
Takahiro Maeba et al.
Acta medica Okayama, 73(2), 135-146 (2019-04-25)
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Janice L Walker et al.
Developmental dynamics : an official publication of the American Association of Anatomists, 237(11), 3128-3141 (2008-09-26)
The formation of acinar and ductal structures during epithelial tissue branching morphogenesis is not well understood. We report that in the mouse submandibular gland (SMG), acinar and ductal cell fates are determined early in embryonic morphogenesis with E-cadherin playing pivotal
C A Miqueloto et al.
Journal of anatomy, 211(1), 16-25 (2007-06-05)
The morphogenesis of tissues and organs requires dynamic changes in cells and in extracellular matrix components. It is known that various extracellular matrix molecules are of fundamental importance for gonad differentiation and growth. In the adult testis, the extracellular matrix
Shunichi Fukuda et al.
Stroke, 35(4), 998-1004 (2004-03-06)
Focal cerebral ischemia causes microvessel matrix degradation and generates proteases known to degrade this matrix. However, proof that the proteases generated do indeed degrade vascular matrix is lacking. Here we demonstrate that active proteases derived from ischemic tissue after middle
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