MAB2000
Anti-Integrin β1 Antibody, clone HB1.1
clone HB1.1, Chemicon®, from mouse
Szinonimák:
CD29
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
HB1.1, monoclonal
application:
FACS
IHC
IP
WB
IHC
IP
WB
faj reaktivitás:
human, pig
technika/technikák:
flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
citations:
21
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
antitest forma
purified immunoglobulin
antitest terméktípus
primary antibodies
klón
HB1.1, monoclonal
faj reaktivitás
human, pig
gyártó/kereskedő neve
Chemicon®
technika/technikák
flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
izotípus
IgG1κ
alkalmasság
not suitable for activity/function inhibition
NCBI elérési szám
UniProt elérési szám
kiszállítva
wet ice
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... ITGB1(3688)
Egyediség
Reacts with beta-1 subunit of VLA integrins
Alkalmazás
Anti-Integrin β1 Antibody, clone HB1.1 detects level of Integrin β1 & has been published & validated for use in FC, IP, WB, IH.
Immunoprecipitation of VLA integrins from lysate of 10E6 cell equivalent requires 2 μg of MAB2000.
Flow cytometry: 10 μg/mL
Western blot
Immunohistochemistry in frozen tissue samples: 5 μg/mL
Induction of cell aggregation: 10 μg/mL. MAB2000 is a potent stimulator of cell aggregation tested in U937, Jurkat and human peripheral blood lymphocytes.
MAB2000 does not affect VLA integrin-mediated cell adhesion to matrix proteins.
Optimal working dilutions must be determined by end user.
Flow cytometry: 10 μg/mL
Western blot
Immunohistochemistry in frozen tissue samples: 5 μg/mL
Induction of cell aggregation: 10 μg/mL. MAB2000 is a potent stimulator of cell aggregation tested in U937, Jurkat and human peripheral blood lymphocytes.
MAB2000 does not affect VLA integrin-mediated cell adhesion to matrix proteins.
Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Integrins
Integrins
Kapcsolódás
Replaces: 04-1109
Fizikai forma
Format: Purified
Purified immunoglobulin from Protein A chromatography. Liquid in 0.02M PB pH 7.6, 0.25M NaCl with 0.1% sodium azide.
Tárolás és stabilitás
Maintain at 2-8°C for up to 6 months after date of receipt.
Egyéb megjegyzések
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Jogi információk
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Jogi nyilatkozat
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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javasolt
Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 2
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Phosphoinositide signaling regulates the exocyst complex and polarized integrin trafficking in directionally migrating cells.
Thapa, N; Sun, Y; Schramp, M; Choi, S; Ling, K; Anderson, RA
Developmental Cell null
Roland Thuenauer et al.
mBio, 11(2) (2020-03-12)
The opportunistic bacterium Pseudomonas aeruginosa produces the fucose-specific lectin LecB, which has been identified as a virulence factor. LecB has a tetrameric structure with four opposing binding sites and has been shown to act as a cross-linker. Here, we demonstrate
Wulin Aerbajinai et al.
The Journal of biological chemistry, 291(16), 8549-8564 (2016-02-21)
Monocyte migration requires the dynamic redistribution of integrins through a regulated endo-exocytosis cycle, but the complex molecular mechanisms underlying this process have not been fully elucidated. Glia maturation factor-γ (GMFG), a novel regulator of the Arp2/3 complex, has been shown
D Oguey et al.
Gene therapy, 7(15), 1292-1303 (2000-08-05)
We explored the possibility of using a genetic approach to inhibit integrin-mediated endothelial cell adhesion and survival. We constructed recombinant adenoviruses (Ads) expressing chimeric proteins consisting of the cytoplasmic and transmembrane domains of integrin beta1 (CH1), beta3 (CH3) or the
Sarah M Short et al.
The Journal of cell biology, 168(4), 643-653 (2005-02-18)
The anti-angiogenic effect of thrombospondin-1 has been shown to be mediated through binding of the type-1 repeat (TSR) domain to the CD36 transmembrane receptor. We now report that the TSR domain can inhibit VEGF-induced migration in human umbilical vein endothelial
Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.
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