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Merck
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Fontos dokumentumok

MAB1959

Sigma-Aldrich

Anti-Integrin β1 Antibody, clone P5D2

clone P5D2, Chemicon®, from mouse

Szinonimák:

CD29, MAB1959Z

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
P5D2, monoclonal
application:
ELISA
FACS
ICC
IHC
IP
faj reaktivitás:
human
technika/technikák:
ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
citations:
57

biológiai forrás

mouse

Minőségi szint

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

P5D2, monoclonal

faj reaktivitás

human

gyártó/kereskedő neve

Chemicon®

technika/technikák

ELISA: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

izotípus

IgG2bκ

UniProt elérési szám

kiszállítva

wet ice

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... ITGB1(3688)

Általános leírás

Integrin beta 1, also known as CD29, is a 130 kDa transmembrane glycoprotein that forms noncovalent complexes with various Integrin alpha subunits (including alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, and alpha 6) to form the functional receptors that bind to specific extracellular matrix proteins. Integrin receptors are involved in the regulation of a variety of important biological functions, including embryonic development, wound repair, hemostasis, and prevention of programmed cell death. They are also implicated in abnormal pathological states such as tumor directed angiogenesis, tumor cell growth, and metastasis. These heterodimeric receptors bridge the cytoplasmic actin cytoskeleton with proteins present in the extracellular matrix and/or on adjacent cells. Interactions between integrins and the extracellular matrix lead to activation of signal transduction pathways and regulation of gene expression.

Egyediség

Reacts with Human Integrin Beta 1.

Immunogén

Human keratinocytes derived from skin.

Alkalmazás

Immunoprecipitation: A representative lot of this antibody clone was used in immunoprecipitation.

Immunohistochemistry: A representative lot of this antibody clone was used in immunohistochemistry (acetone fixation, no paraffin embedding).

ELISA: A representative lot of this antibody was used in ELISA.

Immunocytochemistry: A representative lot of this antibody clone was used in immunocytochemistry (paraformaldehyde fixation at less than 4%).

Functional Activity Assay: A representative lot of this antibody clone was used in cell attachment assay of SV-HFO cells with a characteristic spread morphology. In the presence of function-blocking mAbs to β1 integrin (P5D2), the cells attached but no longer spread, and displayed a rounded morphology with many cytoplasmic projections (Iba, K. et al., 2000).
Anti-Integrin β1 Antibody, clone P5D2 detects level of Integrin β1 & has been published & validated for use in ELISA, FC, IC, IH & IP.
Research Category
Cell Structure
Research Sub Category
Integrins

Minőség

Flow Cytometry Analysis:
4 µg of the antibody was used to detect Integrin β1 in 1x10^6 A431 cells.
4 µg of the antibody was used to detect Integrin β1 in 1x10^6 HeLa cells.

Fizikai forma

Format: Purified
Protein A purified
Purified immunoglobulin in 0.02M PB, 0.25M NaCl, pH 7.6, 0.1% sodium azide.

Tárolás és stabilitás

Maintain for 1 year at 2–8°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Analízis megjegyzés

Control
Human tonsil, human skin tissue

A431 & HeLa Cells

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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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.

Dokumentumtár megtekintése

Saubhik Sengupta et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 17(11), 1570-1572 (2003-06-26)
We have reported previously that levels of lysophosphatidic acid (LPA) are elevated in the blood and ascites from patients with ovarian cancer. LPA stimulates proliferation of ovarian cancer cells and has been proposed as an autocrine growth factor. Here, we
Polo-like kinase 1 is involved in invasion through extracellular matrix.
Rizki, A; Mott, JD; Bissell, MJ
Cancer Research null
Elizabeth A Waterman et al.
Cancer research, 67(9), 4264-4270 (2007-05-08)
Laminin-332 (formerly laminin-5) and collagen VII are basement membrane proteins expressed at the invasive front of human squamous cell carcinoma (SCC) tumors. These proteins have protumorigenic properties, but whether laminin-332 and collagen VII promote SCC tumors by providing adhesion or
Blockade of tumor growth due to matrix metalloproteinase-9 inhibition is mediated by sequential activation of beta1-integrin, ERK, and NF-kappaB.
Bhoopathi, P; Chetty, C; Kunigal, S; Vanamala, SK; Rao, JS; Lakka, SS
The Journal of Biological Chemistry null
Hiroaki Kimura et al.
International journal of cancer, 131(9), 2027-2033 (2012-02-11)
Integrins play a role in tumor growth and metastasis. However, the effect of integrin inhibition has not been visualized on single cancer cells in vivo. In this study, we used a powerful subcellular in vivo imaging model to demonstrate how

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