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Merck
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Key Documents

MAB1997

Sigma-Aldrich

Anti-Integrin β1 Antibody, clone MB1.2

clone MB1.2, Chemicon®, from rat

Szinonimák:

CD29 antigen, Fibronectin receptor subunit beta, Integrin VLA-4 subunit beta, fibronectin receptor beta subunit, integrin VLA-4 beta subunit, integrin beta 1, integrin beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biológiai forrás

rat

Minőségi szint

antitest forma

purified immunoglobulin

antitest terméktípus

primary antibodies

klón

MB1.2, monoclonal

faj reaktivitás

mouse, human

faj reaktivitás (homológia által előrejelzett)

rat

kiszerelés

antibody small pack of 25 μg

gyártó/kereskedő neve

Chemicon®

technika/technikák

flow cytometry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

izotípus

IgG2κ

NCBI elérési szám

UniProt elérési szám

kiszállítva

ambient

tárolási hőmérséklet

2-8°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... ITGB1(3688)

Általános leírás

Integrin beta-1 (UniProt P05556; also known as CD29, Glycoprotein Iia, GPIIA, Integrin VLA-4 subunit beta, Very late activation protein, beta polypeptide) is encoded by the ITGB1 (also known as FNRB, MDF2, MSK12, VLA-BETA, VLAB) gene (Gene ID 3688) in human. Integrin beta-1 is a 130 kDa transmembrane glycoprotein that interact with various integrin alpha subunits (including alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, and alpha 6) to form the functional receptor complexes that bind to specific extracellular matrix proteins. Integrin receptors regulate 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 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 the activation of signal transduction pathways and regulation of gene expression.

Egyediség

Reacts with β1 subunit of VLA (β1) integrins

Immunogen

Mouse Integrin beta-1, as per (Von Ballestrem, C.G., et al. (1996). Hybridoma. 15(2):125-132). Mouse Integrin beta-1, as per (Von Ballestrem, C.G., et al. (1996). Hybridoma. 15(2):125-132).

Alkalmazás

Anti-Integrin β1 Antibody, clone MB1.2 is an antibody against Integrin β1 for use in FC, IH, IP & WB.
Immunoprecipitation:
A previous lot of this anitbody was used to immunoprecipitate VLA (β1) integrins from lysate of 106 cell equivalent: 2 μg.

Flow cytometry:
A 10 μg/mL concentration of a previous lot was used in FC.

Immunohistochemistry in frozen tissue sections:
20 μg/mL from a previous lot was used. As a result of the wide tissue distribution of VLA (β1), binding of MAB1997 to diverse cell types is commonly observed.
Does not block VLA integrin mediated cell adhesion to matrix proteins. Activation of VLA (β1) integrin signaling properties by MAB1997 has not been characterized.

Western blot:
10 µg/mL. Effective for samples that have been SDS-denatured and heated. Not effective for reduced samples.

Optimal working dilutions must be determined by end user.

Minőség

Routinely evaluated by Western Blot on C2C12 lysate.

Western Blot Analysis:
1:1000 dilution of this lot detected integrin β1 on 10 μg of C2C12 lysate.

Cél megnevezése

~88 kDa (non-glycosylated) and ~130 kDa ( glycosylated).

Kapcsolódás

Replaces: 04-1109

Fizikai forma

Format: Purified
Purified rat monoclonal IgG2κ liquid in buffer containing 0.02 M phosphate buffer, pH 7.6, 0.25 M NaCl with 0.1% NaN3

Analízis megjegyzés

Control
Human OVCAR5 cell line whole cell lysate

C2C12 lysate.

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

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Tárolási osztály kódja

12 - Non 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.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

?Np63 knockout mice reveal its indispensable role as a master regulator of epithelial development and differentiation.
Romano, RA; Smalley, K; Magraw, C; Serna, VA; Kurita, T; Raghavan, S; Sinha, S
Development null
Dystroglycan does not contribute significantly to kidney development or function, in health or after injury.
Jarad, G; Pippin, JW; Shankland, SJ; Kreidberg, JA; Miner, JH
American Journal of Physiology: Renal Physiology null
Reversion of the Jun-induced oncogenic phenotype by enhanced synthesis of sialosyllactosylceramide (GM3 ganglioside).
Miura, Y; Kainuma, M; Jiang, H; Velasco, H; Vogt, PK; Hakomori, S
Proceedings of the National Academy of Sciences of the USA null
Won-Jing Wang et al.
The Journal of cell biology, 159(1), 169-179 (2002-10-09)
Death-associated protein kinase (DAP-kinase) is a calcium/calmodulin-dependent serine/threonine kinase, and participates in various apoptosis systems. However, its apoptosis-promoting mechanism is poorly understood. Here, we demonstrate that DAP-kinase suppresses integrin-mediated cell adhesion and signal transduction, whereas dominant-negative interference of this kinase
Olivier Destaing et al.
Molecular biology of the cell, 21(23), 4108-4119 (2010-10-12)
Invadosomes are adhesion structures involved in tissue invasion that are characterized by an intense actin polymerization-depolymerization associated with β1 and β3 integrins and coupled to extracellular matrix (ECM) degradation activity. We induced the formation of invadosomes by expressing the constitutive

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