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Merck
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Key Documents

MAB16983Z

Sigma-Aldrich

Anti-Integrin α4 Antibody, clone P1H4, azide free

clone P1H4, Chemicon®, from mouse

Synonyme(s) :

CD49d, MAB16983

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

P1H4, monoclonal

Espèces réactives

human, primate

Fabricant/nom de marque

Chemicon®

Technique(s)

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

Isotype

IgG1

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ITGA4(3676)

Catégories apparentées

Spécificité

The involvement of integrins in vascular proliferation, adhesion, and wound repair and have been well-documented. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits Monoclonal antibody MAB16983Z was produced by immunization with human T lymphocytes. The antibody is reactive with integrin alpha-4 from primate and human species.

Application

Anti-Integrin α4 Antibody, clone P1H4, azide free is an antibody against Integrin α4 for use in ELISA, FC, IC, IH & IP.
Immunohistochemistry (preferred fixatives are acetone and alcohols)

Immunocytochemistry

Immunoprecipitation

FACS Analysis

ELISA

Radioimmunoassay

Biological Activity: MAB16983Z inhibits CS-1 and VCAM binding.

Optimal working dilutions must be determined by end user.

Forme physique

Format: Purified
Protein A Purified immunoglobulin in 0.01M PBS pH 7.1, 0.15M NaCl containing no preservatives.

Remarque sur l'analyse

Control
Widely expressed, Intestinal mucosa

Autres remarques

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

O Jung et al.
Oncogenesis, 5, e202-e202 (2016-03-02)
Multiple myeloma arises when malignant plasma cells invade and form multiple tumors in the bone marrow. High levels of heparanase (HPSE) correlate with poor prognosis in myeloma patients. A likely target of the enzyme is the heparan sulfate (HS) proteoglycan
Arti V Shinde et al.
Matrix biology : journal of the International Society for Matrix Biology, 41, 26-35 (2014-11-30)
Prompt deposition of fibronectin-rich extracellular matrix is a critical feature of normal development and the host-response to injury. Fibronectin isoforms that include the EDA and EDB domains are prominent in these fibronectin matrices. We now report using human dermal fibroblast
Neisseria gonorrhoeae-induced transactivation of EGFR enhances gonococcal invasion.
Swanson KV, Griffiss JM, Edwards VL, Stein DC, Song W.
Cellular Microbiology null
N Assa-Munt et al.
Biochemistry, 40(8), 2373-2378 (2001-05-01)
The Arg-Gly-Asp (RGD) sequence serves as the primary integrin recognition site in extracellular matrix proteins, and peptides containing this sequence can mimic the activities of the matrix proteins. Depending on the context of the RGD sequence, an RGD-containing peptide may
Neisseria meningitidis adhesin NadA targets beta1 integrins: functional similarity to Yersinia invasin.
Nagele, V; Heesemann, J; Schielke, S; Jimenez-Soto, LF; Kurzai, O; Ackermann, N
The Journal of Biological Chemistry null

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