Skip to Content
Merck
All Photos(5)

Key Documents

MAB16983Z

Sigma-Aldrich

Anti-Integrin α4 Antibody, clone P1H4, azide free

clone P1H4, Chemicon®, from mouse

Synonym(s):

CD49d, MAB16983

Sign Into View Organizational & Contract Pricing


About This Item

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

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

P1H4, monoclonal

species reactivity

human, primate

manufacturer/tradename

Chemicon®

technique(s)

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

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... ITGA4(3676)

Specificity

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.

Physical form

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

Analysis Note

Control
Widely expressed, Intestinal mucosa

Other Notes

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

Legal Information

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

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service