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Anti-Integrin α3 Antibody, clone P1B5, azide free

clone P1B5, Chemicon®, from mouse

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CD49c, MAB1952

biological source


Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies


P1B5, monoclonal

species reactivity





immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)



NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification


Gene Information

human ... ITGA3(3675)

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Anti-Integrin α3 Antibody serum, Chemicon®


Anti-Integrin α3 Antibody


P1B5, monoclonal




M-KID2, monoclonal


P1D6, monoclonal

antibody form

purified immunoglobulin

antibody form


antibody form

purified immunoglobulin

antibody form

purified antibody

biological source


biological source


biological source


biological source


species reactivity


species reactivity

porcine, rat, goat, canine, sheep, hamster, equine, pig, bovine, human, mouse, chicken, horse

species reactivity


species reactivity



immunocytochemistry: suitable, immunohistochemistry: suitable (paraffin)


ELISA: suitable, immunofluorescence: suitable, immunohistochemistry: suitable, immunoprecipitation (IP): suitable, radioimmunoassay: suitable, western blot: suitable


ELISA: suitable, immunocytochemistry: suitable, immunohistochemistry: suitable (paraffin), immunoprecipitation (IP): suitable, radioimmunoassay: suitable


immunohistochemistry: suitable

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General description

Integrins are a family of dimeric, transmembrane proteins that mediate cell-cell and extracellular matrix adhesion. Signals transduced by integrins play a role in many biological processes, including cell growth, differentiation, migration and apoptosis. The integrin family is composed of at least 15 alpha and 8 beta subunits that may form over twenty different alpha-beta non-covalently bound dimeric combinations on the cell surface. The alpha subunits all have some homology to each other, as do the beta subunits. Both of the subunits contribute to the binding of the ligand. Integrin alpha subunits contain seven weak sequence repeats in the N-terminal region, which may be important in ligand binding, and have been predicted to fold cooperatively into a single beta-propeller domain with seven beta-sheets. The alpha-3 subunit (CD49c) is highly concentrated in epithelial cells where it strongly adheres to Laminin-5 and Laminin-5 induced rapid adhesion can be blocked by antibodies against the alpha-3 integrin subunit. The alpha-3 subunit exists in two different splice variants, denoted as "A" and "B". The only difference that results from this differential splicing is a total change in the cytoplasmic domain, while the extracellular domain stays the same. Knock-out mice lacking this subunit show prenatal lethality and abnormalities in the kidneys.


Reacts with Human alpha3 integrin.


Anti-Integrin α3 Antibody, clone P1B5, azide free detects level of Integrin α3 & has been published & validated for use in IC, IH(P).
Research Category
Cell Structure
Research Sub Category
Suitable for use in attachment inhibition assays using fibroblasts, most epithelial cells, activated lymphocytes on laminin, collagen and fibronectin.

Immunohistochemistry on human tonsil

fresh frozen tissue

paraffin embedded tissue; protease digestion required:

Optimal working dilutions must be determined by end user.

Physical form

Format: Purified
Protein A Purified mouse immunoglobulin in 20 mM sodium phosphate, 250 mM NaCl, pH. 7.6, with no preservatives.
Protein A purified

Storage and Stability

Maintain at 2–8°C in undiluted aliquots for up to 6 months after date of receipt.

During shipment, small volumes of product will occasionally become entrapped in the seal of the product vial. For products with volumes of 200μL or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container′s cap.

Analysis Note

Human foetal foreskin fibroblasts (HFFF), neuroblastomas

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


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.

Storage Class

12 - Non Combustible Liquids




Not applicable


Not applicable

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Feng-Yi Ke et al.
Cancer science, 111(10), 3478-3492 (2020-07-11)
Ovarian cancer has a high recurrence rate after platinum-based chemotherapy. To improve the treatment of ovarian cancer and identify ovarian cancer-specific antibodies, we immunized mice with the human ovarian carcinoma cell line, SKOV-3, and generated hybridoma clones. Several rounds of
James Kenney et al.
PloS one, 16(7), e0254714-e0254714 (2021-07-17)
Integrin receptors for the extracellular matrix play critical roles at all stages of carcinogenesis, including tumor growth, tumor progression and metastasis. The laminin-binding integrin α3β1 is expressed in all epithelial tissues where it has important roles in cell survival, migration
Anna Valeria Samarelli et al.
The Journal of biological chemistry, 289(28), 19466-19476 (2014-05-27)
The synaptic protein Neuroligin 1 (NLGN1), a cell adhesion molecule, is critical for the formation and consolidation of synaptic connectivity and is involved in vascular development. The mechanism through which NLGN1 acts, especially in vascular cells, is unknown. Here, we
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Aspergillus fumigatus is an opportunistic fungal pathogen that invades pulmonary epithelial cells and vascular endothelial cells by inducing its own endocytosis, but the mechanism by which this process occurs is poorly understood. Here, we show that the thaumatin-like protein CalA
Integrins modulate fast excitatory transmission at hippocampal synapses.
Kramar, EA; Bernard, JA; Gall, CM; Lynch, G
The Journal of Biological Chemistry null

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